|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
67-665 |
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: 871.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 67 ATLVWRDLCVYTNVGGSGQR----------------MKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTV 130
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGSWkqlvsrlrgcfcrerpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 131 VQGDILINGRRIG-PFMHRISGYVYQDDLFLGSLTVLEHLNFMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGS 209
Cdd:TIGR00955 81 GSGSVLLNGMPIDaKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 210 GDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFNNVMLL 289
Cdd:TIGR00955 161 PGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 290 ADGRVAFTGSPQHALSFFANHGYYCPEAYNPADFLIGVLATDPGYEQASQRSAQHLCDQFAVSSAAKQRDMLVNLEIHMA 369
Cdd:TIGR00955 241 AEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENESRERIEKICDSFAVSDIGRDMLVNTNLWSGKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 370 qsGNFPFDTEVESFRG--VAWYKRFHVVWLRASLTLLRDPTIQWLRFIQKIAMAFIIGACFAGtTEPSQLGVQAVQGALF 447
Cdd:TIGR00955 321 --GGLVKDSENMEGIGynASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLG-QGLTQKGVQNINGALF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 448 IMISENTYHPMYSVLNLFPQGFPLFMRETRSGLYSTGQYYAANILALLPGMIIEPLIFVIICYWLTGLRSTFYAFGVTAM 527
Cdd:TIGR00955 398 LFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 528 CVVLVMNVATACGCFFSTAFNSVPLAMAYLVPLDYIFMITSGIFIQVNSLPVAFWWTQFLSWMLYANEAMTAAQWSGVQN 607
Cdd:TIGR00955 478 LVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDN 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 608 ITCFQESADLPCFHTGQDVLDKYSFNESNVYRNLLAMVGLYFGFHLLGYYCLWRRARK 665
Cdd:TIGR00955 558 IECTSANTTGPCPSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRR 615
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
88-661 |
7.99e-80 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 266.75 E-value: 7.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQpAGTVVQGDILINGRRIGPFMHRISGYVYQDDLFLGSLTVLE 167
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI-QGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 168 HLNFMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSGDDKKVlSGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGI-SGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 248 SYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFNNVMLLADGRVAFTGSPQHALSFFANHGYYCPEAYNPADFLI-- 325
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLdl 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 326 --GVLATDPGYEQASQRSAQHLCDQFAVSSAAKQRDMlVNLEIHMAQSGNFPFDTEVESFRG------VAWYKRFHVVwL 397
Cdd:PLN03211 319 anGVCQTDGVSEREKPNVKQSLVASYNTLLAPKVKAA-IEMSHFPQANARFVGSASTKEHRSsdrisiSTWFNQFSIL-L 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 398 RASLTLLRDPTIQWLRFIQKIAMAFIIGACFAGTtepSQLGVQAVQGALFIMISENTYHPMYSVLNLFPQGFPLFMRETR 477
Cdd:PLN03211 397 QRSLKERKHESFNTLRVFQVIAAALLAGLMWWHS---DFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 478 SGLYSTGQYYAANILALLPGMIIEPLIFVIICYWLTGLRSTFYAFGVTAMCVVLVMNVATACGCFFSTAFNSVPLAMAYL 557
Cdd:PLN03211 474 SGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIV 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 558 VPLDYIFMITSGIFiqVNSLPVAFWWTQFLSWMLYANEAMTAAQWSGVQNIT----CFQESA--DLPCFHTGQDVLDKYS 631
Cdd:PLN03211 554 TVTMLAFVLTGGFY--VHKLPSCMAWIKYISTTFYSYRLLINVQYGEGKRISsllgCSLPHGsdRASCKFVEEDVAGQIS 631
|
570 580 590
....*....|....*....|....*....|
gi 17647959 632 FNESnvyrnLLAMVGLYFGFHLLGYYCLWR 661
Cdd:PLN03211 632 PATS-----VSVLIFMFVGYRLLAYLALRR 656
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
57-610 |
1.18e-70 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 250.03 E-value: 1.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 57 YSKWSPTEQG-ATLVWRDLCvYTnVGGSGQRmKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTVVQGDI 135
Cdd:TIGR00956 747 DEKDMEKESGeDIFHWRNLT-YE-VKIKKEK-RVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDR 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 136 LINGRRIGPFMHRISGYVYQDDLFLGSLTVLEHLNFMAHLRLDRRVSKEER-RLI--IKELLERTGLLSAAQTRIGSGdd 212
Cdd:TIGR00956 824 LVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKmEYVeeVIKLLEMESYADAVVGVPGEG-- 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 213 kkvLSGGERKRLAFAVELLNNP-VILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFNNVMLLAD 291
Cdd:TIGR00956 902 ---LNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQK 978
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 292 G-RVAFTG----SPQHALSFFANHG-YYCPEAYNPADFLIGVLATDPGyEQASQRSAQHlcdqFAVSSAAKQRDMLVN-L 364
Cdd:TIGR00956 979 GgQTVYFGdlgeNSHTIINYFEKHGaPKCPEDANPAEWMLEVIGAAPG-AHANQDYHEV----WRNSSEYQAVKNELDrL 1053
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 365 EIHMAQSGNFPFDTEVESFRGVAWYKRFHVVWlRASLTLLRDPTIQWLRFIQKIAMAFIIGACF--AGTtepSQLGVQAV 442
Cdd:TIGR00956 1054 EAELSKAEDDNDPDALSKYAASLWYQFKLVLW-RTFQQYWRTPDYLYSKFFLTIFAALFIGFTFfkVGT---SLQGLQNQ 1129
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 443 QGALFIMI-----SENTYHPMY-SVLNLFpqgfplFMRETRSGLYSTGQYYAANILALLPGMIIEPLIFVIICYWLTGLR 516
Cdd:TIGR00956 1130 MFAVFMATvlfnpLIQQYLPPFvAQRDLY------EVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFY 1203
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 517 STFYAFGVTAMCVVLVMNVATACGCFFST------AFNSVPLAMAYLVPLDYIFMIT-SGIFIQVNSLPvAFW-WTQFLS 588
Cdd:TIGR00956 1204 WNASKTGQVHERGVLFWLLSTMFFLYFSTlgqmviSFNPNADNAAVLASLLFTMCLSfCGVLAPPSRMP-GFWiFMYRCS 1282
|
570 580
....*....|....*....|..
gi 17647959 589 WMLYANEAMTAAQWSGVQnITC 610
Cdd:TIGR00956 1283 PFTYLVQALLSTGLADVP-VTC 1303
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
66-298 |
2.32e-68 |
|
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: 221.66 E-value: 2.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 66 GATLVWRDLCVYTNvGGSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTVvQGDILINGRRIGPF 145
Cdd:cd03213 1 GVTLSFRNLTVTVK-SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV-SGEVLINGRPLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 146 MHR-ISGYVYQDDLFLGSLTVLEHLNFMAHLRldrrvskeerrliikellertgllsaaqtrigsgddkkVLSGGERKRL 224
Cdd:cd03213 79 SFRkIIGYVPQDDILHPTLTVRETLMFAAKLR--------------------------------------GLSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647959 225 AFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFNNVMLLADGRVAFTG 298
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
88-298 |
4.09e-67 |
|
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: 219.45 E-value: 4.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTVVQGDILINGRRIGPF-MHRISGYVYQDDLFLGSLTVL 166
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDqFQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 EHLNFMAHLRLDRRVSKEERrliiKELLERTGLLSAAQTRIGsGDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGL 246
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIR----KKRVEDVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17647959 247 DSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFNNVMLLADGRVAFTG 298
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
66-292 |
6.29e-61 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 201.70 E-value: 6.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 66 GATLVWRDLCvYTnVGGSGQRmKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGtVVQGDILINGRRIGPF 145
Cdd:cd03232 1 GSVLTWKNLN-YT-VPVKGGK-RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAG-VITGEILINGRPLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 146 MHRISGYVYQDDLFLGSLTVLEHLNFMAHLRldrrvskeerrliikellertGllsaaqtrigsgddkkvLSGGERKRLA 225
Cdd:cd03232 77 FQRSTGYVEQQDVHSPNLTVREALRFSALLR---------------------G-----------------LSVEQRKRLT 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 226 FAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFNNVMLLADG 292
Cdd:cd03232 119 IGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
85-604 |
1.17e-52 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 196.48 E-value: 1.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 85 QRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfrqpaGTVVQGDILINGR----RIGP--FMHRISG---YVYQ 155
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA-----SNTDGFHIGVEGVitydGITPeeIKKHYRGdvvYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 156 DDLFLGSLTVLEHLNFMAHLRLDRR----VSKEERRLIIKELLERT-GLLSAAQTRIGSgDDKKVLSGGERKRLAFAVEL 230
Cdd:TIGR00956 146 TDVHFPHLTVGETLDFAARCKTPQNrpdgVSREEYAKHIADVYMATyGLSHTRNTKVGN-DFVRGVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 231 LNNPVILFCDEPTTGLDSYSAQQLVATLYELAQ-KGTTILCTIHQPSSQLFDNFNNVMLLADGRVAFTGSPQHALSFFAN 309
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 310 HGYYCPEAYNPADFLIGVlaTDP-------GYEQASQRSAQHLCDQFAVSSAAKQ--RDMLVNL-------------EIH 367
Cdd:TIGR00956 305 MGFKCPDRQTTADFLTSL--TSPaerqikpGYEKKVPRTPQEFETYWRNSPEYAQlmKEIDEYLdrcsesdtkeayrESH 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 368 MA-QSGNfpfdTEVESFRGVAWYKRFHVVWLRASLTLLRDPTIQWLRFIQKIAMAFIIGACFAgTTEPSQLGVQAVQGAL 446
Cdd:TIGR00956 383 VAkQSKR----TRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFY-NLPKNTSDFYSRGGAL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 447 FIMISENTYHPMYSVLNLFpQGFPLFMRETRSGLYSTGQYYAANILALLPGMIIEPLIFVIICYWLTGLRST----FYAF 522
Cdd:TIGR00956 458 FFAILFNAFSSLLEIASMY-EARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTagrfFFYL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 523 GVTAMCvVLVMN-----VATACgcffstafNSVPLAMAYLVPLDYIFMITSGIFIQVNSLPVAFWWTQFLSWMLYANEAM 597
Cdd:TIGR00956 537 LILFIC-TLAMShlfrsIGAVT--------KTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESL 607
|
....*..
