|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
59-679 |
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: 1072.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 59 LTYSWYNLDVFGAVHQPGSsWKQLVNRVKGVFCNERhipaPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRS 138
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGS-WKQLVSRLRGCFCRER----PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 139 SKGVQISPStiRMLNGHPVDAKEMQARCAYVQQDDLFIGSLTAREHLIFQAMVRMPRHMTQKQKVQRVDQVIQDLSLGKC 218
Cdd:TIGR00955 76 PKGVKGSGS--VLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 219 QNTLIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFEL 298
Cdd:TIGR00955 154 ANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 299 FDKILLMAEGRVAFLGTPGEAVDFFSYIGATCPTNYNPADFYVQVLAVVPGREVESRERIAKICDNFAVGKVSREMEQNF 378
Cdd:TIGR00955 234 FDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENESRERIEKICDSFAVSDIGRDMLVNT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 379 QKLV-KSNGFGKEDEN--GYTYKASWFMQFRAVLWRSWLSVLKEPLLVKVRLLQTTMVAVLIGLIFLGQQLTQVGVMNIN 455
Cdd:TIGR00955 314 NLWSgKAGGLVKDSENmeGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 456 GAIFLFLTNMTFQNSFATITVFTTELPVFMRETRSRLYRCDTYFLGKTIAELPLFLVVPFLFTAIAYPLIGLRPGVDHFF 535
Cdd:TIGR00955 394 GALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 536 TALALVTLVANVSTSFGYLISCACSSTSMALSVGPPVIIPFLLFGGFFLNSGSVPAYFKWLSYLSWFRYANEGLLINQWA 615
Cdd:TIGR00955 474 TFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWS 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 616 DVKPGEitCTLSNTT--CPSSGEVILETLNFSASDLPFDFIGLALLIVGFRISAYIALTMRARRKE 679
Cdd:TIGR00955 554 DVDNIE--CTSANTTgpCPSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
101-671 |
5.78e-91 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 296.79 E-value: 5.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRsskgVQISPSTIRMLNGHPVDAKEMQARCAYVQQDDLFIGSLT 180
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGR----IQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 AREHLIFQAMVRMPRHMTQKQKVQRVDQVIQDLSLGKCQNTLIGvPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTS 260
Cdd:PLN03211 157 VRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIG-NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 261 GLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPGEAVDFFSYIGATCPTNYNPADFY 340
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 341 V-------QVLAVVPGREVESRERIAKICDNFAVGKV--SREMEQNFQKLVKSNGFGKEDENG---YTYKASWFMQFRAV 408
Cdd:PLN03211 316 LdlangvcQTDGVSEREKPNVKQSLVASYNTLLAPKVkaAIEMSHFPQANARFVGSASTKEHRssdRISISTWFNQFSIL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 409 LWRSwLSVLKEPLLVKVRLLQTTMVAVLIGLIFLGQQLTQvgVMNINGAIFLFLTNMTFQNSFATITVFTTELPVFMRET 488
Cdd:PLN03211 396 LQRS-LKERKHESFNTLRVFQVIAAALLAGLMWWHSDFRD--VQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKER 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 489 RSRLYRCDTYFLGKTIAELPLFLVVPFLFTAIAYPLIGLRPGVDHFFTALALVTLVANVSTSFGYLISCACSSTSMALSV 568
Cdd:PLN03211 473 ASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTI 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 569 GPPVIIPFLLFGGFFLNsgSVPAYFKWLSYLSWFRYANEgLLINqwadVKPGEITCTLSNTTCPSSGEVILETLNFSASD 648
Cdd:PLN03211 553 VTVTMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYR-LLIN----VQYGEGKRISSLLGCSLPHGSDRASCKFVEED 625
|
570 580
....*....|....*....|....*....
gi 577718259 649 L-----PFDFIG-LALLIVGFRISAYIAL 671
Cdd:PLN03211 626 VagqisPATSVSvLIFMFVGYRLLAYLAL 654
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
78-642 |
6.43e-86 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 294.71 E-value: 6.43e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 78 SWKQLvnrvkgvfCNERHIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGVqISpSTIRMLNGHPV 157
Cdd:TIGR00956 761 HWRNL--------TYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGV-IT-GGDRLVNGRPL 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 158 DAKeMQARCAYVQQDDLFIGSLTAREHLIFQAMVRMPRHMTQKQKVQRVDQVIQDLSLGKCQNTLIGVPGrvKGLSGGER 237
Cdd:TIGR00956 831 DSS-FQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPG--EGLNVEQR 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 238 KRLAFASEALTDPPLLI-CDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEG-RVAFLGT 315
Cdd:TIGR00956 908 KRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGD 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 316 PGEA----VDFFSYIGAT-CPTNYNPADFYVQVLAVVPGREVESreriakicDNFAVGKVSREMEQNFQKLVK-SNGFGK 389
Cdd:TIGR00956 988 LGENshtiINYFEKHGAPkCPEDANPAEWMLEVIGAAPGAHANQ--------DYHEVWRNSSEYQAVKNELDRlEAELSK 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 390 -----EDENGYTYKASWFMQFRAVLWRSWLSVLKEPLLVKVRLLQTTMVAVLIGLIFLGQQLTQVGVMNINGAIFLFLTN 464
Cdd:TIGR00956 1060 aeddnDPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQMFAVFMATVL 1139
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 465 MTFQNSFATITVFTTELPVFMRETRSRLYRCDTYFLGKTIAELPLFLVVPFLFTAIAYPLIGL-----RPGVDHFFTALA 539
Cdd:TIGR00956 1140 FNPLIQQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFywnasKTGQVHERGVLF 1219
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 540 --LVTLVANVSTSFGYLISCACSSTSMALSVGPPVIIPFLLFGGFFLNSGSVPAYFKWLSYLSWFRYANEGLLINQWADV 617
Cdd:TIGR00956 1220 wlLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADV 1299
|
570 580
....*....|....*....|....*..
gi 577718259 618 kpgEITC--TLSNTTCPSSGEVILETL 642
Cdd:TIGR00956 1300 ---PVTCkvKELLTFNPPSGQTCGEYM 1323
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
103-314 |
4.86e-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: 246.03 E-value: 4.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGvqispSTIR---MLNGHPVDAKEMQARCAYVQQDDLFIGSL 179
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGG-----GTTSgqiLFNGQPRKPDQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLIFQAMVRMPRHMTQKQKVQRVDqviqDLSLGKCQNTLIGVPgRVKGLSGGERKRLAFASEALTDPPLLICDEPT 259
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRKKRVE----DVLLRDLALTRIGGN-LVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 260 SGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLG 314
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
100-314 |
4.79e-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: 228.97 E-value: 4.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSsKGVQISPSTirMLNGHPVDAKEMQARCAYVQQDDLFIGSL 179
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR-TGLGVSGEV--LINGRPLDKRSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLIFQAmvrmprhmtqkqkvqrvdqviqdlslgkcqntligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPT 259
Cdd:cd03213 98 TVRETLMFAA--------------------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 260 SGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLG 314
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
93-617 |
5.55e-62 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 224.73 E-value: 5.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 93 ERHIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKG-----VQISpstirmlnGHPvDAKEMQARCA 167
Cdd:PLN03140 885 EQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiegdIRIS--------GFP-KKQETFARIS 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 168 -YVQQDDLFIGSLTAREHLIFQAMVRMPRHMTQKQKVQRVDQVIQDLSLGKCQNTLIGVPGrVKGLSGGERKRLAFASEA 246
Cdd:PLN03140 956 gYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPG-VTGLSTEQRKRLTIAVEL 1034
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 247 LTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAE-GRVAFLGTPG----EAVD 321
Cdd:PLN03140 1035 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLGrnshKIIE 1114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 322 FFSYIGAT--CPTNYNPADFYVqvlavvpgrEVESRERIAKICDNFAVGKVSREMEQNFQKLVKSNGF---GKEDENGYT 396
Cdd:PLN03140 1115 YFEAIPGVpkIKEKYNPATWML---------EVSSLAAEVKLGIDFAEHYKSSSLYQRNKALVKELSTpppGASDLYFAT 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 397 -YKASWFMQFRAVLWRSWLSVLKEPLLVKVRLLQTTMVAVLIGLIF--LGQQLTQVGVMN-INGAIFLFLTNMTFQNSFA 472
Cdd:PLN03140 1186 qYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFwkVGTKRSNANDLTmVIGAMYAAVLFVGINNCST 1265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 473 TITVFTTELPVFMRETRSRLYRCDTYFLGKTIAELPLFLVVPFLFTAIAYPLIGLRPGVDHFF-------------TALA 539
Cdd:PLN03140 1266 VQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFwfyfisffsflyfTYYG 1345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 540 LVTlvanVSTSFGYLISCACSSTSMALsvgppviipFLLFGGFFLNSGSVP---AYFKWLSYLSWFRYaneGLLINQWAD 616
Cdd:PLN03140 1346 MMT----VSLTPNQQVAAIFAAAFYGL---------FNLFSGFFIPRPKIPkwwVWYYWICPVAWTVY---GLIVSQYGD 1409
|
.
gi 577718259 617 V 617
Cdd:PLN03140 1410 V 1410
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
103-638 |
3.88e-59 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 216.13 E-value: 3.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSkGVQISPSTIRMLNGHPVD--AKEMQARCAYVQQDDLFIGSLT 180
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTD-GFHIGVEGVITYDGITPEeiKKHYRGDVVYNAETDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 AREHLIFQAMVRMPRH----MTQKQKVQRV-DQVIQDLSLGKCQNTLIGvPGRVKGLSGGERKRLAFAsEALTDPPLLIC 255
Cdd:TIGR00956 155 VGETLDFAARCKTPQNrpdgVSREEYAKHIaDVYMATYGLSHTRNTKVG-NDFVRGVSGGERKRVSIA-EASLGGAKIQC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 256 -DEPTSGLDSFMAHSVVQVLKKLSQKGK-TVILTIHQPSSELFELFDKILLMAEGRVAFLGTPGEAVDFFSYIGATCPTN 333
Cdd:TIGR00956 233 wDNATRGLDSATALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDR 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 334 YNPADFYVQVLA-----VVPGRE---VESRERIAKICDNFAVGK-VSREMEQNFQK--------LVKSNGFGKEDENGYT 396
Cdd:TIGR00956 313 QTTADFLTSLTSpaerqIKPGYEkkvPRTPQEFETYWRNSPEYAqLMKEIDEYLDRcsesdtkeAYRESHVAKQSKRTRP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 397 ---YKASWFMQFRAVLWRSWLSVLKEPLLVKVRLLQTTMVAVLIGLIFLGQQLTQVGVMNINGAIFL-FLTNMTfqNSFA 472
Cdd:TIGR00956 393 sspYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFaILFNAF--SSLL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 473 TITVFTTELPVFMRETRSRLYRCDTYFLGKTIAELPLFLVVPFLFTAIAYPLIGLRPGVDHFFTALALVTLVANVSTSFG 552
Cdd:TIGR00956 471 EIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLF 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 553 YLISCACSSTSMALSVGPPVIIPFLLFGGFFLNSGSVPAYFKWLSYLSWFRYANEGLLINQWADVK----------PGEI 622
Cdd:TIGR00956 551 RSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRfecsqyvpsgGGYD 630
|
570
....*....|....*.
gi 577718259 623 TCTLSNTTCPSSGEVI 638
Cdd:TIGR00956 631 NLGVTNKVCTVVGAEP 646
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
78-308 |
2.61e-50 |
|
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: 173.58 E-value: 2.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 78 SWKQLVNRVKgvfcnerhIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGVqISPStiRMLNGHPV 157
Cdd:cd03232 5 TWKNLNYTVP--------VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGV-ITGE--ILINGRPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 158 DaKEMQARCAYVQQDDLFIGSLTAREHLIFQAMVRmprhmtqkqkvqrvdqviqdlslgkcqntligvpgrvkGLSGGER 237
Cdd:cd03232 74 D-KNFQRSTGYVEQQDVHSPNLTVREALRFSALLR--------------------------------------GLSVEQR 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 238 KRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEG 308
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
408-612 |
5.08e-49 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 170.53 E-value: 5.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 408 VLWRSWLSVLKEPLLVKVRLLQTTMVAVLIGLIFlGQQLTQVGVMNINGAIFLFLTNMTFQNSFATITVFTTELPVFMRE 487
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLF-GNLGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 488 TRSRLYRCDTYFLGKTIAELPLFLVVPFLFTAIAYPLIGLRPGVDHFFTALALVTLVANVSTSFGYLISCACSSTSMALS 567
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 577718259 568 VGPPVIIPFLLFGGFFLNSGSVPAYFKWLSYLSWFRYANEGLLIN 612
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
100-318 |
5.75e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.40 E-value: 5.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPS--TIRmLNGHPV--DAKEMQARCAYVQQDDLF 175
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLL-----GL-LRPTsgEVR-VLGEDVarDPAEVRRRIGYVPQEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSLTAREHLIFQAMVRmprHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLIC 255
Cdd:COG1131 85 YPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADR------KVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
103-613 |
3.36e-44 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 171.18 E-value: 3.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGVQISPSTirMLNGHPVDAKEMQARCAYVQQDDLFIGSLTAR 182
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEI--TYNGYRLNEFVPRKTSAYISQNDVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 183 EHLIFQA--------------MVRMPRHM--------------TQKQKVQR---VDQVIQDLSLGKCQNTLIGvPGRVKG 231
Cdd:PLN03140 258 ETLDFSArcqgvgtrydllseLARREKDAgifpeaevdlfmkaTAMEGVKSsliTDYTLKILGLDICKDTIVG-DEMIRG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAfASEALTDP-PLLICDEPTSGLDSFMAHSVVQVLKKLSQKGK-TVILTIHQPSSELFELFDKILLMAEGR 309
Cdd:PLN03140 337 ISGGQKKRVT-TGEMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILLSEGQ 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 310 VAFLGTPGEAVDFFSYIGATCPTNYNPADFYVQVLAV-----------VPGREVESRErIAKICDNFAVG-KVSREMEQN 377
Cdd:PLN03140 416 IVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKkdqeqywadrnKPYRYISVSE-FAERFKSFHVGmQLENELSVP 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 378 FQklvKSNG------FGKedengytYKASWFMQFRAVLWRSWLSVLKEPLLVKVRLLQTTMVAVLIGLIFLGQQL----T 447
Cdd:PLN03140 495 FD---KSQShkaalvFSK-------YSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMhtrnE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 448 QVGVMNINGAIFLFLTNMTfqNSFATITVFTTELPVFMRETRSRLYRCDTYFLGKTIAELPLFLVVPFLFTAIAYPLIGL 527
Cdd:PLN03140 565 EDGALYIGALLFSMIINMF--NGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGF 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 528 RPGVDHFFTALALVTLVANVSTSFGYLISCACSSTSMALSVGPPVIIPFLLFGGFFLNSGSVPAYFKWLSYLSWFRYANE 607
Cdd:PLN03140 643 APEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFN 722
|
....*.
gi 577718259 608 GLLINQ 613
Cdd:PLN03140 723 ALAVNE 728
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
101-318 |
8.36e-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: 146.54 E-value: 8.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDAKEMQAR--CAYVQQDDLFI 176
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAglLKPDSG------SIL-IDGEDVRKEPREARrqIGVLPDERGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTAREHLIFQAMVRmprHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICD 256
Cdd:COG4555 87 DRLTVRENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDR------RVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 257 EPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
103-314 |
1.61e-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: 144.33 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGVqiSPSTIRMLNGHPvdAKEMQARC----AYVQQDDLFIGS 178
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNV--SVEGDIHYNGIP--YKEFAEKYpgeiIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTAREHLIFQAmvrmprhmtqkqkvqrvdqviqdlslgKCQNTLIgvpgrVKGLSGGERKRLAFAsEALTDPPLLIC-DE 257
Cdd:cd03233 98 LTVRETLDFAL---------------------------RCKGNEF-----VRGISGGERKRVSIA-EALVSRASVLCwDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 258 PTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPSSELFELFDKILLMAEGRVAFLG 314
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
99-318 |
9.83e-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: 136.87 E-value: 9.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIrMLNGHPV--DAKEMQARCAYVQQDDL 174
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTgeLRPTSG------TA-YINGYSIrtDRKAARQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLTAREHLIFQAMVrmpRHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLI 254
Cdd:cd03263 86 LFDELTVREHLRFYARL---KGLPKSEIKEEVELLLRVLGLTDKANK------RARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 255 CDEPTSGLDSFMAHSVVQVLKKLsQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSM-DEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
103-309 |
3.01e-35 |
|
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: 132.59 E-value: 3.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDA---KEMQARCAYVQQ--DDLF 175
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNglLGPTSG------EVL-VDGKDLTKlslKELRRKVGLVFQnpDDQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSlTAREHLIFqAMVRMprHMTQKQKVQRVDQVIQDLSLGKCQNTLIgvpgrvKGLSGGERKRLAFASEALTDPPLLIC 255
Cdd:cd03225 89 FGP-TVEEEVAF-GLENL--GLPEEEIEERVEEALELVGLEGLRDRSP------FTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGR 309
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
100-310 |
4.96e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 127.90 E-value: 4.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPS--TIRmLNGHPV--DAKEMQARCAYVQQDDLF 175
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL-----GL-LKPDsgEIK-VLGKDIkkEPEEVKRRIGYLPEEPSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSLTAREHLIfqamvrmprhmtqkqkvqrvdqviqdlslgkcqntligvpgrvkgLSGGERKRLAFASEALTDPPLLIC 255
Cdd:cd03230 85 YENLTVRENLK---------------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRV 310
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHIL-EEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
101-319 |
1.43e-33 |
|
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: 128.22 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDAKEMQA---RCAYVQQ--DD 173
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNglLKPTSG------EVL-VDGKDITKKNLRElrrKVGLVFQnpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFIGSlTAREHLIFqamvrMPRHM--TQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASeAL-TDP 250
Cdd:COG1122 87 QLFAP-TVEEDVAF-----GPENLglPREEIRERVEEALELVGLEHLADR------PPHELSGGQKQRVAIAG-VLaMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 251 PLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPGEA 319
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDL-DLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
100-321 |
1.26e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.36 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGvQISPS--TIRmLNGHPVDAKemQARCAYVQQDDLFIG 177
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIL-----G-LLPPTsgTVR-LFGKPPRRA--RRRIGYVPQRAEVDW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 S--LTAREhlifqaMVRMPR--HM------TQKQKvQRVDQVIQDLSLGKCQNTLIGvpgrvkGLSGGERKRLAFAsEAL 247
Cdd:COG1121 89 DfpITVRD------VVLMGRygRRglfrrpSRADR-EAVDEALERVGLEDLADRPIG------ELSGGQQQRVLLA-RAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 248 -TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFlGTPGEAVD 321
Cdd:COG1121 155 aQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDL-GAVREYFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
100-310 |
2.89e-32 |
|
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: 124.14 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAF--RSSKGvqispsTIRmLNGHPVDAKEMQARCA-------YVQ 170
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldRPTSG------EVR-VDGTDISKLSEKELAAfrrrhigFVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 171 QDDLFIGSLTAREHlifqamVRMPRHMTQKQKVQRVDQVIQDLslgkcqnTLIGVPGR----VKGLSGGERKRLAFAsEA 246
Cdd:cd03255 89 QSFNLLPDLTALEN------VELPLLLAGVPKKERRERAEELL-------ERVGLGDRlnhyPSELSGGQQQRVAIA-RA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 247 L-TDPPLLICDEPTSGLDSFMAHSVVQVLKKLS-QKGKTVILTIHQPssELFELFDKILLMAEGRV 310
Cdd:cd03255 155 LaNDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
101-318 |
3.80e-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: 124.54 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDA---KEMQA---RCAYV-QQ 171
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVglLRPDSG------EVL-IDGEDISGlseAELYRlrrRMGMLfQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DDLFiGSLTAREHLIFqaMVRMPRHMTqkqkvqrvDQVIQDLSLGKCQntLIGVPGRVK----GLSGGERKRLAFASEAL 247
Cdd:cd03261 86 GALF-DSLTVFENVAF--PLREHTRLS--------EEEIREIVLEKLE--AVGLRGAEDlypaELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 248 TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQ-KGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHD-LDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
101-318 |
5.83e-32 |
|
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: 124.32 E-value: 5.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDA------KEMQARCAYV-QQ 171
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIglLRPDSG------EIL-VDGQDITGlsekelYELRRRIGMLfQG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DDLFiGSLTAREHLIFQamVRMPRHMTQKQKVQRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFAsEAL-TDP 250
Cdd:COG1127 91 GALF-DSLTVFENVAFP--LREHTDLSEAEIRELVLEKLELVGLPGAADKM---PSE---LSGGMRKRVALA-RALaLDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 251 PLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEGTPEE 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
99-321 |
6.35e-32 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 124.39 E-value: 6.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPV---DAKEMQARCAYVQQDD 173
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAglLKPSSG------EVL-LDGRDLaslSRRELARRIAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFIGSLTAREhlifqaMVRMPRH-------MTQKQKVQRVDQVIQDLSLGKCQNTLIGvpgrvkGLSGGERKRLAFASeA 246
Cdd:COG1120 85 PAPFGLTVRE------LVALGRYphlglfgRPSAEDREAVEEALERTGLEHLADRPVD------ELSGGERQRVLIAR-A 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 247 LT-DPPLLICDEPTSGLDsfMAH--SVVQVLKKLSQ-KGKTVILTIHQPssEL-FELFDKILLMAEGRVAFLGTPGEAVD 321
Cdd:COG1120 152 LAqEPPLLLLDEPTSHLD--LAHqlEVLELLRRLAReRGRTVVMVLHDL--NLaARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
99-314 |
1.87e-31 |
|
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: 121.92 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGeLLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRMlNGHPV--DAKEMQARCAYVQQDDL 174
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILAtlTPPSSG------TIRI-DGQDVlkQPQKLRRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLTAREHLIFQAMVRmprHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLI 254
Cdd:cd03264 83 VYPNFTVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKK------KIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 255 CDEPTSGLDSFMAHSVVQVLKKLSqKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 314
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHI-VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
45-318 |
5.75e-31 |
|
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: 127.96 E-value: 5.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 45 GTLSPPSPALTADNLTYSWynldvfgavhqpgsswkqlvnrvkgvfcnerhiPAPRKHLLKNVSGVAYPGELLAVMGSSG 124
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRY---------------------------------PGAGRPVLDGLSLTLPPGERVAIVGPSG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 125 AGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPV---DAKEMQARCAYVQQD-DLFIGSL-----TAREHLIFQAMVRM 193
Cdd:COG4987 372 SGKSTLLALLLrfLDPQSG------SIT-LGGVDLrdlDEDDLRRRIAVVPQRpHLFDTTLrenlrLARPDATDEELWAA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 194 prhmtqkqkVQRV--DQVIQDLSLGkcQNTLIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVV 271
Cdd:COG4987 445 ---------LERVglGDWLAALPDG--LDTWLGEGGR--RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALL 511
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 577718259 272 QVLKKLSQkGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG4987 512 ADLLEALA-GRTVLLITHRLA--GLERMDRILVLEDGRIVEQGTHEE 555
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
100-314 |
7.42e-31 |
|
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: 120.33 E-value: 7.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGvQISPS--TIRMLnghPVDAKEMQARCAYVQQ----DD 173
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL-----G-LLKPTsgSIRVF---GKPLEKERKRIGYVPQrrsiDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFigSLTAREhliFQAMVRMP-----RHMTQKQKvQRVDQVIQDLSLGKCQNTLIGvpgrvkGLSGGERKRLAFASEALT 248
Cdd:cd03235 82 DF--PISVRD---VVLMGLYGhkglfRRLSKADK-AKVDEALERVGLSELADRQIG------ELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSeLFELFDKILLMAeGRVAFLG 314
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
99-309 |
8.64e-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: 118.12 E-value: 8.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPS-TIRmLNGHPV---DAKEMQARCAYVQQddl 174
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA-----GLLKPTSgEIL-IDGKDIaklPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 figsltarehlifqamvrmprhmtqkqkvqrvdqviqdlslgkcqntligvpgrvkgLSGGERKRLAFASEALTDPPLLI 254
Cdd:cd00267 81 ---------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 255 CDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGR 309
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
98-318 |
1.02e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 127.18 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 98 APRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGvQISPS--TIRmLNGHPV---DAKEMQARCAYV-QQ 171
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL-----G-FLPPYsgSIL-INGVDLsdlDPASWRRQIAWVpQN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DDLFIGSLtaREHLifqamvRMPRHMTQKQKVQRV------DQVIQDLSLGkcQNTLIGVPGRvkGLSGGERKRLAFASE 245
Cdd:COG4988 420 PYLFAGTI--RENL------RLGRPDASDEELEAAleaaglDEFVAALPDG--LDTPLGEGGR--GLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 246 ALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSqKGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLA--LLAQADRILVLDDGRIVEQGTHEE 557
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
103-309 |
2.07e-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: 118.74 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGvQISPS--TIRmLNGHPVDAK--EMQARCAYVQQDDLFIGS 178
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILA-----G-LLPPSagEVL-WNGEPIRDAreDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTAREHLIFQAMVRmPRHMTQkqkvQRVDQVIQDLSLGKCQNTLIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEP 258