gi 17647959 598 TAAQWSG 604
Cdd:TIGR00956 608 MVNEFHG 614
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
95-592 |
1.30e-52 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 196.61 E-value: 1.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 95 TGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGtVVQGDILING--RRIGPFMhRISGYVYQDDLFLGSLTVLEHLNFM 172
Cdd:PLN03140 900 TGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGG-YIEGDIRISGfpKKQETFA-RISGYCEQNDIHSPQVTVRESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 173 AHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIG----SGddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDS 248
Cdd:PLN03140 978 AFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGlpgvTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 249 YSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFNNVMLLA-DGRVAFTG----SPQHALSFF-ANHGY-YCPEAYNPA 321
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSGplgrNSHKIIEYFeAIPGVpKIKEKYNPA 1132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 322 DFLIGVLATdpgyeQASQRSAQHLCDQFAVSSAAKQRDMLVN-LEIHMAQSGNFPFDTEvesFRGVAWYKRFHVVWlRAS 400
Cdd:PLN03140 1133 TWMLEVSSL-----AAEVKLGIDFAEHYKSSSLYQRNKALVKeLSTPPPGASDLYFATQ---YSQSTWGQFKSCLW-KQW 1203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 401 LTLLRDPTIQWLRFIQKIAMAFIIGACF--AGTTEPSQLGVQAVQGA-----LFIMISE-NTYHPMYSVLNlfpqgfPLF 472
Cdd:PLN03140 1204 WTYWRSPDYNLVRFFFTLAAALMVGTIFwkVGTKRSNANDLTMVIGAmyaavLFVGINNcSTVQPMVAVER------TVF 1277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 473 MRETRSGLYSTGQYYAANILALLPGMIIEPLIFVIICYWLTGLRST----FYAFGVT-----------AMCVVLVMNVAT 537
Cdd:PLN03140 1278 YRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTaakfFWFYFISffsflyftyygMMTVSLTPNQQV 1357
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 538 AcgCFFSTAFNSvplamaylvpldyIFMITSGIFIQVNSLP---VAFWWTQFLSWMLY 592
Cdd:PLN03140 1358 A--AIFAAAFYG-------------LFNLFSGFFIPRPKIPkwwVWYYWICPVAWTVY 1400
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
88-301 |
3.21e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.39 E-value: 3.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIGP----FMHRIsGYVYQDDLFLGS 162
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLgLLRPTS----GEVRVLGEDVARdpaeVRRRI-GYVPQEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 163 LTVLEHLNFMAHLRldrRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:COG1131 88 LTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT------LSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 243 TTGLDSYSAQQLVATLYELAQKGTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTGSPQ 301
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEeaERLCD---RVAIIDKGRIVADGTPD 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
88-305 |
6.67e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.47 E-value: 6.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPagtvVQGDILINGRRIGPFMHRIsGYVYQDDLFLGS--LT 164
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILgLLPP----TSGTVRLFGKPPRRARRRI-GYVPQRAEVDWDfpIT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 165 VLE--HLNFMAHLRLDRRVSKEERRlIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:COG1121 94 VRDvvLMGRYGRRGLFRRPSRADRE-AVDEALERVGLEDLADRPIGE------LSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647959 243 TTGLDSYSAQQLVATLYELAQKGTTILCTIHQPsSQLFDNFNNVMLLADGRVAFtGSPQHALS 305
Cdd:COG1121 167 FAGVDAATEEALYELLRELRREGKTILVVTHDL-GAVREYFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
395-600 |
3.50e-39 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 143.18 E-value: 3.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 395 VWLRASLTLLRDPTIQWLRFIQKIAMAFIIGACFAGTtePSQLGVQAVQGALFIMISENTYHPMYSVLNLFPQGFPLFMR 474
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNL--GNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 475 ETRSGLYSTGQYYAANILALLPGMIIEPLIFVIICYWLTGLRSTFYAFGVTAMCVVLVMNVATACGCFFSTAFNSVPLAM 554
Cdd:pfam01061 79 ELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17647959 555 AYLVPLDYIFMITSGIFIQVNSLPVAFWWTQFLSWMLYANEAMTAA 600
Cdd:pfam01061 159 QLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
84-302 |
2.11e-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: 138.79 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 84 GQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqGDILINGRRIGPFMHRIS---GYVYQDDLFL 160
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS---GTAYINGYSIRTDRKAARqslGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSLTVLEHLNFMAHLRldrRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:cd03263 88 DELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRART------LSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647959 241 EPTTGLDSYSAQQLVATLYELaQKGTTILCTIHqpSSQLFDNF-NNVMLLADGRVAFTGSPQH 302
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEV-RKGRSIILTTH--SMDEAEALcDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
88-298 |
2.06e-36 |
|
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: 135.74 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIGPFMHRIsGYVYQDDLFLGS--LT 164
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgLLKPT----SGSIRVFGKPLEKERKRI-GYVPQRRSIDRDfpIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 165 VLE--HLNFMAHLRLDRRVSKEERRLIIkELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:cd03235 87 VRDvvLMGLYGHKGLFRRLSKADKAKVD-EALERVGLSELADRQIGE------LSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 243 TTGLDSYSAQQLVATLYELAQKGTTILCTIHQPsSQLFDNFNNVMLLaDGRVAFTG 298
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDL-GLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
82-294 |
2.51e-36 |
|
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: 135.70 E-value: 2.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 82 GSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQpagTVVQGDILINGRRIgpfmHRIS----------- 150
Cdd:cd03255 11 GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLD---RPTSGEVRVDGTDI----SKLSekelaafrrrh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 151 -GYVYQDDLFLGSLTVLEhlNFMAHLRLdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVE 229
Cdd:cd03255 84 iGFVFQSFNLLPDLTALE--NVELPLLL-AGVPKKERRERAEELLERVGLGDRLNHYPSE------LSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 230 LLNNPVILFCDEPTTGLDSYSAQQLVATLYELA-QKGTTILCTIHQPssQLFDNFNNVMLLADGRV 294
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
84-293 |
8.71e-36 |
|
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: 134.13 E-value: 8.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 84 GQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPagtvVQGDILINGRRIGPF----MHRISGYVYQ--D 156
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNgLLGP----TSGEVLVDGKDLTKLslkeLRRKVGLVFQnpD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 157 DLFLGSlTVLEHLNF-MAHLRLDRrvskEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPV 235
Cdd:cd03225 86 DQFFGP-TVEEEVAFgLENLGLPE----EEIEERVEEALELVGLEGLRDRSPFT------LSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 236 ILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPsSQLFDNFNNVMLLADGR 293
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
82-294 |
7.43e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.70 E-value: 7.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 82 GSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIGPF---------MHRIsG 151
Cdd:COG1136 15 GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGgLDRPT----SGEVLIDGQDISSLserelarlrRRHI-G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 152 YVYQDDLFLGSLTVLEhlNFMAHLRLdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELL 231
Cdd:COG1136 90 FVFQFFNLLPELTALE--NVALPLLL-AGVSRKERRERARELLERVGLGDRLDHRPSQ------LSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647959 232 NNPVILFCDEPTTGLDSYSAQQLVATLYELA-QKGTTILCTIHQPssQLFDNFNNVMLLADGRV 294
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDGRI 222
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
90-602 |
1.18e-34 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 141.52 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTVVQGDILINGRRIGPFMHR-ISGYVYQDDLFLGSLTVLEH 168
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRkTSAYISQNDVHVGVMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 169 LNFMAHLR--------LDRRVSKEERRLIIKE-----------------------LLERTGLLSAAQTRIGSgDDKKVLS 217
Cdd:PLN03140 260 LDFSARCQgvgtrydlLSELARREKDAGIFPEaevdlfmkatamegvksslitdyTLKILGLDICKDTIVGD-EMIRGIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 218 GGERKRLAFAvELLNNPV-ILFCDEPTTGLDSYSAQQLVATLYELAQ-KGTTILCTIHQPSSQLFDNFNNVMLLADGRVA 295
Cdd:PLN03140 339 GGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLSEGQIV 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 296 FTGSPQHALSFFANHGYYCPEAYNPADFLIGVLATDPGYEQASQRSAQHLCdqFAVSSAAKQ-RDMLVNLEIHMAQSgnF 374
Cdd:PLN03140 418 YQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRY--ISVSEFAERfKSFHVGMQLENELS--V 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 375 PFDtEVESFRGVAWYKRFHV--------VWLRASLTLLRDPTIQWLRFIQKIAMAFIIGACFAGT---TEPSQLGVQAVQ 443
Cdd:PLN03140 494 PFD-KSQSHKAALVFSKYSVpkmellkaCWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTemhTRNEEDGALYIG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 444 GALFIMISeNTYHPmYSVLNLFPQGFPLFMRETRSGLYSTGQYYAANILALLPGMIIEPLIFVIICYWLTGLRSTFYAFG 523
Cdd:PLN03140 573 ALLFSMII-NMFNG-FAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFF 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 524 VTAMCVVLVMNVATACGCFFSTAFNSVPLAMAYLVPLDYIFMITSGIFIQVNSLPVAFWWTQFLSWMLYANEA-----MT 598
Cdd:PLN03140 651 KQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNAlavneMF 730
|
....