Cdd:COG4133 90 LTVRENLRFWAALY-GLRADR----EAIDEALEAVGLAGLADLPVRQ------LSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577718259 259 TSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPsseLFELFDKILLMAEGR 309
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLGDFK 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
104-260 |
2.23e-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: 116.59 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGvQISPS--TIRmLNGHPVDAKEMQA---RCAYVQQDDLFIGS 178
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIA-----G-LLSPTegTIL-LDGQDLTDDERKSlrkEIGYVFQDPQLFPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTAREHLIFqamVRMPRHMTQKQKVQRVDQVIQDLSLGKCQNTLIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEP 258
Cdd:pfam00005 74 LTVRENLRL---GLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERP--GTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 577718259 259 TS 260
Cdd:pfam00005 149 TA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
102-310 |
5.45e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.22 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 102 HLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQiSPS--TIRmLNGHPV---DAKEMQA-RCAYV----QQ 171
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG-----GLD-RPTsgEVL-IDGQDIsslSERELARlRRRHIgfvfQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DDLfIGSLTAREHLifqAMVRMPRHMTQKQKVQRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFAsEAL-TDP 250
Cdd:COG1136 95 FNL-LPELTALENV---ALPLLLAGVSRKERRERARELLERVGLGDRLDHR---PSQ---LSGGQQQRVAIA-RALvNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 251 PLLICDEPTSGLDSFMAHSVVQVLKKLS-QKGKTVILTIHQPssELFELFDKILLMAEGRV 310
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDGRI 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
101-309 |
9.75e-28 |
|
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: 109.78 E-value: 9.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPV---DAKEMQARCAYVQQDD-L 174
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLrlYDPTSG------EIL-IDGVDLrdlDLESLRKNIAYVPQDPfL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLtaREHLifqamvrmprhmtqkqkvqrvdqviqdlslgkcqntligvpgrvkgLSGGERKRLAFASEALTDPPLLI 254
Cdd:cd03228 88 FSGTI--RENI----------------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 255 CDEPTSGLDSFMAHSVVQVLKKLSqKGKTVILTIHQPSSelFELFDKILLMAEGR 309
Cdd:cd03228 120 LDEATSALDPETEALILEALRALA-KGKTVIVIAHRLST--IRDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
97-318 |
1.33e-27 |
|
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: 118.78 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 97 PAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHP---VDAKEMQARCAYVQQ 171
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLglYEPTSG------RIL-IDGIDlrqIDPASLRRQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DD-LFIGSLtaREHLIFQAmvrmpRHMTQKQkVQR------VDQVIQDLSLGKcqNTLIGVPGRvkGLSGGERKRLAFAS 244
Cdd:COG2274 557 DVfLFSGTI--RENITLGD-----PDATDEE-IIEaarlagLHDFIEALPMGY--DTVVGEGGS--NLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 245 EALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQkGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS--TIRLADRIIVLDKGRIVEDGTHEE 695
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
103-310 |
1.30e-26 |
|
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: 107.73 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRMlNGHPVDAKEMQARCAYVQQD-DLFIGSL 179
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAglIKESSG------SILL-NGKPIKAKERRKSIGYVMQDvDYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLIFQAMvRMPRhmtqkqKVQRVDQVIQDLSLG--KCQNTLIgvpgrvkgLSGGERKRLAFASEALTDPPLLICDE 257
Cdd:cd03226 88 SVREELLLGLK-ELDA------GNEQAETVLKDLDLYalKERHPLS--------LSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577718259 258 PTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPssE-LFELFDKILLMAEGRV 310
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDY--EfLAKVCDRVLLLANGAI 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
95-310 |
1.81e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.59 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 95 HIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FrsskgvqISPS--TIRmLNGHPVDAKEMQA---RCAY 168
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAdL-------DPPTsgEIY-LDGKPLSAMPPPEwrrQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 169 VQQD-DLFIGslTAREHLIFQAMVRmprhmTQKQKVQRVDQVIQDLSLGkcqntligvPG----RVKGLSGGERKRLAFA 243
Cdd:COG4619 79 VPQEpALWGG--TVRDNLPFPFQLR-----ERKFDRERALELLERLGLP---------PDildkPVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 244 SEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLS-QKGKTVILTIHQPsSELFELFDKILLMAEGRV 310
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDP-EQIERVADRVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
85-318 |
4.09e-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: 107.27 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 85 RVKGVFCNERHipapRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGvQISPSTIRMLNGHPVDAKEM 162
Cdd:cd03256 2 EVENLSKTYPN----GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLngLVEPTSG-SVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 163 QARCAYVQQDDLFIGSLTARE---------HLIFQAMVRM-PRHMTQK--QKVQRVDqvIQDLSLGKCQNtligvpgrvk 230
Cdd:cd03256 77 RRQIGMIFQQFNLIERLSVLEnvlsgrlgrRSTWRSLFGLfPKEEKQRalAALERVG--LLDKAYQRADQ---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 231 gLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKL-SQKGKTVILTIHQPssELF-ELFDKILLMAEG 308
Cdd:cd03256 145 -LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQV--DLArEYADRIVGLKDG 221
|
250
....*....|
gi 577718259 309 RVAFLGTPGE 318
Cdd:cd03256 222 RIVFDGPPAE 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
101-309 |
7.06e-26 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 104.58 E-value: 7.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvQISpstirmLNGHPVDAKEMQARcayvqqddlfigs 178
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAglEEPDSG-SIL------IDGEDLTDLEDELP------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 lTAREH--LIFQAMVRMPrHMTqkqkvqrvdqVIQDLSLGkcqntligvpgrvkgLSGGERKRLAFASEALTDPPLLICD 256
Cdd:cd03229 73 -PLRRRigMVFQDFALFP-HLT----------VLENIALG---------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577718259 257 EPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGR 309
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
104-318 |
7.30e-26 |
|
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: 105.91 E-value: 7.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTllnaiafrsskgvqispsTIRML-------------NGHPV--DAKEMQARCAY 168
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTT------------------TIKMLttllkptsgratvAGHDVvrEPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 169 VQQDDLFIGSLTAREHLIFQAMVR-MPRhmtqKQKVQRVDQVIQDLSLGKCQNTLigvpgrVKGLSGGERKRLAFASEAL 247
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYgVPG----AERRERIDELLDFVGLLEAADRL------VKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 248 TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHY-MEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
113-314 |
1.59e-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: 105.07 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVDAKEM-------QARCAYV-QQDDLFiGSLTAREH 184
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIA-----GLEKPDGGTIVLNGTVLFDSRKkinlppqQRKIGLVfQQYALF-PHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 185 LIFQamvrMPRHmTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 264
Cdd:cd03297 96 LAFG----LKRK-RNREDRISVDELLDLLGLDHLLNR------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577718259 265 FMAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLG 314
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 ... |
99-314 |
2.03e-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: 103.67 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIrMLNGHPV---DAKEMQARCAYVQQdd 173
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAglLKPSSG------EI-LLDGKDLaslSPKELARKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 lfigsltarehlifqAMvrmprhmtqkqkvQRVDqvIQDLSlGKCQNTLigvpgrvkglSGGERKRLAFASeALT-DPPL 252
Cdd:cd03214 81 ---------------AL-------------ELLG--LAHLA-DRPFNEL----------SGGERQRVLLAR-ALAqEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 253 LICDEPTSGLDSFMAHSVVQVLKKLS-QKGKTVILTIHQPSSELfELFDKILLMAEGRVAFLG 314
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAA-RYADRVILLKDGRIVAQG 180
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
99-318 |
2.97e-25 |
|
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: 104.61 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvQIspsTIRMLNGHPVDAKEMQARCAYVQQDD-LF 175
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMrfYDPQKG-QI---LIDGIDIRDISRKSLRSMIGVVLQDTfLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSLtaREHLifqamvRMPRHMTQKQKVQRVDQVIQ--DL--SLGKCQNTLIGVPGrvKGLSGGERKRLAFASEALTDPP 251
Cdd:cd03254 90 SGTI--MENI------RLGRPNATDEEVIEAAKEAGahDFimKLPNGYDTVLGENG--GNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 252 LLICDEPTSGLDSFMAHSVVQVLKKLsQKGKTVILTIHQPSSELFElfDKILLMAEGRVAFLGTPGE 318
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEGTHDE 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
97-353 |
6.46e-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: 6.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 97 PAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDA------KEMQARCAY 168
Cdd:COG1123 274 GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLglLRPTSG------SIL-FDGKDLTKlsrrslRELRRRVQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 169 VQQD--DLFIGSLTAREHLIFQAMVRmpRHMTQKQKVQRVDQVIQdlslgkcqntLIGVPGRVKG-----LSGGERKRLA 241
Cdd:COG1123 347 VFQDpySSLNPRMTVGDIIAEPLRLH--GLLSRAERRERVAELLE----------RVGLPPDLADrypheLSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 242 FASeAL-TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGEa 319
Cdd:COG1123 415 IAR-ALaLEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHD-LAVVRYIADRVAVMYDGRIVEDGPTEE- 491
|
250 260 270
....*....|....*....|....*....|....*
gi 577718259 320 vdFFSyigatcptnyNPADFYVQVL-AVVPGREVE 353
Cdd:COG1123 492 --VFA----------NPQHPYTRALlAAVPSLDPA 514
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
96-314 |
6.86e-25 |
|
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: 103.22 E-value: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 96 IPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGVqispSTIRMLNGHPvDAKEMQARCAYVQQDD 173
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAglLEPDAGF----ATVDGFDVVK-EPAEARRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFIGSLTAREHLI-FQAMVRMPRHmtqkQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPL 252
Cdd:cd03266 88 GLYDRLTARENLEyFAGLYGLKGD----ELTARLEELADRLGMEELLDR------RVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 253 LICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 314
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
102-318 |
1.27e-24 |
|
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: 102.51 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 102 HLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDAKEMQARC----AYVQQDDLF 175
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMglLPPRSG------SIR-FDGRDITGLPPHERAragiGYVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSLTAREHLifqamvRMPRHMTQKQKVQRVDQVIQDL--SLGKCQNTLIGVpgrvkgLSGGERKRLAFASEALTDPPLL 253
Cdd:cd03224 87 FPELTVEENL------LLGAYARRRAKRKARLERVYELfpRLKERRKQLAGT------LSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 254 ICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILtIHQPSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILL-VEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
97-318 |
2.33e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 107.30 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 97 PAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGVQISpSTIRmLNGHPV---DAKEMQARCAYVQQD- 172
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVL-LDGRDLlelSEALRGRRIGMVFQDp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 173 DLFIGSLTAREHLIFQAMVRMprhMTQKQKVQRVDQVIQdlslgkcqntLIGVPGRVK----GLSGGERKRLAFASEALT 248
Cdd:COG1123 93 MTQLNPVTVGDQIAEALENLG---LSRAEARARVLELLE----------AVGLERRLDryphQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
101-318 |
2.81e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 102.47 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGV--QISPSTIRMLnGHP---VDAKEMQARCAYVQQD--D 173
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLIT-----GDlpPTYGNDVRLF-GERrggEDVWELRKRIGLVSPAlqL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFIGSLTAREHLI--FQAMVRMPRHMTQKQKvQRVDQVIQDLSLGKCQNTLIGvpgrvkGLSGGERKRLAFAsEAL-TDP 250
Cdd:COG1119 90 RFPRDETVLDVVLsgFFDSIGLYREPTDEQR-ERARELLELLGLAHLADRPFG------TLSQGEQRRVLIA-RALvKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 251 PLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTI-HQPsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVtHHV-EEIPPGITHVLLLKDGRVVAAGPKEE 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
99-318 |
3.39e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.17 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPV---DAKEMQARCAYVQQDD 173
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrfYDPTSG------RIL-IDGVDIrdlTLESLRRQIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 -LF---------IGSLTAREHLIFQAMvrmprhmtqkqKVQRVDQVIQDLSLGkcQNTLIGVPGRvkGLSGGERKRLAFA 243
Cdd:COG1132 424 fLFsgtirenirYGRPDATDEEVEEAA-----------KAAQAHEFIEALPDG--YDTVVGERGV--NLSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 244 SEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSqKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLST--IRNADRILVLDDGRIVEQGTHEE 560
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
104-318 |
3.74e-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: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGvqispsTIRmLNGHPVDAKEMQARCAY-----VQQDDLFi 176
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsgFLRPTSG------SVL-FDGEDITGLPPHEIARLgigrtFQIPRLF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTAREHLIFQAMVRMPRHM-------TQKQKVQRVDQVIQDLSLGKCQNTLIGvpgrvkGLSGGERKRLAFASeAL-T 248
Cdd:cd03219 88 PELTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAG------ELSYGQQRRLEIAR-ALaT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGTPGE 318
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
99-318 |
4.85e-24 |
|
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: 101.15 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIaFR----SSKGVQISPSTIRmlnghPVDAKEMQARCAYVQQDD- 173
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL-FRfydvSSGSILIDGQDIR-----EVTLDSLRRAIGVVPQDTv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LF---------IGSLTAREHLIFQAMvrmprhmtqkqKVQRVDQVIQDLSLGkcQNTLIGVPGrVKgLSGGERKRLAFAS 244
Cdd:cd03253 86 LFndtigynirYGRPDATDEEVIEAA-----------KAAQIHDKIMRFPDG--YDTIVGERG-LK-LSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 245 EALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSqKGKTVILTIHQPSSELFElfDKILLMAEGRVAFLGTPGE 318
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNA--DKIIVLKDGRIVERGTHEE 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
104-305 |
5.14e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.60 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FRSSKGVQISpstirmLNGHPV---DAKEMQARCAYV-QQDDLFIGS 178
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLgFVDPTEGSIA------VNGVPLadaDADSWRDQIAWVpQHPFLFAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LT---------AREHLIFQAmvrmprhmtqkqkVQRV--DQVIQDLSLGkcQNTLIGVPGRvkGLSGGERKRLAFASEAL 247
Cdd:TIGR02857 412 IAenirlarpdASDAEIREA-------------LERAglDEFVAALPQG--LDTPIGEGGA--GLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 248 TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQkGKTVILTIHQPssELFELFDKILLM 305
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL--ALAALADRIVVL 529
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
100-311 |
6.96e-24 |
|
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: 101.03 E-value: 6.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVS-GVAyPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPV---DAKEMQARCAYVQQDD 173
Cdd:COG1124 17 RVPVLKDVSlEVA-PGESFGLVGESGSGKSTLLRALAglERPWSG------EVT-FDGRPVtrrRRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LfiGSLTAReHLIFQAMVRMPRHMTQKQKVQRVDQVIQDLslgkcqntliGVPGRVKG-----LSGGERKRLAFASEALT 248
Cdd:COG1124 89 Y--ASLHPR-HTVDRILAEPLRIHGLPDREERIAELLEQV----------GLPPSFLDryphqLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTI-HQPSSELFeLFDKILLMAEGRVA 311
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVsHDLAVVAH-LCDRVAVMQNGRIV 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
101-310 |
8.08e-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: 99.98 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPS--TIRMLNGHPVDAKEMQARCAYVQQDDLFIGS 178
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL-----GL-IKPDsgEITFDGKSYQKNIEALRRIGALIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTAREHLIFQAMVRMPRHmtqkqkvQRVDQVIQDLSLGkcqntliGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDE 257
Cdd:cd03268 87 LTARENLRLLARLLGIRK-------KRIDEVLDVVGLK-------DSAKKkVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577718259 258 PTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRV 310
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHL-LSEIQKVADRIGIINKGKL 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
101-311 |
3.18e-23 |
|
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: 98.36 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvQISpstirmLNGHPVDAKEMQAR-CAYVQQDD-LFi 176
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAglERPDSG-EIL------IDGRDVTGVPPERRnIGMVFQDYaLF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTAREHLIFqAMVRmpRHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICD 256
Cdd:cd03259 85 PHLTVAENIAF-GLKL--RGVPKAEIRARVRELLELVGLEGLLNR------YPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 257 EPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVA 311
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElGITTIYVTHDQ-EEALALADRIAVMNEGRIV 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
97-318 |
3.71e-23 |
|
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: 104.06 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 97 PAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPS--TIRmLNGHPVDA--KEMQARC-AYVQQ 171
Cdd:COG4618 341 PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV-----GV-WPPTagSVR-LDGADLSQwdREELGRHiGYLPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 D-DLFIGSltarehlIFQAMVRMPRHMTQK-----QKVqRVDQVIQDLSLGkcQNTLIGVPGRvkGLSGGERKRLAFAsE 245
Cdd:COG4618 414 DvELFDGT-------IAENIARFGDADPEKvvaaaKLA-GVHEMILRLPDG--YDTRIGEGGA--RLSGGQRQRIGLA-R 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 246 AL-TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG4618 481 ALyGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
114-314 |
4.32e-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: 97.95 E-value: 4.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVDAKEMQAR--CAYVQQDDLFigsltarEHL-IFQ-- 188
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA-----GFETPQSGRVLINGVDVTAAPPADRpvSMLFQENNLF-------AHLtVEQnv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 189 AMVRMPR-HMTQKQKvQRVDQVIQDLSLgkcQNTLIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 267
Cdd:cd03298 92 GLGLSPGlKLTAEDR-QAIEVALARVGL---AGLEKRLPGE---LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 577718259 268 HSVVQVLKKL-SQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLG 314
Cdd:cd03298 165 AEMLDLVLDLhAETKMTVLMVTHQP-EDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
95-310 |
1.56e-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: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 95 HIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKG-VQISPSTIRMLngHPVDakeMQARCAYVQQ 171
Cdd:cd03245 11 SYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAglYKPTSGsVLLDGTDIRQL--DPAD---LRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 D-DLFIGSLtaREHLIFQAMVRMPRHMTQKQKVQRVDQVIQDLSLGkcQNTLIGVPGRvkGLSGGERKRLAFASEALTDP 250
Cdd:cd03245 86 DvTLFYGTL--RDNITLGAPLADDERILRAAELAGVTDFVNKHPNG--LDLQIGERGR--GLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 251 PLLICDEPTSGLDSFMAHSVVQVLKKLSqKGKTVILTIHQPSseLFELFDKILLMAEGRV 310
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRI 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
103-310 |
1.59e-22 |
|
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: 94.98 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPV---DAKEMQARCAYVQQDD-LFI 176
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILglLRPTSG------RVR-LDGADIsqwDPNELGDHVGYLPQDDeLFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTarehlifqamvrmprhmtqkqkvqrvdqviqdlslgkcQNTLigvpgrvkglSGGERKRLAFASEALTDPPLLICD 256
Cdd:cd03246 90 GSIA--------------------------------------ENIL----------SGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577718259 257 EPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPssELFELFDKILLMAEGRV 310
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDGRV 173
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
100-319 |
1.72e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.53 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVD---AKEMQARCAyV--QQD 172
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgeLSPDSG------EVR-LNGRPLAdwsPAELARRRA-VlpQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 173 DL-FigSLTAREHLifqAMVRMPRHMTQKQKVQRVDQVIQ--DLSlgkcqntliGVPGR-VKGLSGGERKRLAFA----- 243
Cdd:PRK13548 86 SLsF--PFTVEEVV---AMGRAPHGLSRAEDDALVAAALAqvDLA---------HLAGRdYPQLSGGEQQRVQLArvlaq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 244 -SEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKL-SQKGKTVILTIHQPSseLFELF-DKILLMAEGRVAFLGTPGEA 319
Cdd:PRK13548 152 lWEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLN--LAARYaDRIVLLHQGRLVADGTPAEV 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
103-321 |
1.81e-22 |
|
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: 96.79 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIafrssKGVQISPSTIRMLNGHP---VDAKEMQARCAYVQQDD-LFIGS 178
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI-----QRFYVPENGRVLVDGHDlalADPAWLRRQVGVVLQENvLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LtaREHlIFQAMVRMPRH-MTQKQKVQRVDQVIQDLSLGkcQNTLIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDE 257
Cdd:cd03252 92 I--RDN-IALADPGMSMErVIEAAKLAGAHDFISELPEG--YDTIVGEQG--AGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 258 PTSGLDSFMAHSVVQVLKKLSqKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGTPGEAVD 321
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLST--VKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
104-318 |
1.93e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 97.03 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDAKEMQARCAY-----VQQDDLFi 176
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITgfYRPTSG------RIL-FDGRDITGLPPHRIARLgiartFQNPRLF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTAREHL-----------IFQAMVRMPRHMTQKQKV-QRVDQVIQDLSLGKCQNTLigvpgrVKGLSGGERKRLAFAS 244
Cdd:COG0411 92 PELTVLENVlvaaharlgrgLLAALLRLPRARREEREArERAEELLERVGLADRADEP------AGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 245 eAL-TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTihqpssE-----LFELFDKILLMAEGRVAFLGTPG 317
Cdd:COG0411 166 -ALaTEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLI------EhdmdlVMGLADRIVVLDFGRVIAEGTPA 238
|
.
gi 577718259 318 E 318
Cdd:COG0411 239 E 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
101-310 |
4.09e-22 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 94.90 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRsskgVQISPSTIRM----LNGHPVDAKEMQARCAYV-QQDDLF 175
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL----EEPDSGTIIIdglkLTDDKKNINELRQKVGMVfQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 iGSLTAREHLIFQAMVRmpRHMTQKQKVQRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPPLLIC 255
Cdd:cd03262 89 -PHLTVLENITLAPIKV--KGMSKAEAEERALELLEKVGLADKADAY---PAQ---LSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSselF--ELFDKILLMAEGRV 310
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMG---FarEVADRVIFMDDGRI 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
99-311 |
6.67e-22 |
|
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: 94.46 E-value: 6.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGvQISPS--TIRmLNGHPVdaKEMQARCAYVQQDDLFI 176
Cdd:cd03293 15 GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIA-----G-LERPTsgEVL-VDGEPV--TGPGPDRGYVFQQDALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTAREHLIFQA-MVRMPRhmtqKQKVQRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPPLLIC 255
Cdd:cd03293 86 PWLTVLDNVALGLeLQGVPK----AEARERAEELLELVGLSGFENAY---PHQ---LSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAE--GRVA 311
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWREtGKTVLLVTHD-IDEAVFLADRVVVLSArpGRIV 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
85-323 |
9.09e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.76 E-value: 9.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 85 RVKGVFCNERHIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPS--TIRMlNGhpvdakem 162
Cdd:COG1134 23 SLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA-----GI-LEPTsgRVEV-NG-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 163 qaRCAYVqqddL-----FIGSLTAREHLIFQAMVrmpRHMTQKQKVQRVDQVIqDLS-LGKcqntLIGVPgrVKGLSGGE 236
Cdd:COG1134 88 --RVSAL----LelgagFHPELTGRENIYLNGRL---LGLSRKEIDEKFDEIV-EFAeLGD----FIDQP--VKTYSSGM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 237 RKRLAFASEALTDPPLLICDEPTS-GLDSFMAHSvVQVLKKLSQKGKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGT 315
Cdd:COG1134 152 RARLAFAVATAVDPDILLVDEVLAvGDAAFQKKC-LARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDGD 229
|
....*...