gi 17647959 599 AAQW 602
Cdd:PLN03140 731 APRW 734
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
88-301 |
5.30e-34 |
|
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: 129.71 E-value: 5.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIG--------PFMHRIsGYVYQDD- 157
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIgLLRPD----SGEILVDGQDITglsekelyELRRRI-GMLFQGGa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 158 LFlGSLTVLEhlNFMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVIL 237
Cdd:COG1127 93 LF-DSLTVFE--NVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSE------LSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 238 FCDEPTTGLDSYSAQQLVATLYELAQK--GTTILCTiHQPSSqLFDNFNNVMLLADGRVAFTGSPQ 301
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElgLTSVVVT-HDLDS-AFAIADRVAVLADGKIIAEGTPE 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
76-301 |
3.53e-33 |
|
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: 127.23 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 76 VYTNVGGsgqrmKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA--FRQPAGTVvqgdiLINGRRIGPF-------M 146
Cdd:cd03261 6 LTKSFGG-----RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVglLRPDSGEV-----LIDGEDISGLseaelyrL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 147 HRISGYVYQDDLFLGSLTVLEHLNFMahLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAF 226
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE------LSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 227 AVELLNNPVILFCDEPTTGLDSYSA---QQLVATLYElAQKGTTILCTiHQPSSqLFDNFNNVMLLADGRVAFTGSPQ 301
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASgviDDLIRSLKK-ELGLTSIMVT-HDLDT-AFAIADRIAVLYDGKIVAEGTPE 222
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
66-298 |
6.25e-33 |
|
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: 125.45 E-value: 6.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 66 GATLVWRDLCVYTnvgGSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTVVQGDILINGRRIGPF 145
Cdd:cd03233 1 ASTLSWRNISFTT---GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 146 MHRISG---YVYQDDLFLGSLTVLEHLNFMAHLRLDRRVskeerrliikellertgllsaaqtrigsgddkKVLSGGERK 222
Cdd:cd03233 78 AEKYPGeiiYVSEEDVHFPTLTVRETLDFALRCKGNEFV--------------------------------RGISGGERK 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 223 RLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQPSSQLFDNFNNVMLLADGRVAFTG 298
Cdd:cd03233 126 RVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
88-301 |
2.88e-32 |
|
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: 124.99 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQP-AGTVVQGDILIN---GRRIGPFMHRIsGYVYQDDLFLGS 162
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNgLVEPtSGSVLIDGTDINklkGKALRQLRRQI-GMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 163 LTVLEH-----LNFMAHLR-LDRRVSKEERRLIIkELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVI 236
Cdd:cd03256 93 LSVLENvlsgrLGRRSTWRsLFGLFPKEEKQRAL-AALERVGLLDKAYQRADQ------LSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 237 LFCDEPTTGLDSYSAQQLVATLYELAQ-KGTTILCTIHQPssQLF-DNFNNVMLLADGRVAFTGSPQ 301
Cdd:cd03256 166 ILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQV--DLArEYADRIVGLKDGRIVFDGPPA 230
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
88-305 |
4.33e-32 |
|
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: 123.98 E-value: 4.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfrqpaGTVV--QGDILINGRRIGP-FMHRIS---GYVYQD-D--L 158
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN-----GLLKptSGEVLVDGKDITKkNLRELRrkvGLVFQNpDdqL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 159 FlgSLTVLEHLNF-MAHLRLdrrvSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVIL 237
Cdd:COG1122 89 F--APTVEEDVAFgPENLGL----PREEIRERVEEALELVGLEHLADRPPHE------LSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 238 FCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPsSQLFDNFNNVMLLADGRVAFTGSPQHALS 305
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDL-DLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
88-305 |
1.21e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 123.62 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIgpfmHRIS--------GYVYQDDL 158
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAgLLKPSS----GEVLLDGRDL----ASLSrrelarriAYVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 159 FLGSLTVLE--HLNFMAHLRLDRRVSKEERRlIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVI 236
Cdd:COG1120 86 APFGLTVRElvALGRYPHLGLFGRPSAEDRE-AVEEALERTGLEHLADRPVDE------LSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 237 LFCDEPTTGLDSYSAQQLVATLYELAQ-KGTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTGSPQHALS 305
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNlaARYAD---RLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
88-298 |
3.40e-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: 121.15 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGtLMALMGSSGSGKTTLMSTLAFRQPAgtvVQGDILING---RRIGPFMHRISGYVYQDDLFLGSLT 164
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP---SSGTIRIDGqdvLKQPQKLRRRIGYLPQEFGVYPNFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 165 VLEHLNFMAHLRldrRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:cd03264 89 VREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGS------LSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17647959 245 GLDSYSAQQLVATLYELAQKGTTILCTiHQpSSQLFDNFNNVMLLADGRVAFTG 298
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILST-HI-VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
88-301 |
1.70e-30 |
|
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: 119.96 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGR--RIGPFMHRIS-GYVYQDDLFLGSL 163
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAgLLKPD----SGSILIDGEdvRKEPREARRQiGVLPDERGLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLNFMAHLRldrRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:COG4555 90 TVRENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVGE------LSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTGSPQ 301
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQevEALCD---RVVILHKGKVVAQGSLD 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
88-294 |
6.85e-30 |
|
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: 115.96 E-value: 6.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILING---RRIGPFMHRISGYVYQDDLFLGSL 163
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILgLLKPDS----GEIKVLGkdiKKEPEEVKRRIGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLNfmahlrldrrvskeerrliikellertgllsaaqtrigsgddkkvLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:cd03230 89 TVRENLK---------------------------------------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGTTILCTIHQPS--SQLFDnfnNVMLLADGRV 294
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEeaERLCD---RVAILNNGRI 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
91-244 |
9.10e-30 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 115.05 E-value: 9.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIGPFMHRIS----GYVYQDDLFLGSLTV 165
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAgLLSPT----EGTILLDGQDLTDDERKSLrkeiGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 166 LEHLNFMAHLRLDRRVSKEERrliIKELLERTGLLSAAQTRIGSGDdkKVLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDAR---AEEALEKLGLGDLADRPVGERP--GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
88-294 |
2.96e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 115.30 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIGPFM-----HRISgYVYQD-DLFL 160
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAdLDPPT----SGEIYLDGKPLSAMPppewrRQVA-YVPQEpALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GslTVLEHLNFMAHLRlDRRVSKEErrliIKELLERTGL-LSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFC 239
Cdd:COG4619 88 G--TVRDNLPFPFQLR-ERKFDRER----ALELLERLGLpPDILDKPVER------LSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 240 DEPTTGLDSYSAQQLVATLYEL-AQKGTTILCTIHQPsSQLFDNFNNVMLLADGRV 294
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGRL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
98-294 |
3.73e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.53 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPAgtvVQGDILINGRRIG-------PFMHRISGYVYQDDLFLGSLTVLEhlN 170
Cdd:COG2884 25 IEKGEFVFLTGPSGAGKSTLLKLLYGEERP---TSGQVLVNGQDLSrlkrreiPYLRRRIGVVFQDFRLLPDRTVYE--N 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 171 FMAHLRLDRRVSKEERRLIIkELLERTGLLSAAQTRIGsgddkkVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYS 250
Cdd:COG2884 100 VALPLRVTGKSRKEIRRRVR-EVLDLVGLSDKAKALPH------ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17647959 251 AQQLVATLYELAQKGTTILCTIHQPSsqLFDNFNN-VMLLADGRV 294
Cdd:COG2884 173 SWEIMELLEEINRRGTTVLIATHDLE--LVDRMPKrVLELEDGRL 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
61-313 |
1.41e-28 |
|
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: 120.64 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 61 SPTEQGATLVWRDLCV-YTNvggsgqRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPagtvVQGDILIN 138
Cdd:COG4987 326 APAPGGPSLELEDVSFrYPG------AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrFLDP----QSGSITLG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 139 GRRIGPF----MHRISGYVYQD-DLFLGslTVLEhlNfmahLRLDR-RVSKEErrliIKELLERTGLLSAAQ-------T 205
Cdd:COG4987 396 GVDLRDLdeddLRRRIAVVPQRpHLFDT--TLRE--N----LRLARpDATDEE----LWAALERVGLGDWLAalpdgldT 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 206 RIGSGDDKkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTiHQPssQLFDNFNN 285
Cdd:COG4987 464 WLGEGGRR--LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLIT-HRL--AGLERMDR 538
|
250 260
....*....|....*....|....*...
gi 17647959 286 VMLLADGRVAFTGSPQHALsffANHGYY 313
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELL---AQNGRY 563
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
69-305 |
2.54e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 119.24 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 69 LVWRDLCVytnvgGSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTVVQGDILINGRRIG----P 144
Cdd:COG1123 5 LEVRDLSV-----RYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLelseA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 145 FMHRISGYVYQD-DLFLGSLTVLEHLNFMahLRLdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKR 223
Cdd:COG1123 80 LRGRRIGMVFQDpMTQLNPVTVGDQIAEA--LEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQ------LSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 224 LAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTGSP 300
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGvvAEIAD---RVVVMDDGRIVEDGPP 227
|
....*
gi 17647959 301 QHALS 305
Cdd:COG1123 228 EEILA 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
97-275 |
3.94e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.19 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRI---GPFMHRISGYVYQDDLFLGSLTVLEHLNFM 172
Cdd:COG4133 24 TLAAGEALALTGPNGSGKTTLLRILAgLLPPS----AGEVLWNGEPIrdaREDYRRRLAYLGHADGLKPELTVRENLRFW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 173 AHLRlDRRVSKEErrliIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQ 252
Cdd:COG4133 100 AALY-GLRADREA----IDEALEAVGLAGLADLPVRQ------LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
170 180
....*....|....*....|...
gi 17647959 253 QLVATLYELAQKGTTILCTIHQP 275
Cdd:COG4133 169 LLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
88-293 |
4.61e-27 |
|
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: 107.33 E-value: 4.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPagtVVQGDILINGRRIGpfmhrisgyvyqddlflgsltvle 167
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK---PTSGEILIDGKDIA------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 168 hlnfmahlrldrrvskeerRLIIKELLERTGLLSaaQtrigsgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:cd00267 65 -------------------KLPLEELRRRIGYVP--Q-----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17647959 248 SYSAQQLVATLYELAQKGTTILCTIHQPsSQLFDNFNNVMLLADGR 293
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
62-305 |
9.01e-27 |
|
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: 115.24 E-value: 9.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 62 PTEQGATLVWRDLCVytnvgGSGQRmKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGR 140
Cdd:COG4988 330 PAAGPPSIELEDVSF-----SYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLgFLPPY----SGSILINGV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 141 RIGPF-----MHRISgYVYQDD-LFLGSLtvlehlnfMAHLRL-DRRVSKEErrliIKELLERTGLLSAAQ-------TR 206
Cdd:COG4988 400 DLSDLdpaswRRQIA-WVPQNPyLFAGTI--------RENLRLgRPDASDEE----LEAALEAAGLDEFVAalpdgldTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 207 I---GSGddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTiHQPSSQlfDNF 283
Cdd:COG4988 467 LgegGRG-----LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLALL--AQA 538
|
250 260
....*....|....*....|..