gi 577718259 316 PGEAVDFF 323
Cdd:COG1134 230 PEEVIAAY 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
100-318 |
1.02e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 94.53 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPSTIRM-LNGHPVDAKEMQARC----AYVQQDDL 174
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIV-----GL-VKPDSGKIlLDGQDITKLPMHKRArlgiGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLTAREHLIfqAMVRMpRHMTQKQKVQRVDQVIQDLSLGKCQNTLIGvpgrvkGLSGGERKRLAFASEALTDPPLLI 254
Cdd:cd03218 86 IFRKLTVEENIL--AVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKAS------SLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 255 CDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN-VRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
100-314 |
1.12e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 93.88 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVDAkEMQARCAYVQQDDLFIGSL 179
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIL-----GIILPDSGEVLFDGKPLDI-AARNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLIFQAMVR-MPRHMTQKqkvqRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEP 258
Cdd:cd03269 86 KVIDQLVYLAQLKgLKKEEARR----RIDEWLERLELSEYANK------RVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 259 TSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 314
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
104-318 |
5.89e-21 |
|
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: 93.99 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTllnaiafrsskgvqispsTIRML-------------NGHPV--DAKEMQARCAY 168
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTT------------------TIRMLttllrptsgtarvAGYDVvrEPRKVRRSIGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 169 VQQDDLFIGSLTAREHL-IFQAMVRMPRhmtqKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEAL 247
Cdd:TIGR01188 71 VPQYASVDEDLTGRENLeMMGRLYGLPK----DEAEERAEELLELFELGEAADR------PVGTYSGGMRRRLDIAASLI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 248 TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:TIGR01188 141 HQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
104-318 |
6.69e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 91.65 E-value: 6.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGvQIspstirMLNGHPV---DAKEMQA---RCAYVQQDDLF 175
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLygEERPTSG-QV------LVNGQDLsrlKRREIPYlrrRIGVVFQDFRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSLTAREHLIFqAM--VRMPRHMTQKqkvqRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPPLL 253
Cdd:COG2884 91 LPDRTVYENVAL-PLrvTGKSRKEIRR----RVREVLDLVGLSDKAKAL---PHE---LSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 254 ICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPssELFELFDK-ILLMAEGRVAFLGTPGE 318
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDL--ELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
100-328 |
7.80e-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: 91.98 E-value: 7.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIafrsskGVQISPSTIRML-NGHPV---DAKEMQARCAYV-QQDDL 174
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI------NRLIEPTSGEIFiDGEDIreqDPVELRRKIGYViQQIGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FiGSLTAREHLifqAMVRMPRHMTQKQKVQRVDQVIQDLSLGkcqntligvPGRVKG-----LSGGERKRLAFASEALTD 249
Cdd:cd03295 87 F-PHMTVEENI---ALVPKLLKWPKEKIRERADELLALVGLD---------PAEFADrypheLSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 250 PPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE-----AVDFF 323
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHD-IDEAFRLADRIAIMKNGEIVQVGTPDEilrspANDFV 232
|
....*.
gi 577718259 324 -SYIGA 328
Cdd:cd03295 233 aEFVGA 238
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
102-318 |
9.15e-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: 91.87 E-value: 9.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 102 HLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAF--RSSKG-VQISPSTIRMLNGHpvDAKEMQARCAYV-QQDDLFiG 177
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGleRPTSGsVLVDGTDLTLLSGK--ELRKARRRIGMIfQHFNLL-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTAREHlifqamVRMP---RHMTQKQKVQRVDQVIQdlslgkcqntLIGVPGRVKG----LSGGERKRLAFASEALTDP 250
Cdd:cd03258 96 SRTVFEN------VALPleiAGVPKAEIEERVLELLE----------LVGLEDKADAypaqLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 251 PLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGTPGE 318
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
104-315 |
1.70e-20 |
|
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: 90.75 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIafrsSKGVQISPSTIRMlNGHPV---DAKEMQARCAYVQQDdLFIGSLT 180
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLI----PRFYDVDSGRILI-DGHDVrdyTLASLRRQIGLVSQD-VFLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 AREHLIFQAmvrmpRHMTQKQ-----KVQRVDQVIQDLSLGkcQNTLIGVPGrVKgLSGGERKRLAFASEALTDPPLLIC 255
Cdd:cd03251 92 VAENIAYGR-----PGATREEveeaaRAANAHEFIMELPEG--YDTVIGERG-VK-LSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKLsQKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGT 315
Cdd:cd03251 163 DEATSALDTESERLVQAALERL-MKNRTTFVIAHRLST--IENADRIVVLEDGKIVERGT 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
113-318 |
5.92e-20 |
|
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: 92.10 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PG-ELLAVMGSSGAGKTTLLNAIA-----------------FRSSKGVQISPStirmlnghpvdakemQARCAYVQQDDL 174
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAgltrpdegeivlngrtlFDSRKGIFLPPE---------------KRRIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLTAREHLIFQAMVRMPrhmtqKQKVQRVDQVIQDLSLGkcqNTLIGVPGRvkgLSGGERKRLAFASEALTDPPLLI 254
Cdd:TIGR02142 86 LFPHLSVRGNLRYGMKRARP-----SERRISFERVIELLGIG---HLLGRLPGR---LSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 255 CDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
100-263 |
6.34e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.69 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGVQISPStiRMLNGHPVDAKEMQAR-CAYVQQDDLFIGS 178
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGE--VLLNGRRLTALPAEQRrIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTAREHLIFQamvrMPRHMTQKQKVQRVDQVIQDLSLGkcqntliGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDE 257
Cdd:COG4136 91 LSVGENLAFA----LPPTIGRAQRRARVEQALEEAGLA-------GFADRdPATLSGGQRARVALLRALLAEPRALLLDE 159
|
....*.
gi 577718259 258 PTSGLD 263
Cdd:COG4136 160 PFSKLD 165
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
101-315 |
7.12e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.55 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLlnaiaFRSSKGVqISPS--TIRmLNGHPVDAKEMQArcayvqqddlfIG- 177
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTT-----IRIILGI-LAPDsgEVL-WDGEPLDPEDRRR-----------IGy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 ---------SLTAREHLIFQAMVRmprHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALT 248
Cdd:COG4152 76 lpeerglypKMKVGEQLVYLARLK---GLSKAEAKRRADEWLERLGLGDRANK------KVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQ-PSSElfELFDKILLMAEGRVAFLGT 315
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELVE--ELCDRIVIINKGRKVLSGS 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
97-314 |
7.63e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 87.37 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 97 PAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGvQIspstirMLNGHPVDAKEMQARCAyvqqddl 174
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtgDLKPQQG-EI------TLDGVPVSDLEKALSSL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 fIGSLTAREHLiFQAMVRmprhmtqkqkvqrvdqviqdlslgkcQNtlIGVPgrvkgLSGGERKRLAFASEALTDPPLLI 254
Cdd:cd03247 77 -ISVLNQRPYL-FDTTLR--------------------------NN--LGRR-----FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 255 CDEPTSGLDSFMAHSVVQVLKKLSqKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLG 314
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
102-318 |
7.65e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 88.89 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 102 HLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskG-VQISPSTIRmLNGHPVDAKEMQARC----AYVQQD-DLF 175
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAIS-----GlLPPRSGSIR-FDGEDITGLPPHRIArlgiGYVPEGrRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 iGSLTAREHLIfqaMVRMPRHMTQKQKvQRVDQVIqDL--SLGKCQNTLIGVpgrvkgLSGGERKRLAFASeAL-TDPPL 252
Cdd:COG0410 91 -PSLTVEENLL---LGAYARRDRAEVR-ADLERVY-ELfpRLKERRRQRAGT------LSGGEQQMLAIGR-ALmSRPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 253 LICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILtIHQPSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILL-VEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
100-310 |
1.54e-19 |
|
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: 87.95 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA---FRSS-----KGVQISPSTIRMLNGHpvdAKEMQarcaYVQQ 171
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILgllKPTSgsiifDGKDLLKLSRRLRKIR---RKEIQ----MVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DDlfIGSLTAR---EHLIFQAMVRmprHMTQKQKVQRVDQVIQDLSLgkcqntlIGVPGRVKG-----LSGGERKRLAFA 243
Cdd:cd03257 90 DP--MSSLNPRmtiGEQIAEPLRI---HGKLSKKEARKEAVLLLLVG-------VGLPEEVLNrypheLSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 244 SEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKL-SQKGKTVILTIHQPSSeLFELFDKILLMAEGRV 310
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGV-VAKIADRVAVMYAGKI 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
100-311 |
3.30e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.84 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDAKemQARCAYVQQDDlfig 177
Cdd:COG1116 23 GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAglEKPTSG------EVL-VDGKPVTGP--GPDRGVVFQEP---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SL----TAREHLIF-QAMVRMPRhmtqKQKVQRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFAsEAL-TDPP 251
Cdd:COG1116 90 ALlpwlTVLDNVALgLELRGVPK----AERRERARELLELVGLAGFEDAY---PHQ---LSGGMRQRVAIA-RALaNDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 252 LLICDEPTSGLDSFMAHSVVQVLKKL-SQKGKTVILTIHQPSSELFeLFDKILLMAE--GRVA 311
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVF-LADRVVVLSArpGRIV 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
85-314 |
3.61e-19 |
|
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: 86.82 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 85 RVKGVFCNERHIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPSTIRM-LNGHPVDAKEMQ 163
Cdd:cd03220 19 SLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLA-----GI-YPPDSGTVtVRGRVSSLLGLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 164 ARcayvqqddlFIGSLTAREHLIFQAMVrmpRHMTQKQKVQRVDQvIQDLS-LGKCQNTligvpgRVKGLSGGERKRLAF 242
Cdd:cd03220 93 GG---------FNPELTGRENIYLNGRL---LGLSRKEIDEKIDE-IIEFSeLGDFIDL------PVKTYSSGMKARLAF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 243 ASEALTDPPLLICDEPTSGLD-SFMAHSvVQVLKKLSQKGKTVILTIHQPSSeLFELFDKILLMAEGRVAFLG 314
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDaAFQEKC-QRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
103-290 |
6.80e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.95 E-value: 6.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAF--RSSKG-VQISPSTIRMlnghpVDAKEMQARCAYVQQddlfIGSL 179
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFleKPSEGsIVVNGQTINL-----VRDKDGQLKVADKNQ----LRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLIFQAMvRMPRHMTQKQKVqrVDQVIQDLSLGKCQN--------TLIGVPGRVKG-----LSGGERKRLAFASEA 246
Cdd:PRK10619 91 RTRLTMVFQHF-NLWSHMTVLENV--MEAPIQVLGLSKQEAreravkylAKVGIDERAQGkypvhLSGGQQQRVSIARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 577718259 247 LTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQ 290
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
104-318 |
6.81e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 88.62 E-value: 6.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FrsskgvqISPS--TIRmLNGHPVDAKEMQAR-CAYVQQDD-LFiGS 178
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgF-------ETPDsgRIL-LDGRDVTGLPPEKRnVGMVFQDYaLF-PH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTAREH----LifqamvRMpRHMTQKQKVQRVDQVIQdlslgkcqntLIGVPG----RVKGLSGGERKRLAFAsEAL-TD 249
Cdd:COG3842 92 LTVAENvafgL------RM-RGVPKAEIRARVAELLE----------LVGLEGladrYPHQLSGGQQQRVALA-RALaPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 250 PPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQ-EEALALADRIAVMNDGRIEQVGTPEE 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
100-310 |
9.34e-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: 84.41 E-value: 9.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDAKE----MQARCAYVQQDd 173
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFglRPPASG------EIT-LDGKPVTRRSprdaIRAGIAYVPED- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 lfigsltarehlifqamvrmpRHMtqkqkvqrvDQVIQDLSLGkcQNTLIGVpgrvkGLSGGERKRLAFASEALTDPPLL 253
Cdd:cd03215 84 ---------------------RKR---------EGLVLDLSVA--ENIALSS-----LLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 254 ICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRV 310
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLI----SSELDELLglcDRILVMYEGRI 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
107-321 |
1.09e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 107 VSGVAY---PGELLAVMGSSGAGKTTLLNAIAFRSSKGVqispSTIRMLnGHPV--DAKEMQARCAYVQQDDLFIGSLTA 181
Cdd:PRK13536 57 VNGLSFtvaSGECFGLLGPNGAGKSTIARMILGMTSPDA----GKITVL-GVPVpaRARLARARIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 182 REHLI-FQAMVRMprhmtqkqKVQRVDQVIQDL-SLGKCQNTligVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPT 259
Cdd:PRK13536 132 RENLLvFGRYFGM--------STREIEAVIPSLlEFARLESK---ADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 260 SGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGEAVD 321
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLARGKTILLTTHF-MEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
113-324 |
1.15e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.58 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIA-FRSSKGVQISpstirmLNGHPVDAKEMQARCAYV--QQDDLFiGSLTAREHLifqA 189
Cdd:COG3840 24 AGERVAILGPSGAGKSTLLNLIAgFLPPDSGRIL------WNGQDLTALPPAERPVSMlfQENNLF-PHLTVAQNI---G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 190 MVRMPR-HMTQKQKvQRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAH 268
Cdd:COG3840 94 LGLRPGlKLTAEQR-AQVEQALERVGLAGLLDRL---PGQ---LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 269 SVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFlgtPGEAVDFFS 324
Cdd:COG3840 167 EMLDLVDELCRErGLTVLMVTHDP-EDAARIADRVLLVADGRIAA---DGPTAALLD 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
114-297 |
1.27e-18 |
|
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: 85.15 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAIAFRsskgvqISPS--TIRmLNGHPVdAKEMQARCAY-------VQQDDLFIGSLTAREH 184
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLIYKE------ELPTsgTIR-VNGQDV-SDLRGRAIPYlrrkigvVFQDFRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 185 LIFqAM--VRMPRHMTQKqkvqRVDQVIQDLSLGKCQNTLigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 262
Cdd:cd03292 99 VAF-ALevTGVPPREIRK----RVPAALELVGLSHKHRAL------PAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190
....*....|....*....|....*....|....*
gi 577718259 263 DSFMAHSVVQVLKKLSQKGKTVILTIHqpSSELFE 297
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVVVATH--AKELVD 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
104-339 |
1.38e-18 |
|
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: 85.47 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPSTIR-MLNGhpVDAKEM---QARCAYVQQDDLFIGSL 179
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIA-----GF-IKPDSGKiLLNG--KDITNLppeKRDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLIFQamVRMpRHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPT 259
Cdd:cd03299 87 TVYKNIAYG--LKK-RKVDKKEIERKVLEIAEMLGIDHLLNR------KPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 260 SGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPGEAvdFFSyigatcPTNYNPADF 339
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV--FKK------PKNEFVAEF 229
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
103-309 |
2.18e-18 |
|
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: 84.06 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskgvqispSTIRMLNGHpvdaKEMQARCAYVQQDDlFIGSLTAR 182
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-----------GELEKLSGS----VSVPGSIAYVSQEP-WIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 183 EHLIFQAMVRMPRHmtqkQKVQRVDQVIQDLS-LGKCQNTLIGvpgrVKG--LSGGERKRLAFASEALTDPPLLICDEPT 259
Cdd:cd03250 84 ENILFGKPFDEERY----EKVIKACALEPDLEiLPDGDLTEIG----EKGinLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577718259 260 SGLDSFMAHSVVQ-VLKKLSQKGKTVILTIHQPssELFELFDKILLMAEGR 309
Cdd:cd03250 156 SAVDAHVGRHIFEnCILGLLLNNKTRILVTHQL--QLLPHADQIVVLDNGR 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
100-311 |
2.42e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.54 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGvqispsTIRmLNGHPVDAKE----MQARCAYVQQDD 173
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALfgADPADSG------EIR-LDGKPVRIRSprdaIRAGIAYVPEDR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 L---FIGSLTAREHLIFQAMVRMPRH--MTQKQKVQRVDQVIQDLSLgKCQNtlIGVPgrVKGLSGGERKRLAFASEALT 248
Cdd:COG1129 337 KgegLVLDLSIRENITLASLDRLSRGglLDRRRERALAEEYIKRLRI-KTPS--PEQP--VGNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 249 DPPLLICDEPTSGLDsfmahsvV-------QVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRVA 311
Cdd:COG1129 412 DPKVLILDEPTRGID-------VgakaeiyRLIRELAAEGKAVIVI----SSELPELLglsDRILVMREGRIV 473
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
94-291 |
3.08e-18 |
|
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: 88.57 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 94 RHIPAPRkhLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FRSSKGVQISpstirmLNGHPV---DAKEMQARCAYV 169
Cdd:TIGR02868 343 GYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAgLLDPLQGEVT------LDGVPVsslDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 170 QQD-DLFigSLTAREHLIF-------QAMVRMPRhmtqkqKVQRVDQvIQDLSLGkcQNTLIGVPGRVkgLSGGERKRLA 241
Cdd:TIGR02868 415 AQDaHLF--DTTVRENLRLarpdatdEELWAALE------RVGLADW-LRALPDG--LDTVLGEGGAR--LSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 577718259 242 FASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQkGKTVILTIHQP 291
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
97-311 |
5.16e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.53 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 97 PAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FrsskgvqISPSTIR-MLNGHPVDAKEmqARCAYVQQDDL 174
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAgF-------LAPSSGEiTLDGVPVTGPG--ADRGVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLTAREH----LIFQAMVRMPRHmtqkqkvQRVDQVIQdlslgkcqntLIGVPG----RVKGLSGGERKRLAFAsEA 246
Cdd:COG4525 87 LLPWLNVLDNvafgLRLRGVPKAERR-------ARAEELLA----------LVGLADfarrRIWQLSGGMRQRVGIA-RA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 247 LT-DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPSSELFeLFDKILLMA--EGRVA 311
Cdd:COG4525 149 LAaDPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALF-LATRLVVMSpgPGRIV 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
113-336 |
6.98e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 6.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLnaiafRSSKGVQISPSTIRMLNGHPVD--AKEMQARCAYVQQDDLFIGSLTAREHL-IFQA 189
Cdd:PRK13537 32 RGECFGLLGPNGAGKTTTL-----RMLLGLTHPDAGSISLCGEPVPsrARHARQRVGVVPQFDNLDPDFTVRENLlVFGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 190 MVRMPRHmtqkQKVQRVDQViqdLSLGKCQNTligVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHS 269
Cdd:PRK13537 107 YFGLSAA----AARALVPPL---LEFAKLENK---ADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 270 VVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGEAVDffSYIGATCPTNYNP 336
Cdd:PRK13537 177 MWERLRSLLARGKTILLTTHF-MEEAERLCDRLCVIEEGRKIAEGAPHALIE--SEIGCDVIEIYGP 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
104-328 |
7.72e-18 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 83.16 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQiSPSTIRM-LNGHPVDAKEMQAR-CAYVQQDDLFIGSLTA 181
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIA-----GLE-RPDSGTIlFGGEDATDVPVQERnVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 182 REHLIFQAMVRMPRHMTQKQKV-QRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTS 260
Cdd:cd03296 92 FDNVAFGLRVKPRSERPPEAEIrAKVHELLKLVQLDWLADRY---PAQ---LSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 261 GLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGEAVD------FFSYIGA 328
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDElHVTTVFVTHD-QEEALEVADRVVVMNKGRIEQVGTPDEVYDhpaspfVYSFLGE 239
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
103-318 |
9.03e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 9.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIafrssKGVqISPS--TIRmLNGHPV---DAKEMQARCAYVQQDDLFIG 177
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAI-----NGT-LTPTagTVL-VAGDDVealSARAASRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTARehlifqAMVRMPR--HMTQKQKVQRVDQVIQDLSLGKCQNTLIgVPGRVKGLSGGERKRLAFASEALTDPPLLIC 255
Cdd:PRK09536 91 EFDVR------QVVEMGRtpHRSRFDTWTETDRAAVERAMERTGVAQF-ADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHqpSSELFELF-DKILLMAEGRVAFLGTPGE 318
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADGRVRAAGPPAD 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
101-311 |
2.14e-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: 81.03 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSskGVQISPSTIRmLNGHPVDAKEMQARcayvqqddlfigslt 180
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHP--KYEVTEGEIL-FKGEDITDLPPEER--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 ARE--HLIFQAMVRMPrhmtqkqKVqRVDQVIQDLSlgkcqntligvpgrvKGLSGGERKRLAFASEALTDPPLLICDEP 258
Cdd:cd03217 75 ARLgiFLAFQYPPEIP-------GV-KNADFLRYVN---------------EGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 259 TSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPssELFELF--DKILLMAEGRVA 311
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSVLIITHYQ--RLLDYIkpDRVHVLYDGRIV 184
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
106-318 |
2.79e-17 |
|
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: 84.00 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 106 NVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHP-VDAKEMQA------RCAYVQQDD-LF 175
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAglERPDSG------RIR-LGGEVlQDSARGIFlpphrrRIGYVFQEArLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 iGSLTAREHLIFqAMVRMPRHMTQkqkvQRVDQVIQDLSLGkcqnTLIGvpGRVKGLSGGERKRLAFASEALTDPPLLIC 255
Cdd:COG4148 90 -PHLSVRGNLLY-GRKRAPRAERR----ISFDEVVELLGIG----HLLD--RRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTI-HQPsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVsHSL-DEVARLADHVVLLEQGRVVASGPLAE 220
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
100-320 |
3.11e-17 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 81.55 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTllnaiAFRSSKG-VQISPSTIRmLNGHPVDAKEMQARC----AYVQQDDL 174
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTT-----SFYMIVGlVRPDAGKIL-IDGQDITHLPMHERArlgiGYLPQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLTAREHLIfqAMVRMPRHMTQKQKVQRVDQVIQDLSLGKCQNTLIGvpgrvkGLSGGERKRLAFASEALTDPPLLI 254
Cdd:TIGR04406 87 IFRKLTVEENIM--AVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAM------SLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 255 CDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGEAV 320
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHN-VRETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
104-318 |
3.22e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.43 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTL---LNAIaFRSSKGVQispstirMLNGHPV--DAK---EMQARCAYVQQ---D 172
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLflhFNGI-LKPTSGEV-------LIKGEPIkyDKKsllEVRKTVGIVFQnpdD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 173 DLFigSLTAREHLIFQAM-VRMPRHMTQKqkvqRVDQVIQDLSLGKCQNTligVPGRvkgLSGGERKRLAFASEALTDPP 251
Cdd:PRK13639 90 QLF--APTVEEDVAFGPLnLGLSKEEVEK----RVKEALKAVGMEGFENK---PPHH---LSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 252 LLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpsSELFELF-DKILLMAEGRVAFLGTPGE 318
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEGTPKE 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
103-291 |
3.51e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDAKEMQARCAYVQQDDLFIGSLT 180
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAglLPPAAG------TIK-LDGGDIDDPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 AREHLIFQAMVRmprhmtqKQKVQRVDQVIQDLSLGKcqntLIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTS 260
Cdd:PRK13539 90 VAENLEFWAAFL-------GGEELDIAAALEAVGLAP----LAHLPFGY--LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 577718259 261 GLDSfmahSVVQVLKKLSQ----KGKTVILTIHQP 291
Cdd:PRK13539 157 ALDA----AAVALFAELIRahlaQGGIVIAATHIP 187
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
104-314 |
4.08e-17 |
|
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: 80.97 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVDAKEMQaRCAYVQQDDLFiGSLTARE 183
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLIS-----GLAQPTSGGVILEGKQITEPGPD-RMVVFQNYSLL-PWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 184 HlIFQAMVRMPRHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 263
Cdd:TIGR01184 74 N-IALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK------RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577718259 264 SFMAHSVVQVLKKLSQK-GKTVILTIHQPSSELFeLFDKILLMAEGRVAFLG 314
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALL-LSDRVVMLTNGPAANIG 197
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
102-310 |
4.18e-17 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 80.94 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 102 HLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDAKEMQARCA-------YVQQD 172
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAglDRPTSG------TVR-LAGQDLFALDEDARARlrarhvgFVFQS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 173 DLFIGSLTAREHlifqamVRMP------RHMTQK--QKVQRVdqviqdlslgkcqntliGVPGRV----KGLSGGERKRL 240
Cdd:COG4181 99 FQLLPTLTALEN------VMLPlelagrRDARARarALLERV-----------------GLGHRLdhypAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 241 AFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKL-SQKGKTVILTIHQPssELFELFDKILLMAEGRV 310
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDP--ALAARCDRVLRLRAGRL 224
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
104-311 |
4.60e-17 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 80.47 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVdAKEMQARCAYVQQDDL-FIGSLtar 182
Cdd:TIGR02211 21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLG-----GLDNPTSGEVLFNGQSL-SKLSSNERAKLRNKKLgFIYQF--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 183 EHLI--FQAM--VRMP---RHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLIC 255
Cdd:TIGR02211 92 HHLLpdFTALenVAMPlliGKKSVKEAKERAYEMLEKVGLEHRINH------RPSELSGGERQRVAIARALVNQPSLVLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKL-SQKGKTVILTIHQPssELFELFDKILLMAEGRVA 311
Cdd:TIGR02211 166 DEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDL--ELAKKLDRVLEMKDGQLF 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
103-288 |
6.49e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVDAKEMQARCAYVQQDDLFIGSLtar 182
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLG-----GLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 183 EHLI--FQAM--VRMPR---HMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLIC 255
Cdd:PRK11629 96 HHLLpdFTALenVAMPLligKKKPAEINSRALEMLAAVGLEHRANH------RPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190
....*....|....*....|....*....|...
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTI 288
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVV 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
113-321 |
9.47e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.14 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIafrsSKGVQISPSTIRM----LNGHPVDAKEMQARCAYV-QQDDLFiGSLTAREHLIF 187
Cdd:PRK09493 26 QGEVVVIIGPSGSGKSTLLRCI----NKLEEITSGDLIVdglkVNDPKVDERLIRQEAGMVfQQFYLF-PHLTALENVMF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 188 QamvrmPRHmTQKQKVQRVDQVIQDLsLGKcqntlIGVPGRV----KGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 263
Cdd:PRK09493 101 G-----PLR-VRGASKEEAEKQAREL-LAK-----VGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 264 SFMAHSVVQVLKKLSQKGKTVILTIHQPSselF--ELFDKILLMAEGRVAFLGTPGEAVD 321
Cdd:PRK09493 169 PELRHEVLKVMQDLAEEGMTMVIVTHEIG---FaeKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
104-341 |
9.48e-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: 80.77 E-value: 9.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLlnaiafrsskgvqispstIRMLNG--HPVDAKemqarcayVQQDDLFIGSLTA 181
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTL------------------LRCINRliEPTSGK--------VLIDGQDIAAMSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 182 RE---------HLIFQAMVRMPrHMT---------------QKQKVQRVDQVIQDLSLGKCQNTLIGvpgrvkGLSGGER 237
Cdd:cd03294 94 KElrelrrkkiSMVFQSFALLP-HRTvlenvafglevqgvpRAEREERAAEALELVGLEGWEHKYPD------ELSGGMQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 238 KRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTP 316
Cdd:cd03294 167 QRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDL-DEALRLGDRIAIMKDGRLVQVGTP 245
|
250 260
....*....|....*....|....*
gi 577718259 317 GEAVDffsyigatcptnyNPADFYV 341
Cdd:cd03294 246 EEILT-------------NPANDYV 257
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
104-289 |
1.23e-16 |
|
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: 78.62 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGVQispstirMLNGHPVD-----AKEMQARCAYVQQ---DD 173
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNglLRPQSGAV-------LIDGEPLDysrkgLLERRQRVGLVFQdpdDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFIGSltarehlIFQAMVRMPRHM--TQKQKVQRVDQVIQDLSLGKCQNTLIGVpgrvkgLSGGERKRLAFASEALTDPP 251
Cdd:TIGR01166 81 LFAAD-------VDQDVAFGPLNLglSEAEVERRVREALTAVGASGLRERPTHC------LSGGEKKRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 577718259 252 LLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIH 289
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
101-310 |
1.23e-16 |
|
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: 79.53 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--------FRSSKGVQISPSTIRMLNghpVDAKEMQARCAYV-QQ 171
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlndlipgAPDEGEVLLDGKDIYDLD---VDVLELRRRVGMVfQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DDLFIGSltarehlIFQAMVRMPRHMTQKQKVQRVDQVIQDLslgkcqnTLIGVPGRVK------GLSGGERKRLAFASE 245
Cdd:cd03260 90 PNPFPGS-------IYDNVAYGLRLHGIKLKEELDERVEEAL-------RKAALWDEVKdrlhalGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 246 ALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILT--IHQPSSelfeLFDKILLMAEGRV 310
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQAAR----VADRTAFLLNGRL 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
103-291 |
1.31e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.44 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVDAKEMQARCA-------YVQQDDLF 175
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILA-----GLDDGSSGEVSLVGQPLHQMDEEARAKlrakhvgFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSLTAREHLIFQAMVRmprHMTQKQKVQRVDQVIQDLSLGKcqnTLIGVPGRvkgLSGGERKRLAFASEALTDPPLLIC 255
Cdd:PRK10584 100 IPTLNALENVELPALLR---GESSRQSRNGAKALLEQLGLGK---RLDHLPAQ---LSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 577718259 256 DEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQP 291
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
102-315 |
1.52e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.34 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 102 HLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGvQIspstirMLNGHPVDA-KEMQAR---CAYVQQDDLF 175
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtrAWDPQQG-EI------LLNGQPIADySEAALRqaiSVVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSLtaREHLIFQAmvrmpRHMTQKQKVQRVDQVIQD--LSLGKCQNTLIGVPGRvkGLSGGERKRLAFASEALTDPPLL 253
Cdd:PRK11160 427 SATL--RDNLLLAA-----PNASDEALIEVLQQVGLEklLEDDKGLNAWLGEGGR--QLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 254 ICDEPTSGLDSFMAHSVVQVLKKLSQkGKTVILTIHQpsseLFEL--FDKILLMAEGRVAFLGT 315
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHR----LTGLeqFDRICVMDNGQIIEQGT 556
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
113-318 |
2.47e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 80.89 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDAKEMQAR-CAYV-QQDDLFiGSLTAREHLIFq 188
Cdd:COG3839 28 DGEFLVLLGPSGCGKSTLLRMIAglEDPTSG------EIL-IGGRDVTDLPPKDRnIAMVfQSYALY-PHMTVYENIAF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 189 AMvRMpRHMTQKQKVQRVDQV-----IQDLsLGKcqntligvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGL 262
Cdd:COG3839 99 PL-KL-RKVPKAEIDRRVREAaellgLEDL-LDR----------KPKQLSGGQRQRVALG-RALvREPKVFLLDEPLSNL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 263 DsfmAHSVVQV---LKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG3839 165 D---AKLRVEMraeIKRLHRRlGTTTIYVTHDQ-VEAMTLADRIAVMNDGRIQQVGTPEE 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
95-318 |
2.56e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.85 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 95 HIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLlnaiaFRSSKGVQISPSTIRMLNGHPVDAKEMQARCAYV----Q 170
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTL-----FRHFNGILKPTSGSVLIRGEPITKENIREVRKFVglvfQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 171 QDDLFIGSLTAREHLIFQamvrmPRHMTQKQKV--QRVDQVIQDLSLgkcQNTLIGVPGRvkgLSGGERKRLAFASEALT 248
Cdd:PRK13652 86 NPDDQIFSPTVEQDIAFG-----PINLGLDEETvaHRVSSALHMLGL---EELRDRVPHH---LSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ-LDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
104-310 |
2.66e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.36 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGvQISpstirmLNGHPVDAKEMQ----ARCAYVQQD----D 173
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLygALPRTSG-YVT------LDGHEVVTRSPQdglaNGIVYISEDrkrdG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFIG-------SLTAREHLIfQAMVRMpRHmtqKQKVQRVDQVIQDLSlgkcqntlIGVPGR---VKGLSGGERKRLAFA 243
Cdd:PRK10762 341 LVLGmsvkenmSLTALRYFS-RAGGSL-KH---ADEQQAVSDFIRLFN--------IKTPSMeqaIGLLSGGNQQKVAIA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 244 SEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRV 310
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILV----SSEMPEVLgmsDRILVMHEGRI 473
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
104-332 |
3.37e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTL---LNAIaFRSSKGVQISPStirMLNGHPVDAKEMQARCAYVQQ--DDLFIGS 178
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLalhLNGL-LRPQKGKVLVSG---IDTGDFSKLQGIRKLVGIVFQnpETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 lTAREHLIF--QAMVRMPRHMTQkqkvqRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICD 256
Cdd:PRK13644 94 -TVEEDLAFgpENLCLPPIEIRK-----RVDRALAEIGLEKYRHR------SPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 257 EPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHqpSSELFELFDKILLMAEGRVAFLGTPGEAVDFFS--YIGATCPT 332
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLSDVSlqTLGLTPPS 237
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
114-315 |
3.76e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.90 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAIAFRSSkGVQISPSTIRMLnGHPV--------DAKEMQARCAYVQQDDLFIGSLTAREHL 185
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLSGLIT-GDKSAGSHIELL-GRTVqregrlarDIRKSRANTGYIFQQFNLVNRLSVLENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 186 IFQAMVRMP------RHMTQKQKvQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPT 259
Cdd:PRK09984 108 LIGALGSTPfwrtcfSWFTREQK-QRALQALTRVGMVHFAHQ------RVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 260 SGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPSSELfELFDKILLMAEGRVAFLGT 315
Cdd:PRK09984 181 ASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDGS 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
99-310 |
6.62e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 77.51 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FRSSKGVQIspstirMLNGHPV---DAKEMQARCAYVQQDD- 173
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnFYQPQGGQV------LLDGKPIsqyEHKYLHSKVSLVGQEPv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFIGSLTARehlIFQAMVRMPRHM-TQKQKVQRVDQVIQDLSLGkcQNTLIGVPGRVkgLSGGERKRLAFASEALTDPPL 252
Cdd:cd03248 99 LFARSLQDN---IAYGLQSCSFECvKEAAQKAHAHSFISELASG--YDTEVGEKGSQ--LSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 253 LICDEPTSGLDSFMAHSVVQVLKKLSQKgKTVILTIHQPSseLFELFDKILLMAEGRV 310
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLS--TVERADQILVLDGGRI 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
104-311 |
9.17e-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: 75.16 E-value: 9.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPSTIRM-LNGHPVDakemqarcayvqqddlFIGSLTAR 182
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILS-----GL-YKPDSGEIlVDGKEVS----------------FASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 183 EHLIfqAMVrmprhmTQkqkvqrvdqviqdlslgkcqntligvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 262
Cdd:cd03216 74 RAGI--AMV------YQ--------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 577718259 263 DSFMAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVA 311
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVIFISHRL-DEVFEIADRVTVLRDGRVV 161
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
92-316 |
1.14e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.56 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 92 NERHIPAPRKH--LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGVQISPSTIR---MLNGHP---VDAKEMQ 163
Cdd:PRK13547 3 TADHLHVARRHraILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTgdvTLNGEPlaaIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 164 ARCAYVQQDDLFIGSLTAREHLIfqaMVRMPrHMTQKQKVQRVDQVIQDLSLGKC-QNTLIGvpGRVKGLSGGERKRLAF 242
Cdd:PRK13547 83 RLRAVLPQAAQPAFAFSAREIVL---LGRYP-HARRAGALTHRDGEIAWQALALAgATALVG--RDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 243 A---------SEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTI-HQPSSELfELFDKILLMAEGRVAF 312
Cdd:PRK13547 157 ArvlaqlwppHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAA-RHADRIAMLADGAIVA 235
|
....
gi 577718259 313 LGTP 316
Cdd:PRK13547 236 HGAP 239
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
101-318 |
1.22e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.36 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfRSSKGVQispSTIrMLNGHPV---DAKEMQARCAYVQQDDLFIG 177
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTPQS---GTV-FLGDKPIsmlSSRQLARRLALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTAREhLIfqAMVRMPR-----HMTQKQKvQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRlAFASEALT-DPP 251
Cdd:PRK11231 90 GITVRE-LV--AYGRSPWlslwgRLSAEDN-ARVNQAMEQTRINHLADR------RLTDLSGGQRQR-AFLAMVLAqDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 252 LLICDEPTSGLDsfMAHSV--VQVLKKLSQKGKTVILTIH---QPSselfELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK11231 159 VVLLDEPTTYLD--INHQVelMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
102-318 |
1.43e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.58 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 102 HLLKNVSGVAYPGELLAVMGSSGAGKTTLlnaiaFRSSKGVqISPSTIRML-NGHPVD--AK---EMQARCAYVQQD--- 172
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTL-----FQNLNGI-LKPSSGRILfDGKPIDysRKglmKLRESVGMVFQDpdn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 173 DLFigSLTAREHLIFQAM-VRMPRHMTQKqkvqRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPP 251
Cdd:PRK13636 94 QLF--SASVYQDVSFGAVnLKLPEDEVRK----RVDNALKRTGIEHLKDK------PTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 252 LLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHqpSSELFELF-DKILLMAEGRVAFLGTPGE 318
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATH--DIDIVPLYcDNVFVMKEGRVILQGNPKE 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
95-311 |
1.64e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.05 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 95 HIPA--PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FrsskgVQISPSTIRmLNGHPVDAKemQARCAYVQQ 171
Cdd:PRK11248 6 HLYAdyGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAgF-----VPYQHGSIT-LDGKPVEGP--GAERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DDLFIGSLTAREHLIF----QAMVRMPRHMTQKQKVQRVDqviqdlslgkcqntLIGVPGR-VKGLSGGERKRLAFASEA 246
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFglqlAGVEKMQRLEIAHQMLKKVG--------------LEGAEKRyIWQLSGGQRQRVGIARAL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 247 LTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQPSSELFELFDKILLM-AEGRVA 311
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSpGPGRVV 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
104-318 |
1.74e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 76.66 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSgVAYP-GELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPV---DAKEMQARCAYVQQDDLFIG 177
Cdd:COG4604 17 LDDVS-LTIPkGGITALIGPNGAGKSTLLSMISrlLPPDSG------EVL-VDGLDVattPSRELAKRLAILRQENHINS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTAREHLIFQamvRMPRH---MTQKQKvQRVDQVIQDLSLGKCQNTLIgvpgrvKGLSGGERKRlAFASEAL---TDPP 251
Cdd:COG4604 89 RLTVRELVAFG---RFPYSkgrLTAEDR-EIIDEAIAYLDLEDLADRYL------DELSGGQRQR-AFIAMVLaqdTDYV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 252 LLicDEPTSGLDsfMAHSV--VQVLKKLS-QKGKTVILTIHqpsselfEL-F-----DKILLMAEGRVAFLGTPGE 318
Cdd:COG4604 158 LL--DEPLNNLD--MKHSVqmMKLLRRLAdELGKTVVIVLH-------DInFascyaDHIVAMKDGRVVAQGTPEE 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
114-291 |
1.94e-15 |
|
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: 75.22 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVDAK--EMQARCAYVQQDDLFIGSLTAREHLIFQAmv 191
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILA-----GLSPPLAGRVLLNGGPLDFQrdSIARGLLYLGHAPGIKTTLSVLENLRFWH-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 192 rmPRHMTqkqkvqrvDQVIQDLSlgkcQNTLIGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSV 270
Cdd:cd03231 99 --ADHSD--------EQVEEALA----RVGLNGFEDRpVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|.
gi 577718259 271 VQVLKKLSQKGKTVILTIHQP 291
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQD 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
104-318 |
2.88e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.03 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FRSSKGvQIspstirMLNGHPVDAKEMQA---RCAYVQQDDLFIGSL 179
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAgLLPGQG-EI------LLNGRPLSDWSAAElarHRAYLSQQQSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLifqaMVRMPRHMTQKQKVQRVDQVIQDLSLGKcqntLIGVPgrVKGLSGGE--RKRLAFA-----SEALTDPPL 252
Cdd:COG4138 85 PVFQYL----ALHQPAGASSEAVEQLLAQLAEALGLED----KLSRP--LTQLSGGEwqRVRLAAVllqvwPTINPEGQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 253 LICDEPTSGLDsfMAHSVV--QVLKKLSQKGKTVILTIHQPSSELFELfDKILLMAEGRVAFLGTPGE 318
Cdd:COG4138 155 LLLDEPMNSLD--VAQQAAldRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASGETAE 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
101-314 |
4.52e-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: 74.60 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGV-QISPSTIRmLNGHPVDAKEMQAR-CAYVQQDDLFIGS 178
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIA-----GLeEPTSGRIY-IGGRDVTDLPPKDRdIAMVFQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTAREHLIFQamVRMpRHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEP 258
Cdd:cd03301 87 MTVYDNIAFG--LKL-RKVPKDEIDERVREVAELLQIEHLLDR------KPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 259 TSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 314
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHD-QVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
101-310 |
5.69e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.35 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAI-AFRSSKG-VQIspstirmlNGHP---VDAKEMQARCAYVQQD-DL 174
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlGFLPYQGsLKI--------NGIElreLDPESWRKHLSWVGQNpQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLtaREHlifqamVRMPRHMTQKQKVQR------VDQVIQDLSLGkcQNTLIGvpGRVKGLSGGERKRLAFASEALT 248
Cdd:PRK11174 435 PHGTL--RDN------VLLGNPDASDEQLQQalenawVSEFLPLLPQG--LDTPIG--DQAAGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQkGKTVILTIHQpsseLFEL--FDKILLMAEGRV 310
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQ----LEDLaqWDQIWVMQDGQI 561
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
113-291 |
6.72e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIA--FRSSKGvQISpstirmLNGHPVDAkemqARCAYvQQDDLFIG-------SLTARE 183
Cdd:PRK13538 26 AGELVQIEGPNGAGKTSLLRILAglARPDAG-EVL------WQGEPIRR----QRDEY-HQDLLYLGhqpgiktELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 184 HLIF-QAMvrmprhmtqkQKVQRVDQVIQdlSLGKcqntlIGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDEP 258
Cdd:PRK13538 94 NLRFyQRL----------HGPGDDEALWE--ALAQ-----VGLAGFedvpVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 577718259 259 TSGLDsfmAHSVVQVLKKLSQ---KGKTVILTIHQP 291
Cdd:PRK13538 157 FTAID---KQGVARLEALLAQhaeQGGMVILTTHQD 189
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
103-298 |
8.07e-15 |
|
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: 73.55 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPS-TIRMLNGHPVDAKEMQAR-CAYVQQDDLFIGSLT 180
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA-----GLLRPDSgEVRWNGTPLAEQRDEPHEnILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 AREHLIFQAMVRMPRHMTqkqkvqrVDQVIQDLSLGKCQNTLigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTS 260
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLP------AAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 577718259 261 GLDS-----FMAHsvvqvLKKLSQKGKTVILTIHQ--PSSELFEL 298
Cdd:TIGR01189 157 ALDKagvalLAGL-----LRAHLARGGIVLLTTHQdlGLVEAREL 196
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
101-318 |
1.47e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.77 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTT---LLNAIAFRSSKGVQISPSTIRMLnghPVDAKEMQArCAYVQQDDLFIG 177
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfyMVVGIVPRDAGNIIIDDEDISLL---PLHARARRG-IGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTAREHLIfqAMVRMPRHMTQKQKVQRVDQVIQDLSLGKCQNTLigvpgrVKGLSGGERKRLAFASEALTDPPLLICDE 257
Cdd:PRK10895 92 RLSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM------GQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 258 PTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN-VRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
104-314 |
1.49e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVD----AKEMQARCAYVQQDDLFIGSL 179
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIA-----GIVPPDSGTLEIGGNPCArltpAKAHQLGIYLVPQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLIFqamvRMPRHMTQKQKVQrvdQVIQDLSlgkCQNTLIGVPGrvkGLSGGERKRLAFASEALTDPPLLICDEPT 259
Cdd:PRK15439 102 SVKENILF----GLPKRQASMQKMK---QLLAALG---CQLDLDSSAG---SLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 260 SGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 314
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLAQGVGIVFISHK-LPEIRQLADRISVMRDGTIALSG 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
100-318 |
1.50e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.52 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvQIspstirMLNGHPVDAKEMQARC----AYVQQD- 172
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVglVKPDSG-RI------FLDGEDITHLPMHKRArlgiGYLPQEa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 173 DLFIGsLTAREHLifQAMVRMpRHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgrvKG--LSGGERKRLAFAsEAL-TD 249
Cdd:COG1137 88 SIFRK-LTVEDNI--LAVLEL-RKLSKKEREERLEELLEEFGITHLRKS--------KAysLSGGERRRVEIA-RALaTN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 250 PPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNV-RETLGICDRAYIISEGKVLAEGTPEE 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
101-318 |
1.52e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 74.26 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTT---LLNAIaFRSSKG-VQISPSTIRMLNghpvdAKEMQARCAYVQQ--DDL 174
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGL-LKPQSGeIKIDGITISKEN-----LKEIRKKIGIIFQnpDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSlTAREHLIFQAMVRM--PRHMtqKQKVQRVDQVIQDLSLGK--CQNtligvpgrvkgLSGGERKRLAFASEALTDP 250
Cdd:PRK13632 96 FIGA-TVEDDIAFGLENKKvpPKKM--KDIIDDLAKKVGMEDYLDkePQN-----------LSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 251 PLLICDEPTSGLDSFMAHSVVQVLKKLSQKG-KTVILTIHQPSSELfeLFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI--LADKVIVFSEGKLIAQGKPKE 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
104-318 |
2.17e-14 |
|
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: 73.34 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FRSSKGVQIspstirMLNGHPV---DAKEMQARCAYVQQD-DLFIGS 178
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErFYDPTSGEI------LLDGVDIrdlNLRWLRSQIGLVSQEpVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LtaREHLIFQamvRMPRHMTQKQKVQRV---DQVIQDLSLGkcQNTLIGVPGrvKGLSGGERKRLAFASEALTDPPLLIC 255
Cdd:cd03249 93 I--AENIRYG---KPDATDEEVEEAAKKaniHDFIMSLPDG--YDTLVGERG--SQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 256 DEPTSGLDsfmAHSVVQVLKKLSQ--KGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGTPGE 318
Cdd:cd03249 164 DEATSALD---AESEKLVQEALDRamKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQGTHDE 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
104-291 |
2.98e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.30 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAF--RSSKGV-QISPSTIRMLNGhpvdakemqarcayvqqDDLfigSLT 180
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCldKPTSGTyRVAGQDVATLDA-----------------DAL---AQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 AREHL--IFQAMVRMPrHMTQKQKV---------------QRVDQVIQDLSLGKcqntliGVPGRVKGLSGGERKRLAFA 243
Cdd:PRK10535 84 RREHFgfIFQRYHLLS-HLTAAQNVevpavyaglerkqrlLRAQELLQRLGLED------RVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 577718259 244 SEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQP 291
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
80-310 |
3.29e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 80 KQLVNRVKGVFCNerHIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIaFRSSKGvQISPSTirMLNGHPVD- 158
Cdd:TIGR02633 254 GDVILEARNLTCW--DVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQAL-FGAYPG-KFEGNV--FINGKPVDi 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 159 ---AKEMQARCAYVQQD---DLFIGSLTAREHLIFQAMVRMPRHMT--QKQKVQRVDQVIQDLSLGKCQNTLigvpgRVK 230
Cdd:TIGR02633 328 rnpAQAIRAGIAMVPEDrkrHGIVPILGVGKNITLSVLKSFCFKMRidAAAELQIIGSAIQRLKVKTASPFL-----PIG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 231 GLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTihqpSSELFE---LFDKILLMAE 307
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVV----SSELAEvlgLSDRVLVIGE 478
|
...