gi 17647959 284 NNVMLLADGRVAFTGSPQHALS 305
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLA 560
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
79-295 |
1.82e-26 |
|
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: 107.82 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 79 NVGGSGQRMK---RIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRI--------GPFM 146
Cdd:TIGR02211 6 NLGKRYQEGKldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGgLDNPT----SGEVLFNGQSLsklssnerAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 147 HRISGYVYQDDLFLGSLTVLEhlNFMAHLrLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAF 226
Cdd:TIGR02211 82 NKKLGFIYQFHHLLPDFTALE--NVAMPL-LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSE------LSGGERQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 227 AVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQ-KGTTILCTIHQPssQLFDNFNNVMLLADGRVA 295
Cdd:TIGR02211 153 ARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNReLNTSFLVVTHDL--ELAKKLDRVLEMKDGQLF 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
88-298 |
2.13e-26 |
|
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: 107.22 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIG--PFMHRISGYVYQDDLFLGSLT 164
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAgLERPD----SGEILIDGRDVTgvPPERRNIGMVFQDYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 165 VLEHLNFmaHLRLdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:cd03259 89 VAENIAF--GLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHE------LSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 245 GLDSYSAQQLVATLYEL--AQKGTTILCTiHQPSSQLF--DnfnNVMLLADGRVAFTG 298
Cdd:cd03259 160 ALDAKLREELREELKELqrELGITTIYVT-HDQEEALAlaD---RIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
82-269 |
7.30e-26 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 106.44 E-value: 7.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 82 GSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTL-MSTLAFRQPA-GTV-VQG-DILINGRRIGPFMHRISGYVYQDD 157
Cdd:cd03257 12 PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLaRAILGLLKPTsGSIiFDGkDLLKLSRRLRKIRRKEIQMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 158 LflGSL----TVLEHLN--FMAHLRLDRrvsKEERRLIIKELLErtgllsaaqtriGSGDDKKV-------LSGGERKRL 224
Cdd:cd03257 92 M--SSLnprmTIGEQIAepLRIHGKLSK---KEARKEAVLLLLV------------GVGLPEEVlnrypheLSGGQRQRV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17647959 225 AFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTIL 269
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLL 200
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
98-313 |
1.23e-25 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 112.23 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILING---RRIGP-FMHRISGYVYQDD-LFLGslTVLEHLNF 171
Cdd:COG2274 498 IKPGERVAIVGRSGSGKSTLLKLLLgLYEPT----SGRILIDGidlRQIDPaSLRRQIGVVLQDVfLFSG--TIRENITL 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 MahlrlDRRVSKEErrliIKELLERTGLLSAA-------QTRIGSGDdkKVLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:COG2274 572 G-----DPDATDEE----IIEAARLAGLHDFIealpmgyDTVVGEGG--SNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 245 GLDSYSAQQLVATLYELAQKGTTILCTiHQPSsqLFDNFNNVMLLADGRVAFTGSPQHALsffANHGYY 313
Cdd:COG2274 641 ALDAETEAIILENLRRLLKGRTVIIIA-HRLS--TIRLADRIIVLDKGRIVEDGTHEELL---ARKGLY 703
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
98-299 |
4.26e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.96 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA--FRQPAGTvvqgdILINGRRIGPFMHRISGYV------YQDdlflgsLTVLEHL 169
Cdd:COG4152 24 VPKGEIFGLLGPNGAGKTTTIRIILgiLAPDSGE-----VLWDGEPLDPEDRRRIGYLpeerglYPK------MKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 NFMAHLR-LDRRVSKEErrliIKELLERTGLLSAAqtrigsgdDKKV--LSGGERKRLAFAVELLNNPVILFCDEPTTGL 246
Cdd:COG4152 93 VYLARLKgLSKAEAKRR----ADEWLERLGLGDRA--------NKKVeeLSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17647959 247 DSYSAQQLVATLYELAQKGTTILCTIHQPSS--QLFDnfnNVMLLADGRVAFTGS 299
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELveELCD---RIVIINKGRKVLSGS 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
95-275 |
4.31e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.08 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 95 TGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQP-AGTVVQGDilinGRRIGpfmhrisgYVYQ----DDLFlgSLTVLE- 167
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAgVLRPtSGTVRRAG----GARVA--------YVPQrsevPDSL--PLTVRDl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 168 -HLNFMAHLRLDRRVSKEERRLIIKELlERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGL 246
Cdd:NF040873 78 vAMGRWARRGLWRRLTRDDRAAVDDAL-ERVGLADLAGRQLGE------LSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*....
gi 17647959 247 DSYSAQQLVATLYELAQKGTTILCTIHQP 275
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
82-269 |
7.65e-25 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 102.94 E-value: 7.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 82 GSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRI-GPFMHRisGYVYQDDLF 159
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAgLERPTS----GEVLVDGEPVtGPGPDR--GYVFQQDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 LGSLTVLEhlNFMAHLRLdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFC 239
Cdd:cd03293 85 LPWLTVLD--NVALGLEL-QGVPKAEARERAEELLELVGLSGFENAYPHQ------LSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190
....*....|....*....|....*....|.
gi 17647959 240 DEPTTGLDSYSAQQLVATLYELAQK-GTTIL 269
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWREtGKTVL 186
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
97-294 |
1.55e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 102.51 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLAfrqpaG--TVVQGDILINGRRIGP--------FMHRISGYVYQDDLFLGSLTVL 166
Cdd:COG4181 34 EVEAGESVAIVGASGSGKSTLLGLLA-----GldRPTSGTVRLAGQDLFAldedararLRARHVGFVFQSFQLLPTLTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 EhlNFMAHLRLDRRVSKEERrliIKELLERTGL---LSA--AQtrigsgddkkvLSGGERKRLAFAVELLNNPVILFCDE 241
Cdd:COG4181 109 E--NVMLPLELAGRRDARAR---ARALLERVGLghrLDHypAQ-----------LSGGEQQRVALARAFATEPAILFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17647959 242 PTTGLDSYSAQQLVATLYEL-AQKGTTILCTIHQPssQLFDNFNNVMLLADGRV 294
Cdd:COG4181 173 PTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDP--ALAARCDRVLRLRAGRL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-304 |
1.92e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 107.68 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 24 VMPVGSTIEVPSLDSTPKLSKRNSSERSLPLRSYSKWSPTEQGATLV-WRDLCVYTNVGGSGQRmkRIINNSTGAIQPGT 102
Cdd:COG1123 215 VMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLeVRNLSKRYPVRGKGGV--RAVDDVSLTLRRGE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 103 LMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIG--------PFMHRIsGYVYQDDLflGSL----TVLEHL 169
Cdd:COG1123 293 TLGLVGESGSGKSTLARLLLgLLRPTS----GSILFDGKDLTklsrrslrELRRRV-QMVFQDPY--SSLnprmTVGDII 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 nfMAHLRLDRRVSKEERRLIIKELLERTGL-LSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDS 248
Cdd:COG1123 366 --AEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHE------LSGGQRQRVAIARALALEPKLLILDEPTSALDV 437
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 249 YSAQQLVATLYELAQK-GTTILC------TIHQPSSQlfdnfnnVMLLADGRVAFTGS-------PQHAL 304
Cdd:COG1123 438 SVQAQILNLLRDLQRElGLTYLFishdlaVVRYIADR-------VAVMYDGRIVEDGPteevfanPQHPY 500
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
98-302 |
4.20e-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: 101.36 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIGPF-MHRIS----GYVYQDDLFLGSLTVLEhlNF 171
Cdd:cd03219 23 VRPGEIHGLIGPNGAGKTTLFNLISgFLRPTS----GSVLFDGEDITGLpPHEIArlgiGRTFQIPRLFPELTVLE--NV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 M--AHLR-----LDRRVSKEERRLI--IKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:cd03219 97 MvaAQARtgsglLLARARREEREARerAEELLERVGLADLADRPAGE------LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 243 TTGLDSYSAQQLVATLYELAQKGTTILCTIHqpssqlfdNFNNVMLLAD-------GRVAFTGSPQH 302
Cdd:cd03219 171 AAGLNPEETEELAELIRELRERGITVLLVEH--------DMDVVMSLADrvtvldqGRVIAEGTPDE 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
98-274 |
8.82e-24 |
|
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: 99.91 E-value: 8.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQpagTVVQGDILINGRRIGPFMHRIS------GYVYQD-DLFlGSLTVLEhlN 170
Cdd:cd03262 23 VKKGEVVVIIGPSGSGKSTLLRCINLLE---EPDSGTIIIDGLKLTDDKKNINelrqkvGMVFQQfNLF-PHLTVLE--N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 171 FMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYS 250
Cdd:cd03262 97 ITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQ------LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180
....*....|....*....|....
gi 17647959 251 AQQLVATLYELAQKGTTILCTIHQ 274
Cdd:cd03262 171 VGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
88-298 |
9.08e-24 |
|
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: 98.66 E-value: 9.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRrigpfmhrisgyvyqddlflgsltvl 166
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAgLLKPS----SGEILLDGK-------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 eHLNFMAHLRLDRRVSkeerrlIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGL 246
Cdd:cd03214 62 -DLASLSPKELARKIA------YVPQALELLGLAHLADRPFNE------LSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17647959 247 DSYSAQQLVATLYELA-QKGTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTG 298
Cdd:cd03214 129 DIAHQIELLELLRRLArERGKTVVMVLHDLNlaARYAD---RVILLKDGRIVAQG 180
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
98-265 |
9.27e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.09 E-value: 9.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRI-GPFMHRisGYVYQDDLFLGSLTVLEHLNFmaHL 175
Cdd:COG4525 30 IESGEFVVALGASGCGKTTLLNLIAgFLAPSS----GEITLDGVPVtGPGADR--GVVFQKDALLPWLNVLDNVAF--GL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 176 RLdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSY---SAQ 252
Cdd:COG4525 102 RL-RGVPKAERRARAEELLALVGLADFARRRIWQ------LSGGMRQRVGIARALAADPRFLLMDEPFGALDALtreQMQ 174
|
170
....*....|...
gi 17647959 253 QLVATLYELAQKG 265
Cdd:COG4525 175 ELLLDVWQRTGKG 187
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
91-294 |
1.07e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 99.79 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQpagTVVQGDILING-------RRIGPFMHRISGYVYQDDLFLGSL 163
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEE---LPTSGTIRVNGqdvsdlrGRAIPYLRRKIGVVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLNFMAhlrldrRVSKEERRLI---IKELLERTGLLSAAQTrIGSGddkkvLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:cd03292 94 NVYENVAFAL------EVTGVPPREIrkrVPAALELVGLSHKHRA-LPAE-----LSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17647959 241 EPTTGLDSYSAQQLVATLYELAQKGTTILCTIHqpSSQLFDNFNN-VMLLADGRV 294
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH--AKELVDTTRHrVIALERGKL 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
88-300 |
1.25e-23 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 99.92 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLmstlaFRQPAGTVV--QGDILINGRRIGPF-MHRIS----GYVYQDDLFL 160
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTT-----FYMIVGLVKpdSGKILLDGQDITKLpMHKRArlgiGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSLTVLEhlNFMAHLRLdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:cd03218 88 RKLTVEE--NILAVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKASS------LSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 241 EPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSP 300
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN-VRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
88-313 |
2.82e-23 |
|
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: 98.84 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMStLAFRqpAGTVVQGDILINGRRIG----PFMHRISGYVYQDdlflgsl 163
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILR-LLFR--FYDVSSGSILIDGQDIRevtlDSLRRAIGVVPQD------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLNFMAHLRLDR-RVSKEE-----RRLIIKELLERtgLLSAAQTRIGSGDDKkvLSGGERKRLAFAVELLNNPVIL 237
Cdd:cd03253 84 TVLFNDTIGYNIRYGRpDATDEEvieaaKAAQIHDKIMR--FPDGYDTIVGERGLK--LSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 238 FCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTiHQPSSQLfdNFNNVMLLADGRVAFTGSPQHALsffANHGYY 313
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIV--NADKIIVLKDGRIVERGTHEELL---AKGGLY 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
98-269 |
6.53e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 98.62 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIGPFMHRIsGYVYQDDLFLGSLTVLEhlNFMAHLR 176
Cdd:COG1116 34 VAAGEFVALVGPSGCGKSTLLRLIAgLEKPTS----GEVLVDGKPVTGPGPDR-GVVFQEPALLPWLTVLD--NVALGLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 177 LdRRVSKEERRLIIKELLERTGLLSAAqtrigsgdDK--KVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDS---YSA 251
Cdd:COG1116 107 L-RGVPKAERRERARELLELVGLAGFE--------DAypHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltrERL 177
|
170
....*....|....*...