gi 577718259 308 GRV 310
Cdd:TIGR02633 479 GKL 481
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
104-318 |
3.69e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.51 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTL---LNAIaFRSSKGvqispsTIRmLNGHPVDAK---EMQARCAYVQQ--DDLF 175
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGL-LLPEAG------TIT-VGGMVLSEEtvwDVRRQVGMVFQnpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSlTAREHLIFQAMVR-MPRhmtqKQKVQRVDQVIQDLSLgkcQNTLIGVPGRvkgLSGGERKRLAFASEALTDPPLLI 254
Cdd:PRK13635 95 VGA-TVQDDVAFGLENIgVPR----EEMVERVDQALRQVGM---EDFLNREPHR---LSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 255 CDEPTSGLDSFMAHSVVQVLKKL-SQKGKTVILTIHQPSSELFElfDKILLMAEGRVAFLGTPGE 318
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQA--DRVIVMNKGEILEEGTPEE 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
82-361 |
4.91e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.58 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 82 LVNRVKGVFCNERHIpaprKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPS--TIRMLNGHPVda 159
Cdd:COG4586 20 LKGALKGLFRREYRE----VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT-----GI-LVPTsgEVRVLGYVPF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 160 KEmqaRCAYVQQddlfIGS-----------LTAREHL-IFQAMVRMPRhmtqKQKVQRVDQVIQDLSLGKcqntLIGVPg 227
Cdd:COG4586 88 KR---RKEFARR----IGVvfgqrsqlwwdLPAIDSFrLLKAIYRIPD----AEYKKRLDELVELLDLGE----LLDTP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 228 rVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMA 306
Cdd:COG4586 152 -VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHD-MDDIEALCDRVIVID 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 307 EGRVAFLGTPGEAVDFFSY---IGATCPTNYNPADF--YVQVLAVVPGR---EVESRERIAKI 361
Cdd:COG4586 230 HGRIIYDGSLEELKERFGPyktIVLELAEPVPPLELprGGEVIEREGNRvrlEVDPRESLAEV 292
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
104-316 |
5.68e-14 |
|
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: 71.76 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIaFRSskgVQISPSTIRmLNGHP---VDAKEMQARCAYVQQDD-LFIGSL 179
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLAL-FRL---VELSSGSIL-IDGVDiskIGLHDLRSRISIIPQDPvLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 taREHL----------IFQAMvrmprhmtqkQKVQrVDQVIQDLSLGKcqNTLIGVPGrvKGLSGGERKRLAFASEALTD 249
Cdd:cd03244 95 --RSNLdpfgeysdeeLWQAL----------ERVG-LKEFVESLPGGL--DTVVEEGG--ENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 250 PPLLICDEPTSGLDSFMAHSVVQVLKKlSQKGKTVIL------TIHQpsselfelFDKILLMAEGRVAFLGTP 316
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTiahrldTIID--------SDRILVLDKGRVVEFDSP 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
104-321 |
6.55e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.00 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKG-VQISPSTIRMLNghpvdAKEMQARCAYVQQ--------- 171
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrVFDPQSGrILIDGTDIRTVT-----RASLRRNIAVVFQdaglfnrsi 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 -DDLFIGSLTAREHLIFQAMVRMPRHmtqkqkvqrvdqviqDLSLGK--CQNTLIGVPGRVkgLSGGERKRLAFASEALT 248
Cdd:PRK13657 426 eDNIRVGRPDATDEEMRAAAERAQAH---------------DFIERKpdGYDTVVGERGRQ--LSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSqKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGTPGEAVD 321
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLST--VRNADRILVFDNGRVVESGSFDELVA 558
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
112-316 |
7.71e-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: 75.44 E-value: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 112 YPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVDAK--EMQARCAYVQQDDLFIGSLTAREHLIFQA 189
Cdd:TIGR01257 954 YENQITAFLGHNGAGKTTTLSILT-----GLLPPTSGTVLVGGKDIETNldAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 190 MVRmprHMTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHS 269
Cdd:TIGR01257 1029 QLK---GRSWEEAQLEMEAMLEDTGLHHKRNE------EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577718259 270 VVQVLKKLsQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTP 316
Cdd:TIGR01257 1100 IWDLLLKY-RSGRTIIMSTHH-MDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
101-322 |
9.34e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.20 E-value: 9.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGVQISPSTIrmlnghpvdakemqarcAYVQQdDLFIGS 178
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlsQFEISEGRVWAERSI-----------------AYVPQ-QAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTAREHLIFQAMVRMPRhmtqKQKVQRVDQVIQDL-SLGKCQNTLIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDE 257
Cdd:PTZ00243 735 ATVRGNILFFDEEDAAR----LADAVRVSQLEADLaQLGGGLETEIGEKG--VNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 258 PTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpsSELFELFDKILLMAEGRVAFlgtPGEAVDF 322
Cdd:PTZ00243 809 PLSALDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDGRVEF---SGSSADF 868
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
71-314 |
9.94e-14 |
|
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: 71.21 E-value: 9.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 71 AVHQPGSSWKqlvNRVKGVFCNE-RHIPAprkhlLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPS-- 147
Cdd:cd03267 11 RVYSKEPGLI---GSLKSLFKRKyREVEA-----LKGISFTIEKGEIVGFIGPNGAGKTTTLKILS-----GL-LQPTsg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 148 TIRMLNGHPVDAKEmqarcAYVQQDDLFIGSltaREHLIFQAMV----RMPRHMTQKQKVQ---RVDQVIQDLSLGKcqn 220
Cdd:cd03267 77 EVRVAGLVPWKRRK-----KFLRRIGVVFGQ---KTQLWWDLPVidsfYLLAAIYDLPPARfkkRLDELSELLDLEE--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 221 tLIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLS-QKGKTVILTIHQpSSELFELF 299
Cdd:cd03267 146 -LLDTP--VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSHY-MKDIEALA 221
|
250
....*....|....*
gi 577718259 300 DKILLMAEGRVAFLG 314
Cdd:cd03267 222 RRVLVIDKGRLLYDG 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
102-324 |
1.07e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.80 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 102 HLLKNVSGVAYPGELLAVMGSSGAGKTTLlnaiafrsskgvqispstIRMLNG--HP------VDAKEmqarcayvqqdd 173
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKSTL------------------IRCINLleRPtsgsvlVDGVD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 lfIGSLTAREhL---------IFQ--------------AM----VRMPRhmtqKQKVQRVDQVIQdlslgkcqntLIGVP 226
Cdd:COG1135 69 --LTALSERE-LraarrkigmIFQhfnllssrtvaenvALpleiAGVPK----AEIRKRVAELLE----------LVGLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 227 GRVKG----LSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFD 300
Cdd:COG1135 132 DKADAypsqLSGGQKQRVGIA-RALaNNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHE-MDVVRRICD 209
|
250 260
....*....|....*....|....
gi 577718259 301 KILLMAEGRVAFLGTpgeAVDFFS 324
Cdd:COG1135 210 RVAVLENGRIVEQGP---VLDVFA 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
231-318 |
1.36e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.19 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 231 GLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELfELFDKILLMAEGRV 310
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKGKI 254
|
....*...
gi 577718259 311 AFLGTPGE 318
Cdd:PRK13631 255 LKTGTPYE 262
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
101-263 |
1.90e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.18 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGvQISPS--TIRMLNGhpvdakemqARCAYVQQDDLFIGS 178
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA-----G-ELEPDsgEVSIPKG---------LRIGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTAREHlIFQAMVRMPRHMTQKQKV-QRVDQVIQDLS-LGKCQNTL------------------IGVPG-----RVKGLS 233
Cdd:COG0488 76 LTVLDT-VLDGDAELRALEAELEELeAKLAEPDEDLErLAELQEEFealggweaearaeeilsgLGFPEedldrPVSELS 154
|
170 180 190
....*....|....*....|....*....|
gi 577718259 234 GGERKRLAFASEALTDPPLLICDEPTSGLD 263
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
101-315 |
1.99e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.18 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGvQISPS--TIRMlnGHPVdakemqaRCAYVQQD-DLFIG 177
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA-----G-ELEPDsgTVKL--GETV-------KIGYFDQHqEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTAREHLifqamvrmpRHMTQKQKVQRVDQVIQDLSL-GKCQNTLIGVpgrvkgLSGGERKRLAFASEALTDPPLLICD 256
Cdd:COG0488 393 DKTVLDEL---------RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGV------LSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 257 EPTSGLDSFMAHSVVQVLKKLsqKGkTVILTIHQPSselF--ELFDKILLMAEGRV-AFLGT 315
Cdd:COG0488 458 EPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRY---FldRVATRILEFEDGGVrEYPGG 513
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
101-318 |
2.01e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.56 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FRSSKGVQIspstirMLNGhpvdakemqarcayvqQDDLFIGSL 179
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAgFEQPTAGQI------MLDG----------------VDLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLIFQAMVRMPrHMTQKQ------------KVQRVDQVIQDLSLGKCQNTLIGVPGRvkgLSGGERKRLAFASEAL 247
Cdd:PRK11607 90 QRPINMMFQSYALFP-HMTVEQniafglkqdklpKAEIASRVNEMLGLVHMQEFAKRKPHQ---LSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 248 TDPPLLICDEPTSGLDS----FMAHSVVQVLKKLsqkGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKklrdRMQLEVVDILERV---GVTCVMVTHD-QEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
113-315 |
3.58e-13 |
|
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: 73.51 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTllnaiAFRSSKGVQISPSTIRMLNGHPV--DAKEMQARCAYVQQDDLFIGSLTAREHLIFQAM 190
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTT-----TFKMLTGDTTVTSGDATVAGKSIltNISDVHQNMGYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 191 VR-MPrhmtqKQKVQRV-DQVIQDLSLGKCQNTLIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAH 268
Cdd:TIGR01257 2039 LRgVP-----AEEIEKVaNWSIQSLGLSLYADRLAGT------YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577718259 269 SVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGT 315
Cdd:TIGR01257 2108 MLWNTIVSIIREGRAVVLTSHS-MEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
113-321 |
5.08e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIA-FRSSKGVQIspstirMLNG--HPVDAKEMQARCAYVQQDDLFigsltarEHLIFQA 189
Cdd:PRK10771 24 RGERVAILGPSGAGKSTLLNLIAgFLTPASGSL------TLNGqdHTTTPPSRRPVSMLFQENNLF-------SHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 190 MVRMPRH----MTQKQKvQRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 265
Cdd:PRK10771 91 NIGLGLNpglkLNAAQR-EKLHAIARQMGIEDLLARL---PGQ---LSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 266 MAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPGEAVD 321
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
85-319 |
5.17e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.98 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 85 RVKGVFC-NERHIPAprkhlLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGV-QISPSTIRmLNGHPV---DA 159
Cdd:COG3845 259 EVENLSVrDDRGVPA-----LKDVSLEVRAGEILGIAGVAGNGQSELAEALA-----GLrPPASGSIR-LDGEDItglSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 160 KEM-QARCAYVQQDDL---FIGSLTAREHLIFQAMVRMP---RHMTQKQKVQR-VDQVIQDLSLgKCQNtlIGVPgrVKG 231
Cdd:COG3845 328 RERrRLGVAYIPEDRLgrgLVPDMSVAENLILGRYRRPPfsrGGFLDRKAIRAfAEELIEEFDV-RTPG--PDTP--ARS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAFASEALTDPPLLICDEPTSGLDsFMA-HSVVQVLKKLSQKGKTVILtIhqpSSELFELF---DKILLMAE 307
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLD-VGAiEFIHQRLLELRDAGAAVLL-I---SEDLDEILalsDRIAVMYE 477
|
250
....*....|..
gi 577718259 308 GRVAFLGTPGEA 319
Cdd:COG3845 478 GRIVGEVPAAEA 489
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
100-318 |
5.23e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.88 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHpvDAKEMQAR---CAYVQQDDLFI 176
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIA-----GLEHQTSGHIRFHGT--DVSRLHARdrkVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTAREHLIFQAMVrMPRHMTQ-----KQKVQRVDQVIQdlsLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPP 251
Cdd:PRK10851 87 RHMTVFDNIAFGLTV-LPRRERPnaaaiKAKVTQLLEMVQ---LAHLADRY---PAQ---LSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 252 LLICDEPTSGLDSFMAHSVVQVLKKLSQKGK--TVILTIHQpsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKftSVFVTHDQ--EEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
103-291 |
5.65e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.03 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPS--TIRMLNGhpvdakemqARCAYVQQ----DDLFi 176
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLA-----GV-LRPTsgTVRRAGG---------ARVAYVPQrsevPDSL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 gSLTAREhlifqaMVRMPR--HMTQKQKVQRVDQVIQDLSLGKCQntLIGVPGR-VKGLSGGERKRLAFASEALTDPPLL 253
Cdd:NF040873 71 -PLTVRD------LVAMGRwaRRGLWRRLTRDDRAAVDDALERVG--LADLAGRqLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 577718259 254 ICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQP 291
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
114-320 |
6.23e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.08 E-value: 6.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTT-------LLNAiafrsSKGvqispsTIRMLnGHPVDAKEMQAR--CAYVQQDDLFIGSLTAREH 184
Cdd:NF033858 292 GEIFGFLGSNGCGKSTtmkmltgLLPA-----SEG------EAWLF-GQPVDAGDIATRrrVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 185 LIFQAmvrmpR--HMTQKQKVQRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 262
Cdd:NF033858 360 LELHA-----RlfHLPAAEIAARVAEMLERFDLADVADAL---PDS---LPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 263 D-----SFMahsvvQVLKKLS-QKGKTVILTIHqpsselF----ELFDKILLMAEGRVAFLGTPGEAV 320
Cdd:NF033858 429 DpvardMFW-----RLLIELSrEDGVTIFISTH------FmneaERCDRISLMHAGRVLASDTPAALV 485
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
101-318 |
7.05e-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: 68.80 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQiSPSTIRMLnghpVDAKEMQARCAY------VQQDDL 174
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA-----GFE-TPTSGEIL----LDGKDITNLPPHkrpvntVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLTAREHLIFQ-AMVRMPRHmTQKQKVQRVDQVIQDLSLGKcqntligvpGRVKGLSGGERKRLAFASEALTDPPLL 253
Cdd:cd03300 83 LFPHLTVFENIAFGlRLKKLPKA-EIKERVAEALDLVQLEGYAN---------RKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 254 ICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHD-QEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
113-324 |
8.17e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.62 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIAF---RSSKGVQISPSTI---RMLNGHPVDAKEMQARCAYVQQDDLFIGSLTAREHLI 186
Cdd:PRK11264 28 PGEVVAIIGPSGSGKTTLLRCINLleqPEAGTIRVGDITIdtaRSLSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLENII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 187 FQAMV--RMPRhmtqKQKVQRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 264
Cdd:PRK11264 108 EGPVIvkGEPK----EEATARARELLAKVGLAGKETSY---PRR---LSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 265 FMAHSVVQVLKKLSQKGKTVILTIHQPSselF--ELFDKILLMAEGRVAflgTPGEAVDFFS 324
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMS---FarDVADRAIFMDQGRIV---EQGPAKALFA 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
95-315 |
8.82e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.28 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 95 HIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIafrsSKGVQISPSTIRmLNGHPVDA---KEMQARCAYVQQ 171
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI----QRHFDVSEGDIR-FHDIPLTKlqlDSWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DDlFIGSLTAREHLifqAMVRMPRHMTQKQKVQRVDQVIQD-LSLGKCQNTLIGVPGRVkgLSGGERKRLAFASEALTDP 250
Cdd:PRK10789 397 TP-FLFSDTVANNI---ALGRPDATQQEIEHVARLASVHDDiLRLPQGYDTEVGERGVM--LSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 251 PLLICDEPTSGLDSFMAHsvvQVLKKLSQ--KGKTVILTIHQPSSeLFELfDKILLMAEGRVAFLGT 315
Cdd:PRK10789 471 EILILDDALSAVDGRTEH---QILHNLRQwgEGRTVIISAHRLSA-LTEA-SEILVMQHGHIAQRGN 532
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
80-310 |
1.02e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.20 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 80 KQLVNRVKG--VFCN------ERHIPAprkhlLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIafrsSKGVQISPSTIrM 151
Cdd:PRK11176 332 KRVIERAKGdiEFRNvtftypGKEVPA-----LRNINFKIPAGKTVALVGRSGSGKSTIANLL----TRFYDIDEGEI-L 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 152 LNGHPVDAKEMQA---RCAYV-QQDDLFIGSLT-----------AREHLIFQAmvRMPRHMtqkQKVQRVDQVIqdlslg 216
Cdd:PRK11176 402 LDGHDLRDYTLASlrnQVALVsQNVHLFNDTIAnniayarteqySREQIEEAA--RMAYAM---DFINKMDNGL------ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 217 kcqNTLIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLsQKGKTVILTIHQPSSelF 296
Cdd:PRK11176 471 ---DTVIGENGVL--LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--I 542
|
250
....*....|....
gi 577718259 297 ELFDKILLMAEGRV 310
Cdd:PRK11176 543 EKADEILVVEDGEI 556
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
101-280 |
1.03e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTT----LLNAIAFRSSKGVQISPStirmlngHPVDAKEM---QARCAYVQQDD 173
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPL-------HNLNRRQLlpvRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 lfIGSLTAR---EHLIFQAMVRMPRHMTQKQKVQRVDQVIQDLSLGKcqNTLIGVPGRvkgLSGGERKRLAFASEALTDP 250
Cdd:PRK15134 372 --NSSLNPRlnvLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDP--ETRHRYPAE---FSGGQRQRIAIARALILKP 444
|
170 180 190
....*....|....*....|....*....|
gi 577718259 251 PLLICDEPTSGLDSFMAHSVVQVLKKLSQK 280
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
102-316 |
1.23e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.61 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 102 HLLKNVSGVAYPGELLAVMGSSGAGKTTLL---NAIAFRSSKGVQISPSTIrmlngHPVDAKEMQARCAYVQQD-DLFIG 177
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLlhlNGIYLPQRGRVKVMGREV-----NAENEKWVRSKVGLVFQDpDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTAREHLIFQamvrmPRHM--TQKQKVQRVDQVIQDLSLGKCqntligvpgRVKG---LSGGERKRLAFASEALTDPPL 252
Cdd:PRK13647 94 SSTVWDDVAFG-----PVNMglDKDEVERRVEEALKAVRMWDF---------RDKPpyhLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 253 LICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELfELFDKILLMAEGRVAFLGTP 316
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEGDK 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
73-310 |
1.32e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 73 HQPGsswkQLVNRVKGVFCneRHIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGVQIspstir 150
Cdd:PRK13549 253 HTIG----EVILEVRNLTA--WDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgAYPGRWEGEI------ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 151 MLNGHPVD----AKEMQARCAYVQQD--------DLFIG---SLTAREHLIFQAMVRMPRhmtqkqKVQRVDQVIQDLSL 215
Cdd:PRK13549 321 FIDGKPVKirnpQQAIAQGIAMVPEDrkrdgivpVMGVGkniTLAALDRFTGGSRIDDAA------ELKTILESIQRLKV 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 216 GKCQNTLigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTihqpSSEL 295
Cdd:PRK13549 395 KTASPEL-----AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI----SSEL 465
|
250
....*....|....*...
gi 577718259 296 FE---LFDKILLMAEGRV 310
Cdd:PRK13549 466 PEvlgLSDRVLVMHEGKL 483
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
99-289 |
1.40e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.28 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIafrsskGVQISPSTIR-MLNGHPV---DAKEMQARCAYVQQDDL 174
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML------GRHQPPSEGEiLLDAQPLeswSSKAFARKVAYLPQQLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLTAREhliFQAMVRMPRHMT----QKQKVQRVDQVIQDLSLGKCQNTLigvpgrVKGLSGGERKRLAFASEALTDP 250
Cdd:PRK10575 96 AAEGMTVRE---LVAIGRYPWHGAlgrfGAADREKVEEAISLVGLKPLAHRL------VDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 577718259 251 PLLICDEPTSGLDsfMAHS--VVQVLKKLSQ-KGKTVILTIH 289
Cdd:PRK10575 167 RCLLLDEPTSALD--IAHQvdVLALVHRLSQeRGLTVIAVLH 206
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
118-310 |
1.56e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.52 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 118 AVMGSSGAGKTTLLNAIAfrsskGVqISPSTIRM-LNGHP-VDAKEM------QARCAYVQQDDLFIGSLTAREHLIFQa 189
Cdd:PRK11144 28 AIFGRSGAGKTSLINAIS-----GL-TRPQKGRIvLNGRVlFDAEKGiclppeKRRIGYVFQDARLFPHYKVRGNLRYG- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 190 mvrmprhMTQKQKVQrVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHS 269
Cdd:PRK11144 101 -------MAKSMVAQ-FDKIVALLGIEPLLDRY---PGS---LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 577718259 270 VVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRV 310
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
94-280 |
1.58e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 70.48 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 94 RHIPAprkhlLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIaFR--SSKGvqispsTIRmLNGHPVDA---KEMQARCAY 168
Cdd:COG4172 297 GHVKA-----VDGVSLTLRRGETLGLVGESGSGKSTLGLAL-LRliPSEG------EIR-FDGQDLDGlsrRALRPLRRR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 169 VQ---QDDLfiGSLTAR---EHLIFQAMVRMPRHMTQKQKVQRVDQVIQDlslgkcqntlIGVPGRVKG-----LSGGER 237
Cdd:COG4172 364 MQvvfQDPF--GSLSPRmtvGQIIAEGLRVHGPGLSAAERRARVAEALEE----------VGLDPAARHrypheFSGGQR 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 577718259 238 KRLAFAsEAL-TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK 280
Cdd:COG4172 432 QRIAIA-RALiLEPKLLVLDEPTSALDVSVQAQILDLLRDLQRE 474
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
104-290 |
1.75e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 67.73 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLL---NAIAFRSSKGVQISPSTIRMLNghPVDAKEMQARCAYV----QQDDLFi 176
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLrvlNLLETPDSGQLNIAGHQFDFSQ--KPSEKAIRLLRQKVgmvfQQYNLW- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTAREHLIfQAMVRMPRhMTQKQKVQRVDQVIQDLSLgkcQNTLIGVPGRvkgLSGGERKRLAFASEALTDPPLLICD 256
Cdd:COG4161 95 PHLTVMENLI-EAPCKVLG-LSKEQAREKAMKLLARLRL---TDKADRFPLH---LSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|....
gi 577718259 257 EPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQ 290
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
101-312 |
1.88e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.80 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvQIspstirMLNGHPVDAKEMQARCAY---VQQDDLf 175
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAgsLPPDSG-SI------LIDGKDVTKLPEYKRAKYigrVFQDPM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IG---SLTAREHLIFQAMVRMPRHMTQKQKVQRVDQVIQDLS-LGkcqntlIGVPGR----VKGLSGGERKRLAFASEAL 247
Cdd:COG1101 91 MGtapSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLAtLG------LGLENRldtkVGLLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 248 TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGK-TVILTIHQPSSELfELFDKILLMAEGRVAF 312
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQAL-DYGNRLIMMHEGRIIL 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
99-315 |
2.17e-12 |
|
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: 70.23 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNaIAFR----SSKGVQISPSTIRMlnghpVDAKEMQARCAYVQQDD- 173
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR-LLFRfydvTSGRILIDGQDIRD-----VTQASLRAAIGIVPQDTv 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LF-------I--GSLTAREHLIFQAMvrmprhmtqkqKVQRVDQVIQDLSLGKcqNTLIGVPGrVKgLSGGERKRLAFAS 244
Cdd:COG5265 443 LFndtiaynIayGRPDASEEEVEAAA-----------RAAQIHDFIESLPDGY--DTRVGERG-LK-LSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 245 EALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQkGKTVILTIHQPS----SelfelfDKILLMAEGRVAFLGT 315
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLStivdA------DEILVLEAGRIVERGT 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
99-315 |
2.27e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTT----LLNaiaFRSSKGVQIspstirMLNGHPV---DAKEMQARCAYVQQ 171
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaalLQN---LYQPTGGQV------LLDGVPLvqyDHHYLHRQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DD-LFIGSLTareHLIFQAMVRMPRHMTQKQKVQR-VDQVIQDLSLGkcQNTLIGVPGRVkgLSGGERKRLAFASEALTD 249
Cdd:TIGR00958 563 EPvLFSGSVR---ENIAYGLTDTPDEEIMAAAKAAnAHDFIMEFPNG--YDTEVGEKGSQ--LSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 250 PPLLICDEPTSGLDSFMAHSVVQvlkKLSQKGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGT 315
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQE---SRSRASRTVLLIAHRLS--TVERADQILVLKKGSVVEMGT 696
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
105-311 |
4.32e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 105 KNVSGVAYPGELLAVMGSSGAGKTTLLNAIaFRSSK---------GVQISPSTirmlnghPVDA--KEMqarcAYV---Q 170
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCL-FGVDKraggeirlnGKDISPRS-------PLDAvkKGM----AYItesR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 171 QDDLFIGSLTAREHLIFQAMVRMPRH------MTQKQKVQRVDQVIQDLSLgKCQNtligVPGRVKGLSGGERKRLAFAS 244
Cdd:PRK09700 348 RDNGFFPNFSIAQNMAISRSLKDGGYkgamglFHEVDEQRTAENQRELLAL-KCHS----VNQNITELSGGNQQKVLISK 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 245 EALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRVA 311
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGRLT 488
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
101-319 |
4.99e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.07 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskgvQISPS---TIRMLNGhpvdakemqARCAYV-QQDDLFI 176
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA-------GLWPYgsgRIARPAG---------ARVLFLpQRPYLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLtaREHLIFQAMvrmPRHMTQkqkvQRVDQVIQDLSLGKcqntLIGvpgRV-------KGLSGGERKRLAFASEALTD 249
Cdd:COG4178 440 GTL--REALLYPAT---AEAFSD----AELREALEAVGLGH----LAE---RLdeeadwdQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 250 PPLLICDEPTSGLDSFMAHSVVQVLKKlSQKGKTVILTIHQPSseLFELFDKIL-LMAEGRVAFLGTPGEA 319
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRST--LAAFHDRVLeLTGDGSWQLLPAEAPA 571
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
498-609 |
6.06e-12 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 65.22 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 498 YFLGKTIAELPLFLVVPFLFTAIAYPLIGLRPGVDHFFTALALVTLVANVSTSFGYLISCACSSTSMALSVGPPVIIPFL 577
Cdd:COG0842 48 ILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLT 127
|
90 100 110
....*....|....*....|....*....|..
gi 577718259 578 LFGGFFLNSGSVPAYFKWLSYLSWFRYANEGL 609
Cdd:COG0842 128 FLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
100-286 |
6.13e-12 |
|
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: 67.39 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVA---YPGELLAVMGSSGAGKTTLLNAI-----AFRSSKGvqispsTIRmLNGHPV---DAKEMQA---- 164
Cdd:COG0444 14 RRGVVKAVDGVSfdvRRGETLGLVGESGSGKSTLARAIlgllpPPGITSG------EIL-FDGEDLlklSEKELRKirgr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 165 RCAYVQQDDLfiGSL----TAREHLIfqAMVRMPRHMTQKQKVQRVDQVIQDLSlgkcqntlIGVPGRVKG-----LSGG 235
Cdd:COG0444 87 EIQMIFQDPM--TSLnpvmTVGDQIA--EPLRIHGGLSKAEARERAIELLERVG--------LPDPERRLDrypheLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577718259 236 ERKRLAFASeAL-TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVIL 286
Cdd:COG0444 155 MRQRVMIAR-ALaLEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILF 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
101-323 |
6.29e-12 |
|
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: 68.29 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAI----AFRSSKG-----VQISPSTIRMlnGHPVDAKEMQARCA---- 167
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdQYEPTSGriiyhVALCEKCGYV--ERPSKVGEPCPVCGgtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 168 -----YVQQDDLFIGSLTAREHLIFQ----------AMVRMPRHMTQ-----KQKVQRVDQVIQDLSLGKcQNTLIGvpg 227
Cdd:TIGR03269 91 peevdFWNLSDKLRRRIRKRIAIMLQrtfalygddtVLDNVLEALEEigyegKEAVGRAVDLIEMVQLSH-RITHIA--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 228 rvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKL-SQKGKTVILTIHQPSSeLFELFDKILLMA 306
Cdd:TIGR03269 167 --RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEV-IEDLSDKAIWLE 243
|
250
....*....|....*..
gi 577718259 307 EGRVAFLGTPGEAVDFF 323
Cdd:TIGR03269 244 NGEIKEEGTPDEVVAVF 260
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
114-287 |
6.99e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.81 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTL---LNAIAFRSSKGVQISPSTIRMlnGHPVDAKEMQARCAYV----QQDDLFiGSLTAREHLI 186
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLlrvLNLLEMPRSGTLNIAGNHFDF--SKTPSDKAIRELRRNVgmvfQQYNLW-PHLTVQQNLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 187 fQAMVRMpRHMTQKQKVQRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 266
Cdd:PRK11124 105 -EAPCRV-LGLSKDQALARAEKLLERLRLKPYADRF---PLH---LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180
....*....|....*....|..
gi 577718259 267 AHSVVQVLKKLSQKGKT-VILT 287
Cdd:PRK11124 177 TAQIVSIIRELAETGITqVIVT 198
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
104-318 |
7.48e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 66.58 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTL---LNAIAFRSSKGVQISPSTIRMlNGHPVDAKEMQARCAYVQQddlFigslt 180
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLlqhLNGLLQPTSGTVTIGERVITA-GKKNKKLKPLRKKVGIVFQ---F----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 aREHLIFQAMVR-------MPRHMTQKQKVQRVDQVIQdlslgkcqntLIGVPGRVKG-----LSGGERKRLAFASEALT 248
Cdd:PRK13634 94 -PEHQLFEETVEkdicfgpMNFGVSEEDAKQKAREMIE----------LVGLPEELLArspfeLSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQ-KGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHS-MEDAARYADQIVVMHKGTVFLQGTPRE 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
232-331 |
7.72e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.61 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGK-TVILTIHqpSSE-LFELFDKILLMAEGR 309
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSH--SMEdVAKLADRIIVMNKGK 222
|
90 100
....*....|....*....|....*
gi 577718259 310 VAFLGTPGEA---VDFFSYIGATCP 331
Cdd:PRK13637 223 CELQGTPREVfkeVETLESIGLAVP 247
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
100-287 |
8.45e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.95 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGVQISPSTIRMLNGHPV-----DAKEMQARCAYV-QQDD 173
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIysprtDTVDLRKEIGMVfQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFIGSltarehlIFQAMVRMPRHMTQKQKvQRVDQVIQdlslgkcqNTLIG--VPGRVK--------GLSGGERKRLAFA 243
Cdd:PRK14239 97 PFPMS-------IYENVVYGLRLKGIKDK-QVLDEAVE--------KSLKGasIWDEVKdrlhdsalGLSGGQQQRVCIA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 577718259 244 SEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILT 287
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
104-315 |
8.66e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 8.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVA---YPGELLAVMGSSGAGKTTLLNAIAfrsskG-VQISPSTIRMLNGHPVDAKEMQARCAY--VQ---QDDL 174
Cdd:PRK15079 34 LKAVDGVTlrlYEGETLGVVGESGCGKSTFARAII-----GlVKATDGEVAWLGKDLLGMKDDEWRAVRsdIQmifQDPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 F-------IGSLTAREHLIFQAmvrmprHMTQKQKVQRVDQVIqdLSLGKCQNTLIGVPGRvkgLSGGERKRLAFASEAL 247
Cdd:PRK15079 109 AslnprmtIGEIIAEPLRTYHP------KLSRQEVKDRVKAMM--LKVGLLPNLINRYPHE---FSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 248 TDPPLLICDEPTSGLDSFMAHSVVQVLKKLsQK--GKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGT 315
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQL-QRemGLSLIFIAHDLAV-VKHISDRVLVMYLGHAVELGT 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
104-289 |
1.16e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.26 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTL---LNA----------IAFRSSK-------------GVQISPSTIRMLNghpv 157
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFiehLNAlllpdtgtieWIFKDEKnkkktkekekvleKLVIQKTRFKKIK---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 158 DAKEMQARCAYVQQ---DDLFigSLTAREHLIFQAMvrmPRHMTQKQKVQRVDQVIQdlslgkcqntLIGVPGRVK---- 230
Cdd:PRK13651 99 KIKEIRRRVGVVFQfaeYQLF--EQTIEKDIIFGPV---SMGVSKEEAKKRAAKYIE----------LVGLDESYLqrsp 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 231 -GLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIH 289
Cdd:PRK13651 164 fELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
99-357 |
1.74e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.09 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQiSPS--TIRmLNGHPVDAKEMQARCAY---VQ--- 170
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLV-----GLE-SPSqgNVS-WRGEPLAKLNRAQRKAFrrdIQmvf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 171 QDDlfIGSLTAREHLifQAMVRMP-RHMT---QKQKVQRVDQVIQ--DLSLGKCQNtligVPGRvkgLSGGERKRLAFAS 244
Cdd:PRK10419 96 QDS--ISAVNPRKTV--REIIREPlRHLLsldKAERLARASEMLRavDLDDSVLDK----RPPQ---LSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 245 EALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTI-HQPSseLFELF-DKILLMAEGRVAFLGTPGEAVDF 322
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFItHDLR--LVERFcQRVMVMDNGQIVETQPVGDKLTF 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 577718259 323 FSYIGatcptnynpadfyvQVL--AVVPGREVESRER 357
Cdd:PRK10419 243 SSPAG--------------RVLqnAVLPAFPVRRRTT 265
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
101-316 |
1.77e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.70 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRssKGVQISPSTIRmLNGHPVDAKEMQARcayvqqddlfigslt 180
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKYEVTSGSIL-LDGEDILELSPDER--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 ARE--HLIFQAMVRMP--------RHMTQKQKVQRVDQViqdLSLGKCQNTLigvpGRVK------------GLSGGERK 238
Cdd:COG0396 75 ARAgiFLAFQYPVEIPgvsvsnflRTALNARRGEELSAR---EFLKLLKEKM----KELGldedfldryvneGFSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 239 RLAFASEALTDPPLLICDEPTSGLD--SFMAhsVVQVLKKLSQKGKTVILTIHQPssELFELF--DKILLMAEGRVAFLG 314
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDidALRI--VAEGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGRIVKSG 223
|
..
gi 577718259 315 TP 316
Cdd:COG0396 224 GK 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
113-310 |
1.83e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKT-TLLnaiafrsskgvqispSTIRMLNGHPVdakemqarcAYVQQDDLFIGS--LTAREH----- 184
Cdd:PRK15134 34 AGETLALVGESGSGKSvTAL---------------SILRLLPSPPV---------VYPSGDIRFHGEslLHASEQtlrgv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 185 ------LIFQ-AMVRM-PRHMTQKQkvqrvdqVIQDLSL----------GKCQNTL--IGV---PGRVKG----LSGGER 237
Cdd:PRK15134 90 rgnkiaMIFQePMVSLnPLHTLEKQ-------LYEVLSLhrgmrreaarGEILNCLdrVGIrqaAKRLTDyphqLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 238 KRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRV 310
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
101-289 |
2.20e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 62.08 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGVQISPSTIRMlnghpvdakemqarcAYVQQddlfigs 178
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgeLEPDEGIVTWGSTVKI---------------GYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 ltarehlifqamvrmprhmtqkqkvqrvdqviqdlslgkcqntligvpgrvkgLSGGERKRLAFASEALTDPPLLICDEP 258
Cdd:cd03221 71 -----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|.
gi 577718259 259 TSGLDSFMAHSVVQVLKKLSQkgkTVILTIH 289
Cdd:cd03221 98 TNHLDLESIEALEEALKEYPG---TVILVSH 125
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
100-291 |
2.23e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLnaiafrsskgvqispstiRMLNGhpvDAKEMQARCAYVQQDDLFIGSL 179
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLL------------------RLLAG---ALKGTPVAGCVDVPDNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLifqamvrmPRHMTQKQKVQRVDQViqdlSLGKCQNTLigvpGRVKGLSGGERKRLAFASEALTDPPLLICDEPT 259
Cdd:COG2401 101 SLIDAI--------GRKGDFKDAVELLNAV----GLSDAVLWL----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|...
gi 577718259 260 SGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQP 291
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRaGITLVVATHHY 197
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
106-310 |
2.61e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.56 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 106 NVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRsskgvqISPST----IRMLNGHPVDAKEM-QAR--------CAYVQQD 172
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSAR------LAPDAgevhYRMRDGQLRDLYALsEAErrrllrteWGFVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 173 --DLFIGSLTA----REHLifqaMVRMPRHM-----TQKQKVQRVDqviqdlslgkcqntlIGvPGRVKGL----SGGER 237
Cdd:PRK11701 98 prDGLRMQVSAggniGERL----MAVGARHYgdiraTAGDWLERVE---------------ID-AARIDDLpttfSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 238 KRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKL-SQKGKTVILTIHQPS-SELfeLFDKILLMAEGRV 310
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAvARL--LAHRLLVMKQGRV 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
104-310 |
2.70e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGVQIspstirmLNGHPVD----AKEMQARCAYVQQDDLFIG 177
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgDPRATSGRIV-------FDGKDITdwqtAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTAREHLifqAMVRMPRHMTQ-KQKVQRVDQVIQDLSLGKCQntligvpgRVKGLSGGERKRLAFASEALTDPPLLICD 256
Cdd:PRK11614 94 RMTVEENL---AMGGFFAERDQfQERIKWVYELFPRLHERRIQ--------RAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577718259 257 EPTSGLDSFMAHSVVQVLKKLSQKGKTVILtIHQPSSELFELFDKILLMAEGRV 310
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFL-VEQNANQALKLADRGYVLENGHV 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
104-344 |
4.13e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.44 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTT---LLNAIafrsskgvqISPSTIRMLNGHPVDAKEMQARCAYVQQDDLfigslt 180
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRL---------IEPTRGQVLIDGVDIAKISDAELREVRRKKI------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 areHLIFQAMVRMPrHMTQKQKV------------QRVDQVIQDLSLGKCQNTLIGVPGRvkgLSGGERKRLAFASEALT 248
Cdd:PRK10070 109 ---AMVFQSFALMP-HMTVLDNTafgmelaginaeERREKALDALRQVGLENYAHSYPDE---LSGGMRQRVGLARALAI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPGEAVDffsyiga 328
Cdd:PRK10070 182 NPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN------- 254
|
250
....*....|....*.
gi 577718259 329 tcptnyNPADFYVQVL 344
Cdd:PRK10070 255 ------NPANDYVRTF 264
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
104-310 |
4.40e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQiSPS--TIRmLNGHPV------DAKEmqARCAYVQQD--- 172
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILS-----GVY-QPDsgEIL-LDGEPVrfrsprDAQA--AGIAIIHQElnl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 173 --DL------FIGSLTAREHLI-FQAMVRMPRHMTQKQKVQ-RVDQVIQDLSLGKCQNTLIgvpgrVKGLSggerkrlaf 242
Cdd:COG1129 91 vpNLsvaeniFLGREPRRGGLIdWRAMRRRARELLARLGLDiDPDTPVGDLSVAQQQLVEI-----ARALS--------- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 243 asealTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRV 310
Cdd:COG1129 157 -----RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHR-LDEVFEIADRVTVLRDGRL 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
104-318 |
4.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.03 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTL---LNAIAFRSSKGVQISPSTIrmlnghpvdakemqarcaYVQQDDLFIGSLT 180
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLiqnINALLKPTTGTVTVDDITI------------------THKTKDKYIRPVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 AREHLIFQamvrMPRHMTQKQKVQR------------VDQVIQD-----LSLGKCQNTLIGVPGRvkgLSGGERKRLAFA 243
Cdd:PRK13646 85 KRIGMVFQ----FPESQLFEDTVEReiifgpknfkmnLDEVKNYahrllMDLGFSRDVMSQSPFQ---MSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 244 SEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLS-QKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHD-MNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
114-315 |
5.06e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAIAFRSSKgVQISPSTIRmlnghpvdakemqARCAYVQQDDlFIGSLTAREHLIFQAMVRM 193
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGELSH-AETSSVVIR-------------GSVAYVPQVS-WIFNATVRENILFGSDFES 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 194 PRHMtqkqKVQRVDQVIQDLSLGKCQN-TLIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQ 272
Cdd:PLN03232 708 ERYW----RAIDVTALQHDLDLLPGRDlTEIGERG--VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577718259 273 VLKKLSQKGKTVILTIHQpsSELFELFDKILLMAEGRVAFLGT 315
Cdd:PLN03232 782 SCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEGMIKEEGT 822
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
101-318 |
5.65e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.97 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA-FRSSKGVQIspstirMLNGHPVDAKEMQARcaYVqqddlfigsl 179
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAgFETPDSGRI------MLDGQDITHVPAENR--HV---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 tareHLIFQAMVRMPrHMT---------QKQKVQRVD---QVIQDLSLGKCQNTligVPGRVKGLSGGERKRLAFASEAL 247
Cdd:PRK09452 89 ----NTVFQSYALFP-HMTvfenvafglRMQKTPAAEitpRVMEALRMVQLEEF---AQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 248 TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHD-QEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
107-318 |
5.74e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.47 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 107 VSGVA---YPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIrMLNGHPVDAKEMQ--ARCAYV---QQDDLFi 176
Cdd:PRK11300 21 VNNVNlevREQEIVSLIGPNGAGKTTVFNCLTgfYKPTGG------TI-LLRGQHIEGLPGHqiARMGVVrtfQHVRLF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTAREHLifqaMVRMPRHM----------------TQKQKVQRVDQVIQDLSLGKCQNtligvpgRVKG-LSGGERKR 239
Cdd:PRK11300 93 REMTVIENL----LVAQHQQLktglfsgllktpafrrAESEALDRAATWLERVGLLEHAN-------RQAGnLAYGQQRR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 240 LAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
103-318 |
1.57e-10 |
|
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: 62.57 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFrsskgvQISPSTIRMlnghpvdakEMQARCAYVQQDDlFIGSLTAR 182
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG------ELEPSEGKI---------KHSGRISFSSQFS-WIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 183 EHLIFQAMVRMPRHMTqkqkVQRVDQVIQDLS-LGKCQNTLIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSG 261
Cdd:cd03291 116 ENIIFGVSYDEYRYKS----VVKACQLEEDITkFPEKDNTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 262 LDSFMAHSVVQ--VLKKLSQkgKTVILTIHQpsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:cd03291 190 LDVFTEKEIFEscVCKLMAN--KTRILVTSK--MEHLKKADKILILHEGSSYFYGTFSE 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
114-318 |
1.98e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.81 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAIAfrsskGVQiSPSTIRM-LNGHPVDAKEMQAR--CAYVQQDDLFigsltarEHLIFQAM 190
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVA-----GLE-KPTEGQIfIDGEDVTHRSIQQRdiCMVFQSYALF-------PHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 191 VRMPRHMTQKQKVQRVDQVIQDLSLGKcqntLIGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHS 269
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEALELVD----LAGFEDRyVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 577718259 270 VVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK11432 175 MREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
114-321 |
2.33e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAIAFRSSKgvqispstirmLNGHpvdaKEMQARCAYVQQDdLFIGSLTAREHLIFQAMVRM 193
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALLAEMDK-----------VEGH----VHMKGSVAYVPQQ-AWIQNDSLRENILFGKALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 194 PRHmtqkQKVQRVDQVIQDLS-LGKCQNTLIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQ 272
Cdd:TIGR00957 728 KYY----QQVLEACALLPDLEiLPSGDRTEIGEKG--VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577718259 273 --VLKKLSQKGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPGEAVD 321
Cdd:TIGR00957 802 hvIGPEGVLKNKTRILVTHGIS--YLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
103-290 |
2.79e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKG-VQISPSTIRmlnghpvdakemQARCAYvQQDDLFIG-- 177
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAglLNPEKGeILFERQSIK------------KDLCTY-QKQLCFVGhr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 -----SLTAREHLIFQAmvrmprHMTQKQkvQRVDQVIQDLSLGKcqntLIGVPGRVkgLSGGERKRLAFASEALTDPPL 252
Cdd:PRK13540 83 sginpYLTLRENCLYDI------HFSPGA--VGITELCRLFSLEH----LIDYPCGL--LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 577718259 253 LICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQ 290
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
103-303 |
2.87e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 59.47 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRMlnghPVDAKEMqarcaYVQQDDLF-IGSL 179
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglWPWGSG------RIGM----PEGEDLL-----FLPQRPYLpLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 taREHLIFqamvrmPRHMTqkqkvqrvdqviqdlslgkcqntligvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPT 259
Cdd:cd03223 81 --REQLIY------PWDDV---------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 577718259 260 SGLDSFMAHSVVQVLKKLsqkGKTVILTIHQPSseLFELFDKIL 303
Cdd:cd03223 120 SALDEESEDRLYQLLKEL---GITVISVGHRPS--LWKFHDRVL 158
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
104-286 |
2.94e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPV------DAkeMQARCAYVQQDDLF 175
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYglYQPDSG------EIL-IDGKPVrirsprDA--IALGIGMVHQHFML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSLTAREHLIFQAMVRMPRHMTQKQKVQRVDQVIQDLSLgkcqntliGVP--GRVKGLSGGERKRLafasE---AL-TD 249
Cdd:COG3845 92 VPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGL--------DVDpdAKVEDLSVGEQQRV----EilkALyRG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 577718259 250 PPLLICDEPTSGL-----DSFMAhsvvqVLKKLSQKGKTVIL 286
Cdd:COG3845 160 ARILILDEPTAVLtpqeaDELFE-----ILRRLAAEGKSIIF 196
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
113-303 |
2.94e-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: 59.30 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIAFrsskgvqispstirmlnghpvdakemqarcayvqqddlfigsltarehLIFQAMVR 192
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGL------------------------------------------------ALGGAQSA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 193 MPRHMTQKQKVQRVDQVIqdlslgkcqnTLIGVpgrVKGLSGGERKR----LAFASEALTDPPLLICDEPTSGLDSFMAH 268
Cdd:cd03227 52 TRRRSGVKAGCIVAAVSA----------ELIFT---RLQLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*
gi 577718259 269 SVVQVLKKLSQKGKTVILTIHQPssELFELFDKIL 303
Cdd:cd03227 119 ALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
105-321 |
3.65e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 105 KNVSGVAYPGELLAVMGSSGAGKTTLLNAI-AFRSSKGVQIspstirMLNGHPVDAKEMQARCA----YV----QQDDLF 175
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLyGLRPARGGRI------MLNGKEINALSTAQRLArglvYLpedrQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 --------IGSLTARehlifqamvRMPRHMTQKQKVQRVDQVIQDLSLgKCQNtligVPGRVKGLSGGERKRLAFASEAL 247
Cdd:PRK15439 354 ldaplawnVCALTHN---------RRGFWIKPARENAVLERYRRALNI-KFNH----AEQAARTLSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 248 TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTihqpSSELFE---LFDKILLMAEGRVAFLgTPGEAVD 321
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGEISGA-LTGAAIN 491
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
58-324 |
4.75e-10 |
|
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: 63.01 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 58 NLTYSWYNL--DVFGAVHQPGSSWKQLVNRVKGVFCNERHIPAPrkhLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIa 135
Cdd:TIGR01271 397 NVTASWDEGigELFEKIKQNNKARKQPNGDDGLFFSNFSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI- 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 136 frsskgvqispstirMLNGHPVDAK-EMQARCAYVQQDDlFIGSLTAREHLIFQAMVRMPRHMTqkqkVQRVDQVIQDLS 214
Cdd:TIGR01271 473 ---------------MGELEPSEGKiKHSGRISFSPQTS-WIMPGTIKDNIIFGLSYDEYRYTS----VIKACQLEEDIA 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 215 -LGKCQNTLIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQ--VLKKLSQKGKTVILTihqp 291
Cdd:TIGR01271 533 lFPEKDKTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEscLCKLMSNKTRILVTS---- 606
|
250 260 270
....*....|....*....|....*....|....*..