gi 17647959 252 QQLVATLyeLAQKGTTIL 269
Cdd:COG1116 178 QDELLRL--WQETGKTVL 193
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
98-300 |
1.01e-22 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 97.06 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPagtVVQGDILING----RRIGPFMHRIsGYVYQDDLFLGSLTVLEHLNFMA 173
Cdd:cd03265 23 VRRGEIFGLLGPNGAGKTTTIKMLTTLLK---PTSGRATVAGhdvvREPREVRRRI-GIVFQDLSVDDELTGWENLYIHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 174 HLRldrRVSKEERRLIIKELLERTGLLSAAQTRIgsgddkKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQ 253
Cdd:cd03265 99 RLY---GVPGAERRERIDELLDFVGLLEAADRLV------KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17647959 254 LVATLYEL-AQKGTTILCTIH--QPSSQLFDnfnNVMLLADGRVAFTGSP 300
Cdd:cd03265 170 VWEYIEKLkEEFGMTILLTTHymEEAEQLCD---RVAIIDHGRIIAEGTP 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
82-274 |
1.05e-22 |
|
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: 97.27 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 82 GSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAF--RQPAGTV-VQG-DI-LINGRRIGPFMHRIsGYVYQD 156
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGleRPTSGSVlVDGtDLtLLSGKELRKARRRI-GMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 157 DLFLGSLTVLEhlNFMAHLRLDRrVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVI 236
Cdd:cd03258 91 FNLLSSRTVFE--NVALPLEIAG-VPKAEIEERVLELLELVGLEDKADAYPAQ------LSGGQKQRVGIARALANNPKV 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 17647959 237 LFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQ 274
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRElGLTIVLITHE 200
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
88-298 |
1.28e-22 |
|
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: 97.46 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvQGDILINGRRIG-----PFMHRIsGYVYQD--DLFL 160
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY--GNDVRLFGERRGgedvwELRKRI-GLVSPAlqLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSLTVLEHL--NFMAHLRLDRRVSKEERRLIiKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILF 238
Cdd:COG1119 93 RDETVLDVVlsGFFDSIGLYREPTDEQRERA-RELLELLGLAHLADRPFGT------LSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 239 CDEPTTGLDSYSAQQLVATLYELAQKG--TTILCTiHQPsSQLFDNFNNVMLLADGRVAFTG 298
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGapTLVLVT-HHV-EEIPPGITHVLLLKDGRVVAAG 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
98-269 |
2.63e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 99.02 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIG---PFMHRIsGYVYQDD-LFlGSLTVLEHLNFm 172
Cdd:COG3842 28 IEPGEFVALLGPSGCGKTTLLRMIAgFETPD----SGRILLDGRDVTglpPEKRNV-GMVFQDYaLF-PHLTVAENVAF- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 173 aHLRLdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQ 252
Cdd:COG3842 101 -GLRM-RGVPKAEIRARVAELLELVGLEGLADRYPHQ------LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLRE 172
|
170
....*....|....*...
gi 17647959 253 QLVATLYELAQK-GTTIL 269
Cdd:COG3842 173 EMREELRRLQRElGITFI 190
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
98-309 |
3.86e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 95.83 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQpagTVVQGDILINGRRIGPFMHRI------SGYVYQD-DLFlGSLTVLEhlN 170
Cdd:COG1126 24 VEKGEVVVIIGPSGSGKSTLLRCINLLE---EPDSGTITVDGEDLTDSKKDInklrrkVGMVFQQfNLF-PHLTVLE--N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 171 FMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSys 250
Cdd:COG1126 98 VTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQ------LSGGQQQRVAIARALAMEPKVMLFDEPTSALDP-- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 251 aqQLV----ATLYELAQKGTTILCTIHQPSsqlfdnF-----NNVMLLADGRVAFTGSPQHalsFFAN 309
Cdd:COG1126 170 --ELVgevlDVMRDLAKEGMTMVVVTHEMG------FarevaDRVVFMDGGRIVEEGPPEE---FFEN 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
98-293 |
4.02e-22 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 93.60 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPagtvVQGDILING---RRIGPF-MHRISGYVYQDDlFLGSLTVLEhlNfm 172
Cdd:cd03228 25 IKPGEKVAIVGPSGSGKSTLLKLLLrLYDP----TSGEILIDGvdlRDLDLEsLRKNIAYVPQDP-FLFSGTIRE--N-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 173 ahlrldrrvskeerrliikellertgllsaaqtrigsgddkkVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQ 252
Cdd:cd03228 96 ------------------------------------------ILSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17647959 253 QLVATLYELAQKGTTILCTiHQPSSqlFDNFNNVMLLADGR 293
Cdd:cd03228 134 LILEALRALAKGKTVIVIA-HRLST--IRDADRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
98-277 |
4.77e-22 |
|
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: 100.44 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIGPF----MHRISGYVYQDD-LFLGSLTvlehlnf 171
Cdd:TIGR02857 345 VPPGERVALVGPSGAGKSTLLNLLLgFVDPTE----GSIAVNGVPLADAdadsWRDQIAWVPQHPfLFAGTIA------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 mAHLRLDRRVSKEERrliIKELLERTGLLSAAQTRiGSGDDKKV------LSGGERKRLAFAVELLNNPVILFCDEPTTG 245
Cdd:TIGR02857 414 -ENIRLARPDASDAE---IREALERAGLDEFVAAL-PQGLDTPIgeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190
....*....|....*....|....*....|..
gi 17647959 246 LDSYSAQQLVATLYELAQKGTTILCTiHQPSS 277
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQGRTVLLVT-HRLAL 519
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
98-301 |
5.14e-22 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 94.81 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAfrqpaG--TVVQGDILINGRRIGPF-MHRIS----GYVYQD-DLFlGSLTVLEHL 169
Cdd:cd03224 23 VPEGEIVALLGRNGAGKTTLLKTIM-----GllPPRSGSIRFDGRDITGLpPHERAragiGYVPEGrRIF-PELTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 NFMAHLRLDRRVSKEERRL-----IIKELLERtgllsAAQTrigsgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:cd03224 97 LLGAYARRRAKRKARLERVyelfpRLKERRKQ-----LAGT----------LSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647959 245 GLDSYSAQQLVATLYELAQKGTTILcTIHQpssqlfdNFNNVMLLAD-------GRVAFTGSPQ 301
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEGVTIL-LVEQ-------NARFALEIADrayvlerGRVVLEGTAA 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
100-298 |
5.39e-22 |
|
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: 94.67 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 100 PGTLMALMGSSGSGKTTLMSTLA--FRQPAGTVVQGDILINGRRIGPFM---HRISGYVYQDDLFLGSLTVLEHLNFMAh 174
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAglEKPDGGTIVLNGTVLFDSRKKINLppqQRKIGLVFQQYALFPHLNVRENLAFGL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 175 lrldRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQL 254
Cdd:cd03297 101 ----KRKRNREDRISVDELLDLLGLDHLLNRYPAQ------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17647959 255 VATLYELAQ--KGTTILCTiHQPsSQLFDNFNNVMLLADGRVAFTG 298
Cdd:cd03297 171 LPELKQIKKnlNIPVIFVT-HDL-SEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
83-294 |
5.97e-22 |
|
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: 94.25 E-value: 5.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 83 SGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfrqpaGTV--VQGDILINGRRIGPFMH-RISGYVYQD-DL 158
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILA-----GLIkeSSGSILLNGKPIKAKERrKSIGYVMQDvDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 159 FLGSLTVLEHLnfmaHLRLDRrvsKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILF 238
Cdd:cd03226 83 QLFTDSVREEL----LLGLKE---LDAGNEQAETVLKDLDLYALKERHPLS------LSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 239 CDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSqLFDNFNNVMLLADGRV 294
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGAI 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
98-247 |
7.54e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.09 E-value: 7.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTVVQGDILINGRRI--GPFMHRISGYVYQDDLFLGSLTVLEHLNFMahl 175
Cdd:COG4136 24 VAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLtaLPAEQRRIGILFQDDLLFPHLSVGENLAFA--- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 176 rLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:COG4136 101 -LPPTIGRAQRRARVEQALEEAGLAGFADRDPAT------LSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
82-269 |
8.19e-22 |
|
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: 95.26 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 82 GSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA--FRQPAGTVVQGDILINGRRIGPFMHRISgYVYQDDLf 159
Cdd:COG1124 12 GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAglERPWSGEVTFDGRPVTRRRRKAFRRRVQ-MVFQDPY- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 lGSL----TVLEHLNF-MAHLRLDRRvskEERrliIKELLERTGLLSAAQTRIGSGddkkvLSGGERKRLAFAVELLNNP 234
Cdd:COG1124 90 -ASLhprhTVDRILAEpLRIHGLPDR---EER---IAELLEQVGLPPSFLDRYPHQ-----LSGGQRQRVAIARALILEP 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 17647959 235 VILFCDEPTTGLDSYSAQQLVATLYEL-AQKGTTIL 269
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYL 193
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
101-301 |
9.88e-22 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 96.31 E-value: 9.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 101 GTLMALMGSSGSGKTTLMSTLA--FRQPAGTV-VQG-DILINGRRIgpfmHRISGYVYQDDLFLGSLTVLEHLNFMAHLR 176
Cdd:TIGR01188 19 GEVFGFLGPNGAGKTTTIRMLTtlLRPTSGTArVAGyDVVREPRKV----RRSIGIVPQYASVDEDLTGRENLEMMGRLY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 177 ldrRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVA 256
Cdd:TIGR01188 95 ---GLPKDEAEERAEELLELFELGEAADRPVGT------YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17647959 257 TLYELAQKGTTILCTIHqpssqlfdNFNNVMLLAD-------GRVAFTGSPQ 301
Cdd:TIGR01188 166 YIRALKEEGVTILLTTH--------YMEEADKLCDriaiidhGRIIAEGTPE 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
88-294 |
1.40e-21 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 93.78 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAF--RQPAGTVVQGDILINGRRI-GPFMHRIS-----GYVYQD-DL 158
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIPGAPDEGEVLLDGKDIyDLDVDVLElrrrvGMVFQKpNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 159 FLGSltVLEhlNFMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSGDdkkvLSGGERKRLAFAVELLNNPVILF 238
Cdd:cd03260 93 FPGS--IYD--NVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHALG----LSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 239 CDEPTTGLDSYSAQQLVATLYELAQKGTTILCT--IHQpSSQLFDnfnNVMLLADGRV 294
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ-AARVAD---RTAFLLNGRL 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
84-294 |
2.24e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.34 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 84 GQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfrqPAGTVVQGDILINGRRI--------GPFMHRISGYVYQ 155
Cdd:PRK11629 18 GSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLG---GLDTPTSGDVIFNGQPMsklssaakAELRNQKLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 156 DDLFLGSLTVLEHLNFMAHLRLDRRVSKEERRLiikELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPV 235
Cdd:PRK11629 95 FHHLLPDFTALENVAMPLLIGKKKPAEINSRAL---EMLAAVGLEHRANHRPSE------LSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 236 ILFCDEPTTGLDSYSAQQLVATLYEL-AQKGTTILCTIHqpSSQLFDNFNNVMLLADGRV 294
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTH--DLQLAKRMSRQLEMRDGRL 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
98-294 |
2.90e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 92.65 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILING---RRIGPF--MHRIsGYVYQD-DLFLGSLTvlEHLN 170
Cdd:cd03245 27 IRAGEKVAIIGRVGSGKSTLLKLLAgLYKPT----SGSVLLDGtdiRQLDPAdlRRNI-GYVPQDvTLFYGTLR--DNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 171 fmahlrLDRRVSKEERrliIKELLERTGLLSAAQtRIGSGDDKKV------LSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:cd03245 100 ------LGAPLADDER---ILRAAELAGVTDFVN-KHPNGLDLQIgergrgLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17647959 245 GLDSYSAQQLVATLYELAQKGTTILCTiHQPSsqLFDNFNNVMLLADGRV 294
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDKTLIIIT-HRPS--LLDLVDRIIVMDSGRI 216
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
98-269 |
2.94e-21 |
|
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: 95.12 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTVVQGDILINGRRIGPF----MHRISG----YVYQDDLflGSL----TV 165
Cdd:COG0444 28 VRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLsekeLRKIRGreiqMIFQDPM--TSLnpvmTV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 166 LEHLnfMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQtRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTG 245
Cdd:COG0444 106 GDQI--AEPLRIHGGLSKAEARERAIELLERVGLPDPER-RLDRyp--heLSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180
....*....|....*....|....*.
gi 17647959 246 LDSySAQ-QLVATLYELAQK-GTTIL 269
Cdd:COG0444 181 LDV-TIQaQILNLLKDLQRElGLAIL 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
88-274 |
3.31e-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: 92.34 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIGPFMHRISGYVYQDDLFLGSLTVL 166
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILgIILPD----SGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 EHLNFMAHLRldrRVSKEERRLIIKELLERTGLLSAAQTRIgsgddkKVLSGGERKRLAFAVELLNNPVILFCDEPTTGL 246
Cdd:cd03269 89 DQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRV------EELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180
....*....|....*....|....*...
gi 17647959 247 DSYSAQQLVATLYELAQKGTTILCTIHQ 274
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
88-305 |
6.37e-21 |
|
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: 92.34 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTlmstlAFRQPAGTVV--QGDILINGRRIG--PfMHRIS----GYVYQDDLF 159
Cdd:TIGR04406 14 RKVVNDVSLSVKSGEIVGLLGPNGAGKTT-----SFYMIVGLVRpdAGKILIDGQDIThlP-MHERArlgiGYLPQEASI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 LGSLTVLEhlNFMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFC 239
Cdd:TIGR04406 88 FRKLTVEE--NIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMS------LSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 240 DEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSPQHALS 305
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHN-VRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
98-304 |
9.99e-21 |
|
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: 91.52 E-value: 9.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIgpfmHRIS--------GYVYQDD-LFLGSltvle 167
Cdd:cd03254 26 IKPGETVAIVGPTGAGKTTLINLLMrFYDPQ----KGQILIDGIDI----RDISrkslrsmiGVVLQDTfLFSGT----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 168 hlnFMAHLRLDRRVSKEERrliIKELLERTGLLSAAQTRIGS-----GDDKKVLSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:cd03254 93 ---IMENIRLGRPNATDEE---VIEAAKEAGAHDFIMKLPNGydtvlGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 243 TTGLDSYSAQQLVATLYELaQKGTTILCTIHQPSSQLfdNFNNVMLLADGRVAFTGSPQHAL 304
Cdd:cd03254 167 TSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIK--NADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
97-298 |
1.42e-20 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 90.63 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIG--PFMHRISGYVYQDDLFLGSLTVLEH--LNF 171
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAgFETPQ----SGRVLINGVDVTaaPPADRPVSMLFQENNLFAHLTVEQNvgLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 MAHLRLdrrvsKEERRLIIKELLERTGLlsaaqtrigSGDDKKV---LSGGERKRLAFAVELLNNPVILFCDEPTTGLDS 248
Cdd:cd03298 96 SPGLKL-----TAEDRQAIEVALARVGL---------AGLEKRLpgeLSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17647959 249 YSAQQLVATLYEL-AQKGTTILCTIHQP--SSQLFDnfnNVMLLADGRVAFTG 298
Cdd:cd03298 162 ALRAEMLDLVLDLhAETKMTVLMVTHQPedAKRLAQ---RVVFLDNGRIAAQG 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
88-293 |
1.97e-20 |
|
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: 89.17 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIG------PFMHRISGYVYQDDLFL 160
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAgLEEPDS----GSILIDGEDLTdledelPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSLTVLEHLNFmahlrldrrvskeerrliikellertgllsaaqtrigsgddkkVLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:cd03229 89 PHLTVLENIAL-------------------------------------------GLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17647959 241 EPTTGLDSYSAQQLVATLYEL-AQKGTTILCTIHQPsSQLFDNFNNVMLLADGR 293
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
97-305 |
3.44e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.81 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGR---RIGPFMHRISgYVYQDD-LFlGSLTVLEHLNF 171
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAgFLPPD----SGRILWNGQdltALPPAERPVS-MLFQENnLF-PHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 maHLRLDRRVSKEERRLIIkELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELL-NNPVILFcDEPTTGLDSYS 250
Cdd:COG3840 95 --GLRPGLKLTAEQRAQVE-QALERVGLAGLLDRLPGQ------LSGGQRQRVALARCLVrKRPILLL-DEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 251 AQQLVATLYELAQK-GTTILCTIHQPSSQLfDNFNNVMLLADGRVAFTGSPQHALS 305
Cdd:COG3840 165 RQEMLDLVDELCRErGLTVLMVTHDPEDAA-RIADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
88-301 |
9.83e-20 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 88.45 E-value: 9.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIG--PFMHRISGYVYQDDLFLGSLT 164
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgFETPT----SGEILLDGKDITnlPPHKRPVNTVFQNYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 165 VLEHLNFmaHLRLdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:cd03300 89 VFENIAF--GLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQ------LSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 245 GLDSYSAQQLVATLYELAQK-GTTILCTIHQPSSQLFDNfNNVMLLADGRVAFTGSPQ 301
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMS-DRIAVMNKGKIQQIGTPE 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
98-301 |
2.57e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 89.82 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIGPFMH----RIsGYVYQD-DLFlGSLTVLEHLNF 171
Cdd:COG1118 25 IASGELVALLGPSGSGKTTLLRIIAgLETPD----SGRIVLNGRDLFTNLPprerRV-GFVFQHyALF-PHMTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 maHLRlDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSA 251
Cdd:COG1118 99 --GLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQ------LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17647959 252 QQLVATLYEL--AQKGTTILCTiHQpssQL--FDNFNNVMLLADGRVAFTGSPQ 301
Cdd:COG1118 170 KELRRWLRRLhdELGGTTVFVT-HD---QEeaLELADRVVVMNQGRIEQVGTPD 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
97-273 |
2.95e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 85.94 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLA--FRQPAGTV-VQGDILINGRRiGPFMHRIS-GYVYQD-DLFLGSLTVLEHLNF 171
Cdd:TIGR01166 14 AAERGEVLALLGANGAGKSTLLLHLNglLRPQSGAVlIDGEPLDYSRK-GLLERRQRvGLVFQDpDDQLFAADVDQDVAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 MAhlrLDRRVSKEERRLIIKELLERTGLLSAAQTRIgsgddkKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSA 251
Cdd:TIGR01166 93 GP---LNLGLSEAEVERRVREALTAVGASGLRERPT------HCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|..