gi 577718259 292 SSELFELFDKILLMAEGRVAFLGT----PGEAVDFFS 324
Cdd:TIGR01271 607 KLEHLKKADKILLLHEGVCYFYGTfselQAKRPDFSS 643
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
103-315 |
5.69e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskgvqispstirmlnGHPvdakemqarcAY--VQQDDLFIGS-- 178
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA------------------GHP----------AYkiLEGDILFKGEsi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 --LTA--REH----LIFQAMVRMP---------RHMTQKQKVQRVDQV--IQDLSLGKCQNTLIGVPGRV------KGLS 233
Cdd:CHL00131 74 ldLEPeeRAHlgifLAFQYPIEIPgvsnadflrLAYNSKRKFQGLPELdpLEFLEIINEKLKLVGMDPSFlsrnvnEGFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 234 GGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPssELFELF--DKILLMAEGRVA 311
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKII 231
|
....
gi 577718259 312 FLGT 315
Cdd:CHL00131 232 KTGD 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
84-311 |
6.52e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 84 NRVKGVFCNERHIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAI-AFRSSKGVQISPSTIRMLNGHPVDAkeM 162
Cdd:PRK10982 244 NKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLfGIREKSAGTITLHGKKINNHNANEA--I 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 163 QARCAYVQQDDLFIGsLTAREHLIFQAMV-RMPRHMTQ-----KQKVQRVDQVIQDLSLGKC--QNTLIGvpgrvkGLSG 234
Cdd:PRK10982 322 NHGFALVTEERRSTG-IYAYLDIGFNSLIsNIRNYKNKvglldNSRMKSDTQWVIDSMRVKTpgHRTQIG------SLSG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 235 GERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRVA 311
Cdd:PRK10982 395 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII----SSEMPELLgitDRILVMSNGLVA 470
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
113-263 |
7.67e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIA--FRSSKGvQISpstirmLNGHPVDAKEMQARCAYVQQDDLFIGSLTAREHLIFQAM 190
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAglLHVESG-QIQ------IDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCG 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 191 V--RMPRHMTqkqkvqrvDQVIQDLSLGKCQNTLigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 263
Cdd:PRK13543 109 LhgRRAKQMP--------GSALAIVGLAGYEDTL------VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
114-318 |
8.69e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.20 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAIAfrsskGVQISPStirmlnghpvdakemqarcayvqqDDLFIGSLTARE--------HL 185
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIA-----GLEDITS------------------------GDLFIGEKRMNDvppaergvGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 186 IFQAMVRMPrHMT---------------QKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDP 250
Cdd:PRK11000 80 VFQSYALYP-HLSvaenmsfglklagakKEEINQRVNQVAEVLQLAHLLDR------KPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 251 PLLICDEPTSGLDSFMAhsvVQV---LKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK11000 153 SVFLLDEPLSNLDAALR---VQMrieISRLHKRlGRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
107-318 |
8.94e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 107 VSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRmLNGHPV---DAKEMQARCAYV--QQDDLFIgslta 181
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMA-----GLLPGSGSIQ-FAGQPLeawSAAELARHRAYLsqQQTPPFA----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 182 rehlifqamvrMP------RHMTQKQKVQRVDQVIQDL-SLGKCQNTLigvpGR-VKGLSGGE--RKRLAFA-----SEA 246
Cdd:PRK03695 84 -----------MPvfqyltLHQPDKTRTEAVASALNEVaEALGLDDKL----GRsVNQLSGGEwqRVRLAAVvlqvwPDI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 247 LTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELfDKILLMAEGRVAFLGTPGE 318
Cdd:PRK03695 149 NPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQGKLLASGRRDE 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
101-315 |
9.15e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFrsskgvQISPstirMLNGHPVdakeMQARCAYVQQDDlFIGSLT 180
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG------ELPP----RSDASVV----IRGTVAYVPQVS-WIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 AREHLIFQAMVRMPRHmtqkQKVQRVDQVIQDLSL--GKCQnTLIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEP 258
Cdd:PLN03130 695 VRDNILFGSPFDPERY----ERAIDVTALQHDLDLlpGGDL-TEIGERG--VNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 259 TSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpsSELFELFDKILLMAEGRVAFLGT 315
Cdd:PLN03130 768 LSALDAHVGRQVFDKCIKDELRGKTRVLVTNQ--LHFLSQVDRIILVHEGMIKEEGT 822
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
95-310 |
1.61e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.92 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 95 HIPAprkhllknvsgvaypGELLAVMGSSGAGKTTLLNAIAfrsskGVQiSPSTIRMLNGhpvdakemQARCAYVQQDdl 174
Cdd:PRK11247 34 HIPA---------------GQFVAVVGRSGCGKSTLLRLLA-----GLE-TPSAGELLAG--------TAPLAEARED-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 figsltarehlifqamVRMprhMTQKQKVQRVDQVIQDLSLG-------KCQNTL--IGVPGRVK----GLSGGERKRLA 241
Cdd:PRK11247 83 ----------------TRL---MFQDARLLPWKKVIDNVGLGlkgqwrdAALQALaaVGLADRANewpaALSGGQKQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 242 FASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRV 310
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHD-VSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
232-323 |
1.66e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.36 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVA 311
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHII 223
|
90
....*....|....*
gi 577718259 312 FLGTPGEA---VDFF 323
Cdd:PRK13643 224 SCGTPSDVfqeVDFL 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
104-318 |
2.17e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.99 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPVDA---KEMQARCAYVQQ--DDLFIGS 178
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMI-----GIEKVKSGEIFYNNQAITDdnfEKLRKHIGIVFQnpDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTArehliFQAMVRMPRHMTQKQKVQR-VDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDE 257
Cdd:PRK13648 100 IVK-----YDVAFGLENHAVPYDEMHRrVSEALKQVDMLERADY------EPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 258 PTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELfDKILLMAEGRVAFLGTPGE 318
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTPTE 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
90-318 |
3.51e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.30 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 90 FCNERHIPAP----RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLL---NAIAFRSSKGVQISPSTIRMLNGHPvDAKEM 162
Cdd:PRK13641 5 FENVDYIYSPgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLKPSSGTITIAGYHITPETGNK-NLKKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 163 QARCAYVQQ---DDLFigsltarEHLIFQAMVRMPRHM---TQKQKVQRVDQVIQdlslgkcqntlIGVPGRVKG----- 231
Cdd:PRK13641 84 RKKVSLVFQfpeAQLF-------ENTVLKDVEFGPKNFgfsEDEAKEKALKWLKK-----------VGLSEDLISkspfe 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVA 311
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGKLI 224
|
....*..
gi 577718259 312 FLGTPGE 318
Cdd:PRK13641 225 KHASPKE 231
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
96-322 |
3.75e-09 |
|
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: 56.56 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 96 IPAPRKHLLKNVSgVAYP-GELLAVMGSSGAGKTTLLNAIAFRSSKGVQISpstirmlnghpvdakemqARCAYVQQDDL 174
Cdd:cd03238 3 VSGANVHNLQNLD-VSIPlNVLVVVTGVSGSGKSTLVNEGLYASGKARLIS------------------FLPKFSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLtarehlifQAMVRMPrhmtqkqkvqrvdqvIQDLSLGKCQNTLigvpgrvkglSGGERKRLAFASEALTDPP--L 252
Cdd:cd03238 64 FIDQL--------QFLIDVG---------------LGYLTLGQKLSTL----------SGGELQRVKLASELFSEPPgtL 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 253 LICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPssELFELFDKILLMAEGRvaflGTPGEAVDF 322
Cdd:cd03238 111 FILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFGPGS----GKSGGKVVF 174
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
103-289 |
4.10e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskgVQISPSTIRML-NGHPVDA---KEMQARCAYVQQDDLFIGS 178
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA------SLISPTSGTLLfEGEDISTlkpEIYRQQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 lTAREHLIFQAMVRmprhmtqKQKVQRvDQVIQDLS-LGKCQNTLigvPGRVKGLSGGERKRLAFASEALTDPPLLICDE 257
Cdd:PRK10247 96 -TVYDNLIFPWQIR-------NQQPDP-AIFLDDLErFALPDTIL---TKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|...
gi 577718259 258 PTSGLDSFMAHSVVQVLKKL-SQKGKTVILTIH 289
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYvREQNIAVLWVTH 196
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
232-340 |
4.92e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.10 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRV 310
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHN-MDQVLRIADEVIVMHEGKV 229
|
90 100 110
....*....|....*....|....*....|
gi 577718259 311 AFLGTPGEavdFFSYIGATCPTNYNPADFY 340
Cdd:PRK13645 230 ISIGSPFE---IFSNQELLTKIEIDPPKLY 256
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
229-318 |
5.31e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.71 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 229 VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSeLFELFDKILLMAEG 308
Cdd:PRK13638 134 IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQG 212
|
90
....*....|
gi 577718259 309 RVAFLGTPGE 318
Cdd:PRK13638 213 QILTHGAPGE 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
114-293 |
7.98e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.20 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAI-AFrsskgVQISPSTIRMLnGHPVDAKEMQARCAYVQQDDLFIGSLTarehLIFQAMVR 192
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALmGF-----VRLASGKISIL-GQPTRQALQKNLVAYVPQSEEVDWSFP----VLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 193 MPR--HMTQKQKVQRVDQVIQDLSLGKCQntLIGVPGRVKG-LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHS 269
Cdd:PRK15056 103 MGRygHMGWLRRAKKRDRQIVTAALARVD--MVEFRHRQIGeLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180
....*....|....*....|....
gi 577718259 270 VVQVLKKLSQKGKTVILTIHQPSS 293
Cdd:PRK15056 181 IISLLRELRDEGKTMLVSTHNLGS 204
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
104-285 |
8.75e-09 |
|
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: 56.29 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLN-----------AIAFRSSKG----VQISPSTIRMLNGHPVdakemqarcAY 168
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKciygnylpdsgSILVRHDGGwvdlAQASPREILALRRRTI---------GY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 169 VQQddlFigsLTArehlifqamvrMPRhmtqkqkVQRVDQVIQDL---------SLGKCQNTL--IGVPGRVKGL----- 232
Cdd:COG4778 98 VSQ---F---LRV-----------IPR-------VSALDVVAEPLlergvdreeARARARELLarLNLPERLWDLppatf 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577718259 233 SGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVI 285
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
101-318 |
9.81e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIafrsSKGVQISPSTIRmlnghpVDAKEMqarcaYVQQDDLFIGSLT 180
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL----NRLIEIYDSKIK------VDGKVL-----YFGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 AREH--LIFQAMVRMPrHMT---------------QKQKVQR-VDQVIQDLSLGKCQNTLIGVPGrvKGLSGGERKRLAF 242
Cdd:PRK14246 88 LRKEvgMVFQQPNPFP-HLSiydniayplkshgikEKREIKKiVEECLRKVGLWKEVYDRLNSPA--SQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 243 ASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLsQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNP-QQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
97-360 |
1.05e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.12 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 97 PAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTT---LLNAIAFRSSkgvqiSPSTIRMLNGHPVDAKEM---QARCAYVQ 170
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDD-----NPNSKITVDGITLTAKTVwdiREKVGIVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 171 Q--DDLFIGSlTAREHLIFQAMVR-MPRhmtqKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEAL 247
Cdd:PRK13640 91 QnpDNQFVGA-TVGDDVAFGLENRaVPR----PEMIKIVRDVLADVGMLDYIDS------EPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 248 TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELfELFDKILLMAEGRVAFLGTPGE---AVDFFS 324
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEifsKVEMLK 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 577718259 325 YIGATCPTNYNPADFYVQVLAVVPgREVESRERIAK 360
Cdd:PRK13640 239 EIGLDIPFVYKLKNKLKEKGISVP-QEINTEEKLVQ 273
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
102-308 |
1.36e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 102 HLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAI--AFRSSKGvqispsTIrMLNGH------PVDAKEMQARCAYvqQDD 173
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLsgIHEPTKG------TI-TINNInynkldHKLAAQLGIGIIY--QEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFIGSLTAREHLIfqamvrMPRHMTQK---------QKVQRVDQVIQD-LSLGKCQNTLIGvpgrvkGLSGGERKRLAFA 243
Cdd:PRK09700 90 SVIDELTVLENLY------IGRHLTKKvcgvniidwREMRVRAAMMLLrVGLKVDLDEKVA------NLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 244 SEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEG 308
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDG 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
113-289 |
1.46e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.65 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIAfrsskGVQiSPSTIRML-NGHpvDAKEMQAR-CAYVQQDdlfIGSLTAREHLIFQAM 190
Cdd:PRK10908 27 PGEMAFLTGHSGAGKSTLLKLIC-----GIE-RPSAGKIWfSGH--DITRLKNReVPFLRRQ---IGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 191 V----RMPRHM---TQKQKVQRVDQVIQDLSL-GKCQNTLIGvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 262
Cdd:PRK10908 96 VydnvAIPLIIagaSGDDIRRRVSAALDKVGLlDKAKNFPIQ-------LSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180
....*....|....*....|....*..
gi 577718259 263 DSFMAHSVVQVLKKLSQKGKTVILTIH 289
Cdd:PRK10908 169 DDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
103-320 |
1.63e-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: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVA---YPGELLAVMGSSGAGKTTLLNAIA--FRSSKG---VQISPSTIRMLNGHPvDAKEMQARcaYV----Q 170
Cdd:TIGR03269 296 VVKAVDNVSlevKEGEIFGIVGTSGAGKTTLSKIIAgvLEPTSGevnVRVGDEWVDMTKPGP-DGRGRAKR--YIgilhQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 171 QDDLFIGSlTAREHLIFQAMVRMPRHMTQKQKVQRVDQViqDLSLGKCQNTLIGVPGRvkgLSGGERKRLAFASEALTDP 250
Cdd:TIGR03269 373 EYDLYPHR-TVLDNLTEAIGLELPDELARMKAVITLKMV--GFDEEKAEEILDKYPDE---LSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 251 PLLICDEPTSGLDSF----MAHSVVQVLKKLSQkgkTVILTIHQPSSELfELFDKILLMAEGRVAFLGTPGEAV 320
Cdd:TIGR03269 447 RIVILDEPTGTMDPItkvdVTHSILKAREEMEQ---TFIIVSHDMDFVL-DVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
100-318 |
2.28e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.95 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHL--LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVqISPSTIRML-NGHPV---DAKEMQARCAYVQQDD 173
Cdd:PRK15112 23 RQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLA-----GM-IEPTSGELLiDDHPLhfgDYSYRSQRIRMIFQDP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 lfIGSLTAREHL--IFQAMVRMPRHMTQKQKVQRVDQVIQDLSLgkcqntligVPGRVK----GLSGGERKRLAFASEAL 247
Cdd:PRK15112 97 --STSLNPRQRIsqILDFPLRLNTDLEPEQREKQIIETLRQVGL---------LPDHASyyphMLAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 248 TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPGE 318
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
99-289 |
2.46e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.25 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQispstiRMLNGhpvDAKEMQ-ARCAYVQQDDLFIG 177
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-----GVD------KDFNG---EARPQPgIKVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTAREHlIFQAMVRMprhmtqKQKVQRVDQVIQDLS--------LGKCQNTLIGV-----------------------P 226
Cdd:TIGR03719 82 TKTVREN-VEEGVAEI------KDALDRFNEISAKYAepdadfdkLAAEQAELQEIidaadawdldsqleiamdalrcpP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 227 G--RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAHSVVQVLKKLSQKGKTVILTIH 289
Cdd:TIGR03719 155 WdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTH 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
103-291 |
4.05e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.92 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIafrsSKGVQISP-STIR---MLNGHPV---DAKEMQARCAYVQQDDLF 175
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVF----NRLIELYPeARVSgevYLDGQDIfkmDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSLTAREHLIFQamVRMPRHMTQKQKVQ-RVDQVIQDLSL-GKCQNTLIGVPGRvkgLSGGERKRLAFASEALTDPPLL 253
Cdd:PRK14247 94 IPNLSIFENVALG--LKLNRLVKSKKELQeRVRWALEKAQLwDEVKDRLDAPAGK---LSGGQQQRLCIARALAFQPEVL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 577718259 254 ICDEPTSGLDSFMAHSVVQVLKKLsQKGKTVILTIHQP 291
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFP 205
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
89-318 |
5.57e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.71 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 89 VFCNERHIPAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTL---LNAIAFRSSKGVQISPSTIRMLNghpvDAKEMQAR 165
Cdd:PRK13633 11 SYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSEGKVYVDGLDTSDEE----NLWDIRNK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 166 CAYV-QQDDLFIGSLTAREHLIFQamvrmPRHM--TQKQKVQRVDQVIQDLSLGKCQNTLIGVpgrvkgLSGGERKRLAF 242
Cdd:PRK13633 87 AGMVfQNPDNQIVATIVEEDVAFG-----PENLgiPPEEIRERVDESLKKVGMYEYRRHAPHL------LSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 243 ASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELfDKILLMAEGRVAFLGTPGE 318
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHY-MEEAVEA-DRIIVMDSGKVVMEGTPKE 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
232-322 |
6.32e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.75 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVA 311
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHL-MDDVANYADFVYVLEKGKLV 224
|
90
....*....|....
gi 577718259 312 FLGTPGEA---VDF 322
Cdd:PRK13649 225 LSGKPKDIfqdVDF 238
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
178-328 |
7.26e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTAREHLIfqaMVRMPRHMTQKQKVQRVDQVIQDLSLGKcqntligVPGRVKG-LSGGERKRLAFASEALTDPPLLICD 256
Cdd:NF000106 100 SFSGRENLY---MIGR*LDLSRKDARARADELLERFSLTE-------AAGRAAAkYSGGMRRRLDLAASMIGRPAVLYLD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 257 EPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIH------QPSSELfELFDKILLMAEGRVAFLGT----------PGEAV 320
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQymeeaeQLAHEL-TVIDRGRVIADGKVDELKTkvggrtlqirPAHAA 248
|
....*...
gi 577718259 321 DFFSYIGA 328
Cdd:NF000106 249 ELDRMVGA 256
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
104-321 |
7.27e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQispstirMLNGHPVDAKEMQARCAYVQQDDlfiGSLTARE 183
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIA-----GVT-------MPNKGTVDIKGSAALIAISSGLN---GQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 184 HLIFQAMVrmpRHMTQKQKVQRVDQVIQDLSLGKcqntLIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 263
Cdd:PRK13545 105 NIELKGLM---MGLTKEKIKEIIPEIIEFADIGK----FIYQP--VKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 264 SFMAHSVVQVLKKLSQKGKTvILTIHQPSSELFELFDKILLMAEGRVAFLGTPGEAVD 321
Cdd:PRK13545 176 QTFTKKCLDKMNEFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
99-310 |
8.36e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.18 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIaFRSSKGVQISpSTIRMlNGHPVD----AKEMQARCAYVQQDdl 174
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSV-FGRSYGRNIS-GTVFK-DGKEVDvstvSDAIDAGLAYVTED-- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 figsltaREH--LIFQAMVRMPRHMTQKQKVQR---VDQVIQDLSLGKCQNTL-IGVPG---RVKGLSGGERKRLAFASE 245
Cdd:NF040905 346 -------RKGygLNLIDDIKRNITLANLGKVSRrgvIDENEEIKVAEEYRKKMnIKTPSvfqKVGNLSGGNQQKVVLSKW 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577718259 246 ALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRV 310
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI----SSELPELLgmcDRIYVMNEGRI 482
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
103-263 |
1.09e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskgvqispstirmlNGHPVDAKEMQ----ARCAYVQQD--DLFI 176
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-----------------GELEPDSGTVKwsenANIGYYAQDhaYDFE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTAREHlifqamvrmprhMTQKQKVQRVDQVIQDLsLGKCQNTLIGVPGRVKGLSGGERKRLAFASEALTDPPLLICD 256
Cdd:PRK15064 397 NDLTLFDW------------MSQWRQEGDDEQAVRGT-LGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
....*..
gi 577718259 257 EPTSGLD 263
Cdd:PRK15064 464 EPTNHMD 470
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
104-316 |
1.67e-07 |
|
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: 52.41 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIaFRSSK---------GVQISPstirmlnghpVDAKEMQARCAYVQQDD- 173
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILAL-FRFLEaeegkieidGIDIST----------IPLEDLRSSLTIIPQDPt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 174 LFIGSLtaREHL-IFQamvrmprHMTQkqkvqrvDQVIQDLSlgkcqntligVPGRVKGLSGGERKRLAFASEALTDPPL 252
Cdd:cd03369 93 LFSGTI--RSNLdPFD-------EYSD-------EEIYGALR----------VSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 253 LICDEPTSGLDSFMAHSVVQVLKKLSQKgkTVILTIHQPSSELFElFDKILLMAEGRVAFLGTP 316
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTN--STILTIAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
424-599 |
1.79e-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: 53.55 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 424 KVRLLQTTMVAVLIGLIFLGQQLTQVGVMNINGAIFLFLTNMTFQNSFATITVFTTELPVFMRETRSRLYRCdTYFLGKT 503
Cdd:pfam12698 132 LVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPL-QYWLGKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 504 IAELPLFLVVPFLFTAIAYpliGLRPGVDHFFTALALVTLVANVSTSFGYLISCACSSTSMALSVGPPVIIPFLLFGGFF 583
Cdd:pfam12698 211 LGDFLVGLLQLLIILLLLF---GIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGL 287
|
170
....*....|....*.