gi 17647959 252 QQLVATLYELAQKGTTILCTIH 273
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTH 185
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
98-301 |
3.14e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 87.34 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAfrqpaG--TVVQGDILINGRRIG---PfmHRIS----GYVYQD-DLFlGSLTVLE 167
Cdd:COG0410 26 VEEGEIVALLGRNGAGKTTLLKAIS-----GllPPRSGSIRFDGEDITglpP--HRIArlgiGYVPEGrRIF-PSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 168 HLNFMAHLRLDRRVSKE--ER------RLiiKELLERtgllsAAQTrigsgddkkvLSGGERKRLAFAVELLNNPVILFC 239
Cdd:COG0410 98 NLLLGAYARRDRAEVRAdlERvyelfpRL--KERRRQ-----RAGT----------LSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647959 240 DEPTTGLdsysA----QQLVATLYELAQKGTTILCtIHQpssqlfdNFNNVMLLAD-------GRVAFTGSPQ 301
Cdd:COG0410 161 DEPSLGL----AplivEEIFEIIRRLNREGVTILL-VEQ-------NARFALEIADrayvlerGRIVLEGTAA 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
98-280 |
3.78e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.45 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPAGtvvQGDILINGRRI-GPFMHRisGYVYQDDLFLGSLTVLEHLNFmaHLR 176
Cdd:PRK11248 24 LESGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGSITLDGKPVeGPGAER--GVVFQNEGLLPWRNVQDNVAF--GLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 177 LdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVA 256
Cdd:PRK11248 97 L-AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ------LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180
....*....|....*....|....*
gi 17647959 257 TLYELAQK-GTTILCTIHQPSSQLF 280
Cdd:PRK11248 170 LLLKLWQEtGKQVLLITHDIEEAVF 194
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
98-300 |
7.47e-19 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 85.98 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRI---GPfmHRIsgYVYQDDLFLGSLTVLEHLnFMA 173
Cdd:TIGR01184 8 IQQGEFISLIGHSGCGKSTLLNLISgLAQPT----SGGVILEGKQItepGP--DRM--VVFQNYSLLPWLTVRENI-ALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 174 HLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQ 253
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ------LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17647959 254 LVATLYELAQK-GTTILCTIHqpssqlfdNFNNVMLLADGRVAFTGSP 300
Cdd:TIGR01184 153 LQEELMQIWEEhRVTVLMVTH--------DVDEALLLSDRVVMLTNGP 192
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
64-275 |
1.08e-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: 89.73 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 64 EQGATLVWRDLcvytNVGGSGQrmKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPagtvVQGDILINGRRI 142
Cdd:TIGR02868 330 LGKPTLELRDL----SAGYPGA--PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAgLLDP----LQGEVTLDGVPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 143 GPFMH----RISGYVYQD-DLFlgSLTVLEHLnfmahlRLDR-RVSKEErrliIKELLERTGLL-------SAAQTRIGS 209
Cdd:TIGR02868 400 SSLDQdevrRRVSVCAQDaHLF--DTTVRENL------RLARpDATDEE----LWAALERVGLAdwlralpDGLDTVLGE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 210 GddKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYElAQKGTTILCTIHQP 275
Cdd:TIGR02868 468 G--GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
98-275 |
1.12e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 84.72 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPAgtvVQGDILINGRRIG---PFMHRISGYVYQDDLFLGSLTVLEHLNFMAH 174
Cdd:TIGR01189 23 LNAGEALQVTGPNGIGKTTLLRILAGLLRP---DSGEVRWNGTPLAeqrDEPHENILYLGHLPGLKPELSALENLHFWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 175 LrldrrvSKEERRLIiKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQL 254
Cdd:TIGR01189 100 I------HGGAQRTI-EDALAAVGLTGFEDLPAAQ------LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|.
gi 17647959 255 VATLYELAQKGTTILCTIHQP 275
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
89-301 |
1.17e-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: 85.85 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 89 RIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIG--PFMHRISGYVYQDDLFLGSLTV 165
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAgLERPD----SGTILFGGEDATdvPVQERNVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 166 LEHLNFMAHLR-LDRRVSKEERRLIIKELLERTGLLSAAQtRIGSGddkkvLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:cd03296 92 FDNVAFGLRVKpRSERPPEAEIRAKVHELLKLVQLDWLAD-RYPAQ-----LSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 245 GLDSYSAQQLVATLYELAQKG--TTILCTIHQpsSQLFDNFNNVMLLADGRVAFTGSPQ 301
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDELhvTTVFVTHDQ--EEALEVADRVVVMNKGRIEQVGTPD 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
98-298 |
1.29e-18 |
|
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: 85.11 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAfrqpagTVVQ---GDILING-----------RRIGpfMHRISGYVYQddlflgSL 163
Cdd:cd03266 28 VKPGEVTGLLGPNGAGKTTTLRMLA------GLLEpdaGFATVDGfdvvkepaearRRLG--FVSDSTGLYD------RL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLNFMAHL------RLDRRVSKEERRLIIKELLERtgllsaaqtRIGSgddkkvLSGGERKRLAFAVELLNNPVIL 237
Cdd:cd03266 94 TARENLEYFAGLyglkgdELTARLEELADRLGMEELLDR---------RVGG------FSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647959 238 FCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIH--QPSSQLFDnfnNVMLLADGRVAFTG 298
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHimQEVERLCD---RVVVLHRGRVVYEG 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
97-309 |
1.69e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.57 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLAF-RQP-AGTVVQGDILINGRR-IGPFMHRIS------GYVYQDDLFLGSLTVLE 167
Cdd:PRK11264 25 EVKPGEVVAIIGPSGSGKTTLLRCINLlEQPeAGTIRVGDITIDTARsLSQQKGLIRqlrqhvGFVFQNFNLFPHRTVLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 168 hlNFMAHLRLDRRVSKEERRLIIKELLERTGLlsaaqtrigSGDDK---KVLSGGERKRLAFAVELLNNP-VILFcDEPT 243
Cdd:PRK11264 105 --NIIEGPVIVKGEPKEEATARARELLAKVGL---------AGKETsypRRLSGGQQQRVAIARALAMRPeVILF-DEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGTTILCTIHQPSsqlF--DNFNNVMLLADGRVAFTGSpqhALSFFAN 309
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS---FarDVADRAIFMDQGRIVEQGP---AKALFAD 234
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
105-324 |
2.19e-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: 84.69 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 105 ALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIGPF---MHRISgYVYQDDLFLGSLTVLEHLNFMAHLRLDRR 180
Cdd:cd03299 29 VILGPTGSGKSVLLETIAgFIKPDS----GKILLNGKDITNLppeKRDIS-YVPQNYALFPHMTVYKNIAYGLKKRKVDK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 181 VSKEERRLIIKELLERTGLLsaaqtrigsgdDKKV--LSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATL 258
Cdd:cd03299 104 KEIERKVLEIAEMLGIDHLL-----------NRKPetLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 259 YELAQK-GTTILCTIHQpssqlFDNF----NNVMLLADGRVAFTGSPQHALSffanhgyyCPEAYNPADFL 324
Cdd:cd03299 173 KKIRKEfGVTVLHVTHD-----FEEAwalaDKVAIMLNGKLIQVGKPEEVFK--------KPKNEFVAEFL 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
90-313 |
2.74e-18 |
|
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: 84.59 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIGPF----MHRISGYVYQDdLFLGSLT 164
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrFYDVD----SGRILIDGHDVRDYtlasLRRQIGLVSQD-VFLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 165 VLEHLNFMAHLRLDRRVSKEERRLIIKELLERT--GLlsaaQTRIGSGDDKkvLSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:cd03251 92 VAENIAYGRPGATREEVEEAARAANAHEFIMELpeGY----DTVIGERGVK--LSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 243 TTGLDSYSAQQLVATLYELAQKGTTI-----LCTIhqpssqlfDNFNNVMLLADGRVAFTGSpqHAlSFFANHGYY 313
Cdd:cd03251 166 TSALDTESERLVQAALERLMKNRTTFviahrLSTI--------ENADRIVVLEDGKIVERGT--HE-ELLAQGGVY 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
98-305 |
2.78e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.51 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMstLAFR---QPAgtvvQGDILINGRRIG------PFMHRISGYVYQ---DDLFlgSLTV 165
Cdd:PRK13639 25 AEKGEMVALLGPNGAGKSTLF--LHFNgilKPT----SGEVLIKGEPIKydkkslLEVRKTVGIVFQnpdDQLF--APTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 166 LEHLNFMAhlrLDRRVSKEERRLIIKELLERTGLlsaaqtrigSGDDKKV---LSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:PRK13639 97 EEDVAFGP---LNLGLSKEEVEKRVKEALKAVGM---------EGFENKPphhLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647959 243 TTGLDSYSAQQLVATLYELAQKGTTILCTIHQpsSQLFDNF-NNVMLLADGRVAFTGSPQHALS 305
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
88-298 |
2.85e-18 |
|
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: 83.81 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGtvvQGDILING----------RRIGPFMHRISgyvyqdd 157
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD---SGEITFDGksyqkniealRRIGALIEAPG------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 158 lFLGSLTVLEhlNFMAHLRLdRRVSKEErrliIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVIL 237
Cdd:cd03268 83 -FYPNLTARE--NLRLLARL-LGIRKKR----IDEVLDVVGLKDSAKKKVKG------FSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647959 238 FCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTG 298
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSeiQKVAD---RIGIINKGKLIEEG 208
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
88-301 |
7.21e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.54 E-value: 7.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLmstlaFRQPAGTVV--QGDILINGRRIGPF-MHR-----IsGYVYQDDLF 159
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTT-----FYMIVGLVKpdSGRIFLDGEDITHLpMHKrarlgI-GYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 LGSLTVLEhlNFMAHLRLdRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFC 239
Cdd:COG1137 90 FRKLTVED--NILAVLEL-RKLSKKEREERLEELLEEFGITHLRKSKAYS------LSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647959 240 DEPTTGLDSYSA---QQLVAtlyELAQKGTTILCTIHqpssqlfdnfnNV----------MLLADGRVAFTGSPQ 301
Cdd:COG1137 161 DEPFAGVDPIAVadiQKIIR---HLKERGIGVLITDH-----------NVretlgicdraYIISEGKVLAEGTPE 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
89-305 |
7.21e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.81 E-value: 7.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 89 RIINNSTGAIQPGTLMALMGSSGSGKTTLMSTL-----AFRQPAgtvVQGDILINGRRIGPF----MHRISGYVYQDDLF 159
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEAR---VSGEVYLDGQDIFKMdvieLRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 LGSLTVLEhlNFMAHLRLDRRV-SKEERRLIIKELLERTGLLSAAQTRIGSGDDKkvLSGGERKRLAFAVELLNNPVILF 238
Cdd:PRK14247 94 IPNLSIFE--NVALGLKLNRLVkSKKELQERVRWALEKAQLWDEVKDRLDAPAGK--LSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647959 239 CDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFnnVMLLADGRVAFTG-------SPQHALS 305
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDY--VAFLYKGQIVEWGptrevftNPRHELT 241
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
90-313 |
7.35e-18 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 83.36 E-value: 7.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPagtvVQGDILINGRRIG----PFMHRISGYVYQD-DLFLGsl 163
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErFYDP----TSGEILLDGVDIRdlnlRWLRSQIGLVSQEpVLFDG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLNFMAhlrlDRRVSKEERRLIIKELLER--TGLLSAAQTRIGSGDDKkvLSGGERKRLAFAVELLNNPVILFCDE 241
Cdd:cd03249 92 TIAENIRYGK----PDATDEEVEEAAKKANIHDfiMSLPDGYDTLVGERGSQ--LSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 242 PTTGLDSYSAQQLVATLYELAQKGTTI-----LCTIHqpssqlfdNFNNVMLLADGRVAFTGSPQhalSFFANHGYY 313
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMKGRTTIviahrLSTIR--------NADLIAVLQNGQVVEQGTHD---ELMAQKGVY 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
88-298 |
8.48e-18 |
|
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: 81.59 E-value: 8.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFR-QPAgtvvQGDILINGRRIGPFMHRISGY--VYQDDLFLGSLT 164
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDlKPQ----QGEITLDGVPVSDLEKALSSLisVLNQRPYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 165 VLEHLNfmahlrldrrvskeeRRLiikellertgllsaaqtrigsgddkkvlSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:cd03247 91 LRNNLG---------------RRF----------------------------SGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17647959 245 GLDSYSAQQLVATLYELAqKGTTILCTIHQPSSqlFDNFNNVMLLADGRVAFTG 298
Cdd:cd03247 128 GLDPITERQLLSLIFEVL-KDKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
105-305 |
9.37e-18 |
|
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: 85.16 E-value: 9.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 105 ALMGSSGSGKTTLMSTLA--FRQPAGTVVQGDILINGRRIGPFM---HRISGYVYQDDLFLGSLTVLEHLNFMAhlrldR 179
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAglTRPDEGEIVLNGRTLFDSRKGIFLppeKRRIGYVFQEARLFPHLSVRGNLRYGM-----K 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 180 RVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLY 259
Cdd:TIGR02142 102 RARPSERRISFERVIELLGIGHLLGRLPGR------LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17647959 260 ELAQK-GTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTGSPQHALS 305
Cdd:TIGR02142 176 RLHAEfGIPILYVSHSLQevLRLAD---RVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
90-294 |
1.06e-17 |
|
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: 81.11 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILING---RRIGPFMHR-ISGYVYQDD-LFLGSL 163
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILgLLRPT----SGRVRLDGadiSQWDPNELGdHVGYLPQDDeLFSGSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TvlehlnfmahlrldrrvskeerrliikellertgllsaaqtrigsgddKKVLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:cd03246 93 A------------------------------------------------ENILSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGTTILCTIHQPSsqLFDNFNNVMLLADGRV 294
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGRV 173
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
98-275 |
1.65e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.39 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIgpfmHRISGYVYQDDLFLG-------SLTVLEHL 169
Cdd:PRK13538 24 LNAGELVQIEGPNGAGKTSLLRILAgLARPD----AGEVLWQGEPI----RRQRDEYHQDLLYLGhqpgiktELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 NFMAhlRLDRRVSKEErrliIKELLERTGL-----LSAAQtrigsgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:PRK13538 96 RFYQ--RLHGPGDDEA----LWEALAQVGLagfedVPVRQ-----------LSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|.