gi 577718259 584 LNSGSVPAYFKWLSYL 599
Cdd:pfam12698 288 FPLEDPPSFLQWIFSI 303
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
104-315 |
2.14e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTtlLNAIAF-----RSSKGVQISPSTIRMLNGHPVDAKEM-QARCAYVQQDDLfig 177
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKS--VTALALmrlleQAGGLVQCDKMLLRRRSRQVIELSEQsAAQMRHVRGADM--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 sltareHLIFQ-----------------AMVRMPRHMTQKQKVQRVDQVIQDLSLGKCQNTLIGVPGRvkgLSGGERKRL 240
Cdd:PRK10261 107 ------AMIFQepmtslnpvftvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ---LSGGMRQRV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 241 AFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGT 315
Cdd:PRK10261 178 MIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
97-290 |
2.52e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.27 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 97 PAPRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAF--RSSKGvQIspstirMLNGHPV---DAKEM-QARcayvQ 170
Cdd:PRK11153 14 GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLleRPTSG-RV------LVDGQDLtalSEKELrKAR----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 171 QddlfIGsltarehLIFQ-----------AMVRMPRHM--TQKQKV-QRVDQVIQDLSLGKCQNTLigvPGRvkgLSGGE 236
Cdd:PRK11153 83 Q----IG-------MIFQhfnllssrtvfDNVALPLELagTPKAEIkARVTELLELVGLSDKADRY---PAQ---LSGGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 237 RKRLAFAsEAL-TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQ 290
Cdd:PRK11153 146 KQRVAIA-RALaSNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHE 200
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
114-324 |
3.49e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTT---------------LLNAIAFRSSKGVQISPSTIRMLNGhpvdakemqARCAYVQQDDLfiGS 178
Cdd:PRK11022 33 GEVVGIVGESGSGKSVsslaimglidypgrvMAEKLEFNGQDLQRISEKERRNLVG---------AEVAMIFQDPM--TS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 179 LTAREHLIFQAMVRMPRHMTQKQKVQRvDQVIQDLslgkcqnTLIGVP---GRVK----GLSGGERKRLAFASEALTDPP 251
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKKTRR-QRAIDLL-------NQVGIPdpaSRLDvyphQLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 252 LLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAflgTPGEAVDFFS 324
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV---ETGKAHDIFR 243
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
104-311 |
3.60e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSG--VAYP-------GELLAVMGSSGAGKTTLLNAI--AFRSSKGvQIspstirMLNGHPVDAKE----MQARCAY 168
Cdd:PRK11288 260 LDGLKGpgLREPisfsvraGEIVGLFGLVGAGRSELMKLLygATRRTAG-QV------YLDGKPIDIRSprdaIRAGIML 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 169 VQQDDLFIG-----------SLTAREHLIFQAMVrmprhMTQKQKVQRVDQVIQDLSlgkcqntlIGVPGR---VKGLSG 234
Cdd:PRK11288 333 CPEDRKAEGiipvhsvadniNISARRHHLRAGCL-----INNRWEAENADRFIRSLN--------IKTPSReqlIMNLSG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 235 GERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTihqpSSELFE---LFDKILLMAEGRVA 311
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFV----SSDLPEvlgVADRIVVMREGRIA 475
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
232-289 |
3.72e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.68 E-value: 3.72e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 232 LSGGERKRLAFASEALT---DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIH 289
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
101-315 |
4.01e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.18 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIA--FRSSKGvqispsTIRmLNGHPVDAKEMQA---RCAYVQQDDLF 175
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMgyYPLTEG------EIR-LDGRPLSSLSHSVlrqGVAMVQQDPVV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 176 IGSltarehlIFQAMVRMPRHMTQKQKVQRVDQV-----IQDLSLGkcQNTLIGVPGrvKGLSGGERKRLAFASEALTDP 250
Cdd:PRK10790 427 LAD-------TFLANVTLGRDISEEQVWQALETVqlaelARSLPDG--LYTPLGEQG--NNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 251 PLLICDEPTSGLDSFMAHSVVQVLKKLSQkgKTVILTIHQPSSELFELfDKILLMAEGRVAFLGT 315
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEA-DTILVLHRGQAVEQGT 557
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
100-292 |
4.98e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.38 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLL---------NAIAfRSSKGVQISPSTIRMLNghpVDAKEMQARCAYVQ 170
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrllelNEEA-RVEGEVRLFGRNIYSPD---VDPIEVRREVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 171 QDDLFIGSLTAREH----LIFQAMVRmprhmTQKQKVQRVDQVIQDLSL-GKCQNTLIGVPGRvkgLSGGERKRLAFASE 245
Cdd:PRK14267 92 QYPNPFPHLTIYDNvaigVKLNGLVK-----SKKELDERVEWALKKAALwDEVKDRLNDYPSN---LSGGQRQRLVIARA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577718259 246 ALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLsQKGKTVILTIHQPS 292
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPA 209
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
100-263 |
6.12e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.27 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 100 RKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLnaiafRSSKGVqISPS--TIRmlnghpvdaKEMQARCAYVQQddlfig 177
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLV-----RVVLGL-VAPDegVIK---------RNGKLRIGYVPQ------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 sltaREHLIFQAMVRMPRHMTQKQKVQRVDqVIQDLSLGKCQNtLIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDE 257
Cdd:PRK09544 75 ----KLYLDTTLPLTVNRFLRLRPGTKKED-ILPALKRVQAGH-LIDAP--MQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
....*.
gi 577718259 258 PTSGLD 263
Cdd:PRK09544 147 PTQGVD 152
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
104-289 |
6.61e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIafrsskGVQISPSTIRMLNGHPVDAKEMQARCAyvqqddlfiGSLTARE 183
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNII------GGSLSPTVGKVDRNGEVSVIAISAGLS---------GQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 184 HLIFQaMVRMprHMTQKQKVQRVDQVIQDLSLGKcqntLIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 263
Cdd:PRK13546 105 NIEFK-MLCM--GFKRKEIKAMTPKIIEFSELGE----FIYQP--VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180
....*....|....*....|....*.
gi 577718259 264 SFMAHSVVQVLKKLSQKGKTVILTIH 289
Cdd:PRK13546 176 QTFAQKCLDKIYEFKEQNKTIFFVSH 201
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
233-348 |
7.86e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.65 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 233 SGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAF 312
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
90 100 110
....*....|....*....|....*....|....*..
gi 577718259 313 LGTpgeAVDFFsyigatcptnYNPADFY-VQVLAVVP 348
Cdd:PRK09473 243 YGN---ARDVF----------YQPSHPYsIGLLNAVP 266
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
166-304 |
1.93e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 166 CAYVQQDDLFIGSLTAREHLIFQAMV----RMPRHMTQKQKVQR------VDQVIQdlSLGKCQNTLIGVPGrvKGLSGG 235
Cdd:PTZ00265 1287 CDYNLKDLRNLFSIVSQEPMLFNMSIyeniKFGKEDATREDVKRackfaaIDEFIE--SLPNKYDTNVGPYG--KSLSGG 1362
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 236 ERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTI-HQPSSelFELFDKILL 304
Cdd:PTZ00265 1363 QKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIaHRIAS--IKRSDKIVV 1430
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
104-263 |
2.18e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 50.12 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVA---YPGELLAVMGSSGAGKTTLLNAIafrsskgVQISPST---IRmLNGHPV---DAKEMQARCAYVQ---Q 171
Cdd:COG4608 31 VKAVDGVSfdiRRGETLGLVGESGCGKSTLGRLL-------LRLEEPTsgeIL-FDGQDItglSGRELRPLRRRMQmvfQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 DDLfiGSLTAR--------EHLIFQAMVrmprhmTQKQKVQRVDQVIQdlslgkcqntligvpgRVkGL----------- 232
Cdd:COG4608 103 DPY--ASLNPRmtvgdiiaEPLRIHGLA------SKAERRERVAELLE----------------LV-GLrpehadryphe 157
|
170 180 190
....*....|....*....|....*....|...
gi 577718259 233 -SGGERKRLAFAsEAL-TDPPLLICDEPTSGLD 263
Cdd:COG4608 158 fSGGQRQRIGIA-RALaLNPKLIVCDEPVSALD 189
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
104-309 |
3.13e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQISPSTIRMLNGHPV---DAKE-MQARCAYVQQ-------- 171
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILS-----GNYQPDAGSILIDGQEMrfaSTTAaLAAGVAIIYQelhlvpem 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 172 ---DDLFIGSLTAREHLIfqamvrmprhmTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALT 248
Cdd:PRK11288 95 tvaENLYLGQLPHKGGIV-----------NRRLLNYEAREQLEHLGVDIDPDT------PLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577718259 249 DPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKtVILTIHQPSSELFELFDKILLMAEGR 309
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGR-VILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
232-318 |
3.61e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAFASE--ALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpsSELFELFDKILLMAE-- 307
Cdd:PRK00635 477 LSGGEQERTALAKHlgAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--EQMISLADRIIDIGPga 554
|
90
....*....|....*
gi 577718259 308 ----GRVAFLGTPGE 318
Cdd:PRK00635 555 gifgGEVLFNGSPRE 569
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
87-358 |
4.75e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 87 KGVFCNERhipaprkhLLKNVSGVAY---PGELLAVMGSSGAGKTTLLNAIAFrsskgvqISPSTI--RMLNGHPV---D 158
Cdd:PRK11308 19 RGLFKPER--------LVKALDGVSFtleRGKTLAVVGESGCGKSTLARLLTM-------IETPTGgeLYYQGQDLlkaD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 159 AKEMQARCAYVQ---QDDLfiGSLTAR--------EHLIFQamvrmprhmTQKQKVQRVDQVIQDLSlgkcqntligvpg 227
Cdd:PRK11308 84 PEAQKLLRQKIQivfQNPY--GSLNPRkkvgqileEPLLIN---------TSLSAAERREKALAMMA------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 228 RVkGL------------SGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSEL 295
Cdd:PRK11308 140 KV-GLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVV 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 296 FELFDKILLMAEGRVAFLGtPGEAVdfFSyigatcptnyNPADFYVQ-VLAVVPGREVE-SRERI 358
Cdd:PRK11308 219 EHIADEVMVMYLGRCVEKG-TKEQI--FN----------NPRHPYTQaLLSATPRLNPDdRRERI 270
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
289-344 |
5.19e-06 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 49.13 E-value: 5.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 289 HQPSSELFELFDK-ILLMAEGRVAFLGTPGEAVDFFSYIGATCPTNYNPADFYVQVL 344
Cdd:pfam19055 1 HQPSYTLFKMFDDlILLAKGGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDIL 57
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
101-310 |
5.69e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSgVAYPGE-LLAVMGSSGAGKTTLLNAIAFRSSKGVQISPSTIRMLNGHPV----DAKEMQARCAYV-QQDDL 174
Cdd:PRK14271 34 KTVLDQVS-MGFPARaVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIfnyrDVLEFRRRVGMLfQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 175 FIGSLTAREHLIFQAMVRMPRHMTQKQKVQRVDQV-IQDlslgKCQNTLIGVPGRvkgLSGGERKRLAFASEALTDPPLL 253
Cdd:PRK14271 113 FPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVgLWD----AVKDRLSDSPFR---LSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 254 ICDEPTSGLDSFMAHSVVQVLKKLSQKgKTVILTIHQpSSELFELFDKILLMAEGRV 310
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHN-LAQAARISDRAALFFDGRL 240
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
113-305 |
5.92e-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: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 113 PGELLAVMGSSGAGKTTLLNAIAfrsskgvqispstiRMLNghpvdakEMQARCAYVQQDDLFIGSLTAREHlifqamvr 192
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA--------------RELG-------PPGGGVIYIDGEDILEEVLDQLLL-------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 193 mprhmtqkqkvqrvdqviqdlslgkcqntlIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQ 272
Cdd:smart00382 52 ------------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577718259 273 ------VLKKLSQKGKTVILTIHQP----SSELFELFDKILLM 305
Cdd:smart00382 102 leelrlLLLLKSEKNLTVILTTNDEkdlgPALLRRRFDRRIVL 144
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
232-292 |
7.28e-06 |
|
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: 48.54 E-value: 7.28e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577718259 232 LSGGERKRLAFAS---EALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPS 292
Cdd:pfam13304 237 LSDGTKRLLALLAallSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
205-289 |
8.00e-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: 49.01 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 205 RVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTV 284
Cdd:COG1245 192 KLDELAEKLGLENILDR------DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYV 265
|
....*
gi 577718259 285 ILTIH 289
Cdd:COG1245 266 LVVEH 270
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
103-310 |
1.24e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 103 LLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGVQISPSTIRmLNGHPVDAKEMQAR-CAYVQQD--DLFIGSL 179
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVL-LDGKPVAPCALRGRkIATIMQNprSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLI--FQAMVRMPRhmtqkqkVQRVDQVIQDLSLGKcqntligvPGRVKGL-----SGGERKRLAFASEALTDPPL 252
Cdd:PRK10418 97 TMHTHARetCLALGKPAD-------DATLTAALEAVGLEN--------AARVLKLypfemSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 253 LICDEPTSGLDSFMAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRV 310
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHD-MGVVARLADDVAVMSHGRI 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
99-270 |
1.27e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 99 PRKHLLKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAfrsskGVQiSPStirmlNGhpvDAKEMQ-ARCAYVQQDDLFIG 177
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-----GVD-KEF-----EG---EARPAPgIKVGYLPQEPQLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 178 SLTAREHlIFQAMVRMprhmtqKQKVQRVDQVIQDLSL------------GKCQNTLIGVPG------------------ 227
Cdd:PRK11819 84 EKTVREN-VEEGVAEV------KAALDRFNEIYAAYAEpdadfdalaaeqGELQEIIDAADAwdldsqleiamdalrcpp 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 577718259 228 ---RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAHSV 270
Cdd:PRK11819 157 wdaKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESV 199
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
114-290 |
2.25e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.17 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAI--AFRSSKGVQISPSTIRMLNGHPVDAKEMQARCAYVQQDDLFIGSlTAREHLIFQAMV 191
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAIlgEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-TVEENITFGSPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 192 rmprhmtQKQKVQRVDQV------IQDLSLGkcQNTLIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 265
Cdd:cd03290 106 -------NKQRYKAVTDAcslqpdIDLLPFG--DQTEIGERG--INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180
....*....|....*....|....*..
gi 577718259 266 MAHSVVQ--VLKKLSQKGKTVILTIHQ 290
Cdd:cd03290 175 LSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
228-286 |
3.07e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 3.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 577718259 228 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVIL 286
Cdd:PRK10938 132 RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
108-289 |
3.64e-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: 47.09 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 108 SGVAYPGELLAVMGSSGAGKTTLlnaiafrsskgvqispstIRMLNG--HPVDAK-EMQARCAY----VQQDdlfiGSLT 180
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTF------------------AKILAGvlKPDEGEvDEDLKISYkpqyISPD----YDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 181 AREHLIFQAMVRMPRHMTQkqkvqrvDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTS 260
Cdd:COG1245 418 VEEFLRSANTDDFGSSYYK-------TEIIKPLGLEKLLDK------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190
....*....|....*....|....*....|
gi 577718259 261 GLDSFMAHSVVQVLKKLS-QKGKTVILTIH 289
Cdd:COG1245 485 HLDVEQRLAVAKAIRRFAeNRGKTAMVVDH 514
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
97-289 |
7.49e-05 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 44.29 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 97 PAPRKHLLKnvsGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGVQispstirmLNGHPVDAKemQARCAYVQQDDlfi 176
Cdd:pfam13481 19 PPPRRWLIK---GLLPAGGLGLLAGAPGTGKTTLALDLAAAVATGKP--------WLGGPRVPE--QGKVLYVSAEG--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 177 GSLTAREHLIfqamvRMPRHMTQKQKVQRVDQViQDLSLGKcqntligvPGRVKGLSGGERKRLAFASEALTDPPLLICD 256
Cdd:pfam13481 83 PADELRRRLR-----AAGADLDLPARLLFLSLV-ESLPLFF--------LDRGGPLLDADVDALEAALEEVEDPDLVVID 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 577718259 257 --EPTSGLDSFMAHSVVQVLKKLS----QKGKTVILTIH 289
Cdd:pfam13481 149 plARALGGDENSNSDVGRLVKALDrlarRTGATVLLVHH 187
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
114-328 |
8.42e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.22 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAIAfrsskGV-QISPSTIRmLNGHPVDAKEMQAR-CAYVQQDDLFIGSLTAREHLIFQAMV 191
Cdd:PRK11650 30 GEFIVLVGPSGCGKSTLLRMVA-----GLeRITSGEIW-IGGRVVNELEPADRdIAMVFQNYALYPHMSVRENMAYGLKI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 192 R-MPRHMTQkqkvQRVDQVIQDLSLGKcqnTLIGVPgrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAHSV 270
Cdd:PRK11650 104 RgMPKAEIE----ERVAEAARILELEP---LLDRKP---RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD---AKLR 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 271 VQV---LKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPGE-----AVDFF-SYIGA 328
Cdd:PRK11650 171 VQMrleIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEvyekpASTFVaSFIGS 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
104-309 |
8.42e-05 |
|
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: 45.59 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 104 LKNVSGVAYPGELLAVMGSSGAGKTTLLNAIAFRSSKGvqiSPSTIRMLNGHPVDAKEM----QARCAYVQQDDLFIGSL 179
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG---TWDGEIYWSGSPLKASNIrdteRAGIVIIHQELTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 180 TAREHLIFQAMVRMP-RHMTQKQKVQRVDQVIQDLSLGKCQNTLigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEP 258
Cdd:TIGR02633 94 SVAENIFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTR-----PVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577718259 259 TSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGR 309
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAHGVACVYISHK-LNEVKAVCDTICVIRDGQ 218
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
226-317 |
1.01e-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: 43.71 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 226 PGRVKgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLm 305
Cdd:cd03222 67 PQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV- 144
|
90
....*....|..
gi 577718259 306 aegrvaFLGTPG 317
Cdd:cd03222 145 ------FEGEPG 150
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
93-289 |
1.12e-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: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 93 ERHIPAP----------------RKHLLKNVSgVAYP-GELLAVMGSSGAGKTTLLNAIAFRS----------------- 138
Cdd:TIGR00630 597 RKKIEVPaerrpgngkfltlkgaRENNLKNIT-VSIPlGLFTCITGVSGSGKSTLINDTLYPAlanrlngaktvpgryts 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 139 -------SKGVQIS-----------PST-------IRMLNGHPVDAKEMQ------------ARCAYVQQD--------- 172
Cdd:TIGR00630 676 ieglehlDKVIHIDqspigrtprsnPATytgvfdeIRELFAETPEAKVRGytpgrfsfnvkgGRCEACQGDgvikiemhf 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 173 --DLFI------GSLTAREHL--------IFQAMvrmprHMTQKQ---------KVQRVDQVIQDLSLGKCQntlIGVPg 227
Cdd:TIGR00630 756 lpDVYVpcevckGKRYNRETLevkykgknIADVL-----DMTVEEayeffeavpSISRKLQTLCDVGLGYIR---LGQP- 826
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577718259 228 rVKGLSGGERKRLAFASEAL---TDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIH 289
Cdd:TIGR00630 827 -ATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
205-289 |
1.14e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 205 RVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSqKGKTV 284
Cdd:PRK13409 192 KLDEVVERLGLENILDR------DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYV 264
|
....*
gi 577718259 285 ILTIH 289
Cdd:PRK13409 265 LVVEH 269
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
114-320 |
1.50e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.21 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 114 GELLAVMGSSGAGKTTLLNAIAfrsskgVQISPSTIRM-LNGHPVD---AKEMQARCAYVQQD-----DLFIGSLTAREH 184
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLS------RLMTPAHGHVwLDGEHIQhyaSKEVARRIGLLAQNattpgDITVQELVARGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 185 LIFQAMVRMPRhmtqKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 264
Cdd:PRK10253 107 YPHQPLFTRWR----KEDEEAVTKAMQATGITHLADQ------SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577718259 265 FMAHSVVQVLKKLS-QKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPGEAV 320
Cdd:PRK10253 177 SHQIDLLELLSELNrEKGYTLAAVLHD-LNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
229-263 |
2.02e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 2.02e-04
10 20 30
....*....|....*....|....*....|....*
gi 577718259 229 VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 263
Cdd:PRK11147 438 VKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
117-315 |
2.50e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 117 LAVMGSSGAGKTTLLNAIA--FRSSKGVQISPSTIRM--LNGHPVDAKEMQ-------ARC---AYVQQDDLFIGSLTAR 182
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISgeLQPSSGTVFRSAKVRMavFSQHHVDGLDLSsnpllymMRCfpgVPEQKLRAHLGSFGVT 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 183 EHLIFQAMVRmprhmtqkqkvqrvdqviqdlslgkcqntligvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 262
Cdd:PLN03073 618 GNLALQPMYT---------------------------------------LSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577718259 263 DSFMAHSVVQVLkKLSQKGktvILTIHQPSSELFELFDKILLMAEGRVA-FLGT 315
Cdd:PLN03073 659 DLDAVEALIQGL-VLFQGG---VLMVSHDEHLISGSVDELWVVSEGKVTpFHGT 708
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
121-303 |
3.42e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 121 GSSGAGKTTLLNAIAF-------RSSKGVQISPSTIRmlnghpvdakemqarcayvqqddlfIGSLTAREHLIFQamVRM 193
Cdd:cd03240 29 GQNGAGKTTIIEALKYaltgelpPNSKGGAHDPKLIR-------------------------EGEVRAQVKLAFE--NAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 194 PRHMTQKQKVQRVDQVI---QDLSlgkcqNTLIgvPGRVKGLSGGERK------RLAFAsEALTDP-PLLICDEPTSGLD 263
Cdd:cd03240 82 GKKYTITRSLAILENVIfchQGES-----NWPL--LDMRGRCSGGEKVlasliiRLALA-ETFGSNcGILALDEPTTNLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 577718259 264 SF-MAHSVVQVLKK-LSQKGKTVILTIHQPssELFELFDKIL 303
Cdd:cd03240 154 EEnIEESLAEIIEErKSQKNFQLIVITHDE--ELVDAADHIY 193
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
188-263 |
4.49e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 188 QAMVR--MPRHMTQK--QKVQRVDQVIQDLSLGKCQNTLI---GVPGRVKGLSGGERK------RLAFASEALTDPPLLI 254
Cdd:PRK01156 751 PAMIRksASQAMTSLtrKYLFEFNLDFDDIDVDQDFNITVsrgGMVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLI 830
|
....*....
gi 577718259 255 CDEPTSGLD 263
Cdd:PRK01156 831 MDEPTAFLD 839
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
232-318 |
4.57e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAFASE---ALTDpPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPssELFELFDKILLMAE- 307
Cdd:TIGR00630 489 LSGGEAQRIRLATQigsGLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDE--DTIRAADYVIDIGPg 565
|
90
....*....|....*.
gi 577718259 308 -----GRVAFLGTPGE 318
Cdd:TIGR00630 566 agehgGEVVASGTPEE 581
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
232-291 |
5.27e-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: 41.86 E-value: 5.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 232 LSGGERKRLAFASE---ALTDPpLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQP 291
Cdd:cd03270 138 LSGGEAQRIRLATQigsGLTGV-LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
232-263 |
5.55e-04 |
|
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: 43.13 E-value: 5.55e-04
10 20 30
....*....|....*....|....*....|..
gi 577718259 232 LSGGERKRLAFASEALTDPPLLICDEPTSGLD 263
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
228-289 |
6.21e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 6.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577718259 228 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAHSVVQVLKKLSQKGKTVILTIH 289
Cdd:PLN03073 341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
197-289 |
1.01e-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: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 197 MTQKQKVQRVDQVIQDLSLGKCQNTligvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKK 276
Cdd:cd03236 111 LKKKDERGKLDELVDQLELRHVLDR------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRE 184
|
90
....*....|...
gi 577718259 277 LSQKGKTVILTIH 289
Cdd:cd03236 185 LAEDDNYVLVVEH 197
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
232-338 |
1.32e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 41.18 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGK--TVILTIHQPSSELFELFDKILLMAEGR 309
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSEltMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
90 100
....*....|....*....|....*....
gi 577718259 310 VaflgtpGEAVDFfsyiGATCPTNYNPAD 338
Cdd:PRK14258 231 I------GQLVEF----GLTKKIFNSPHD 249
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
232-285 |
2.04e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 2.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 232 LSGGERKRLAFASEaL----TDPPLLICDEPTSGLdsfmaHS-----VVQVLKKLSQKGKTVI 285
Cdd:COG0178 827 LSGGEAQRVKLASE-LskrsTGKTLYILDEPTTGL-----HFhdirkLLEVLHRLVDKGNTVV 883
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
101-263 |
2.40e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 40.41 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 101 KHLLKNVSGVAYPGELLAVMGSSGAGKTTLLnaiafRS-------SKGVQISpSTIRmLNGHP-----VDAKEMQARCAY 168
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLL-----RClnrmndlIPGARVE-GEIL-LDGEDiydpdVDVVELRRRVGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 169 V-QQDDLFIGSltarehlIFQAMVRMPRHMTQKQKvQRVDQVIQDlSLGKCqntliGVPGRVK--------GLSGGERKR 239
Cdd:COG1117 97 VfQKPNPFPKS-------IYDNVAYGLRLHGIKSK-SELDEIVEE-SLRKA-----ALWDEVKdrlkksalGLSGGQQQR 162
|
170 180
....*....|....*....|....*
gi 577718259 240 LAFAsEAL-TDPPLLICDEPTSGLD 263
Cdd:COG1117 163 LCIA-RALaVEPEVLLMDEPTSALD 186
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
229-303 |
2.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 229 VKGLSGGERK------RLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQpssELFELFDKI 302
Cdd:COG4717 556 VEELSRGTREqlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHE---ELVELFQEE 632
|
.
gi 577718259 303 L 303
Cdd:COG4717 633 G 633
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
232-287 |
4.00e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.77 E-value: 4.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 577718259 232 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILT 287
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT 207
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
232-318 |
5.56e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.40 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577718259 232 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVA 311
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
....*..
gi 577718259 312 FLGTPGE 318
Cdd:PRK15093 239 ETAPSKE 245
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
114-135 |
6.18e-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: 38.53 E-value: 6.18e-03
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
228-289 |
8.87e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.41 E-value: 8.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577718259 228 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAHSVVQVLKKLS-QKGKTVILTIH 289
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDH 512
|
|
| |