gi 17647959 245 GLDSYSAQQLVATLYELAQKGTTILCTIHQP 275
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
98-324 |
2.63e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.86 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTL-AFRQPA-GTVVQGDILING----RRIGPFMHRIsGYVYQ---DDLFlgSLTVLEH 168
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLnGLLQPTeGKVTVGDIVVSStskqKEIKPVRKKV-GVVFQfpeSQLF--EETVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 169 LNFMAHlrlDRRVSKEERRLIIKELLERTGLLSAAQTRigsgdDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDS 248
Cdd:PRK13643 106 VAFGPQ---NFGIPKEKAEKIAAEKLEMVGLADEFWEK-----SPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 249 YSAQQLVATLYELAQKGTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSPQ---HALSFFANHGYYCPEAYNPADFL 324
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHIISCGTPSdvfQEVDFLKAHELGVPKATHFADQL 255
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
98-313 |
3.08e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.60 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILING---RRIGP--FMHRIsGYVYQDDlFLGSLTVLEhlNf 171
Cdd:COG1132 363 IPPGETVALVGPSGSGKSTLVNLLLrFYDPT----SGRILIDGvdiRDLTLesLRRQI-GVVPQDT-FLFSGTIRE--N- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 mahLRL-DRRVSKEE-----RRLIIKELLERT--GLlsaaQTRIGSGDDKkvLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:COG1132 434 ---IRYgRPDATDEEveeaaKAAQAHEFIEALpdGY----DTVVGERGVN--LSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGTTILctI-HQPSS-QLFDnfnNVMLLADGRVAFTGSPQHALsffANHGYY 313
Cdd:COG1132 505 SALDTETEALIQEALERLMKGRTTIV--IaHRLSTiRNAD---RILVLDDGRIVEQGTHEELL---ARGGLY 568
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
86-298 |
3.58e-17 |
|
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: 81.22 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 86 RMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA--FRQPAGTVVQGDILINGRRIGpFMHRISGYVYQDDLFLGSL 163
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSglLQPTSGEVRVAGLVPWKRRKK-FLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLNFMAHL-RLDRRVSKEeRRLIIKELLERTGLLsaaqtrigsgdDKKV--LSGGERKRLAFAVELLNNPVILFCD 240
Cdd:cd03267 111 PVIDSFYLLAAIyDLPPARFKK-RLDELSELLDLEELL-----------DTPVrqLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 241 EPTTGLDSYSAQQLVATLYEL-AQKGTTILCTIH--QPSSQLFDnfnNVMLLADGRVAFTG 298
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHymKDIEALAR---RVLVIDKGRLLYDG 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
90-313 |
3.80e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.26 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfRqpAGTVVQGDILINGRRIGPF--------MHRISGYVYqddLFLG 161
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-R--AWDPQQGEILLNGQPIADYseaalrqaISVVSQRVH---LFSA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 162 SLTvlEHLNFMAHLRLDRRVSkeerrliikELLERTGLLSAAQTRIG----SGDDKKVLSGGERKRLAFAVELLNNPVIL 237
Cdd:PRK11160 429 TLR--DNLLLAAPNASDEALI---------EVLQQVGLEKLLEDDKGlnawLGEGGRQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 238 FCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTiHQpsSQLFDNFNNVMLLADGRVAFTGSPQHALsffANHGYY 313
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHAQNKTVLMIT-HR--LTGLEQFDRICVMDNGQIIEQGTHQELL---AQQGRY 567
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
98-304 |
4.19e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.20 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPAgTvvQGDILINGRRIG--------PFMHRIsGYVYQDDLFLGSLTVLEhl 169
Cdd:COG1135 28 IEKGEIFGIIGYSGAGKSTLIRCINLLERP-T--SGSVLVDGVDLTalserelrAARRKI-GMIFQHFNLLSSRTVAE-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 NFMAHLRLDRrVSKEERRLIIKELLERTGLlsaaqtrigsgDDKKV-----LSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:COG1135 102 NVALPLEIAG-VPKAEIRKRVAELLELVGL-----------SDKADaypsqLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 245 GLDSYSAQQLVATLYELAQK-GTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTGS-------PQHAL 304
Cdd:COG1135 170 ALDPETTRSILDLLKDINRElGLTIVLITHEMDvvRRICD---RVAVLENGRIVEQGPvldvfanPQSEL 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
90-313 |
7.41e-17 |
|
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: 80.22 E-value: 7.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAgtvVQGDILINGRRIG----PFMHRISGYVYQDDLFLgSLTV 165
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP---ENGRVLVDGHDLAladpAWLRRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 166 LEHLNfMAHLRLDRRVSKEERRL-----IIKELLERTGLLSAAQtriGSGddkkvLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:cd03252 93 RDNIA-LADPGMSMERVIEAAKLagahdFISELPEGYDTIVGEQ---GAG-----LSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647959 241 EPTTGLDSYSAQQLVATLYELAqKGTTILCTIHQPSSqlFDNFNNVMLLADGRVAFTGSPQHALsffANHGYY 313
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLST--VKNADRIIVMEKGRIVEQGSHDELL---AENGLY 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
83-275 |
7.48e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.39 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 83 SGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQP-------AGTVV---QGDILINGRRigpfMHriSG 151
Cdd:PRK10535 16 SGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGcLDKPtsgtyrvAGQDVatlDADALAQLRR----EH--FG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 152 YVYQDDLFLGSLTVLEHLNFMAhlrLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELL 231
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPA---VYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ------LSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17647959 232 NNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQP 275
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
98-302 |
8.07e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 8.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTVVQGDILINGR---RIGPFMHRI------SGYVYQDDLFLGSLTVLEH 168
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRtvqREGRLARDIrksranTGYIFQQFNLVNRLSVLEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 169 LNFMAH---------LRLDRRVSKEERRliikELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFC 239
Cdd:PRK09984 107 VLIGALgstpfwrtcFSWFTREQKQRAL----QALTRVGMVHFAHQRVST------LSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647959 240 DEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQPSSQLfDNFNNVMLLADGRVAFTGSPQH 302
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDGSSQQ 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
103-313 |
9.22e-17 |
|
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: 85.07 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 103 LMALMGSSGSGKTTLMSTLAFRQPAgtvVQGDILINGRRIGPFMHRIS---GYVYQDDLFLGSLTVLEHLNFMAHLRldr 179
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLVGGKDIETNLDAVRqslGMCPQHNILFHHLTVAEHILFYAQLK--- 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 180 RVSKEERRLIIKELLERTGLLSAaqtrigSGDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLY 259
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHK------RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17647959 260 ELAQKGTTILCTIHQPSSQLFDnfNNVMLLADGRVAFTGSPQHALSFFANhGYY 313
Cdd:TIGR01257 1106 KYRSGRTIIMSTHHMDEADLLG--DRIAIISQGRLYCSGTPLFLKNCFGT-GFY 1156
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
97-275 |
9.44e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 9.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLAFRQPAgtvVQGDILINGRRIGPFMHR-ISGYVYQDDLFLGSLTVLEHLNFMAHL 175
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPP---AAGTIKLDGGDIDDPDVAeACHYLGHRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 176 RldrrvskEERRLIIKELLERTGLLSAAQTRIGsgddkkVLSGGERKRLAFAvELL--NNPV-ILfcDEPTTGLDSySAQ 252
Cdd:PRK13539 101 L-------GGEELDIAAALEAVGLAPLAHLPFG------YLSAGQKRRVALA-RLLvsNRPIwIL--DEPTAALDA-AAV 163
|
170 180
....*....|....*....|....*
gi 17647959 253 QLVATLYE--LAQKGTTILCTiHQP 275
Cdd:PRK13539 164 ALFAELIRahLAQGGIVIAAT-HIP 187
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
72-305 |
1.06e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.20 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 72 RDLCVytNVGGsgqrmKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIGPF----- 145
Cdd:PRK13548 6 RNLSV--RLGG-----RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPD----SGEVRLNGRPLADWspael 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 146 -MHRisgyvyqddlflgslTVL---EHLNF---------MAhlRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgdd 212
Cdd:PRK13548 75 aRRR---------------AVLpqhSSLSFpftveevvaMG--RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQ--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 213 kkvLSGGERKRLAFAVELL------NNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHqpssqlfdNFN- 284
Cdd:PRK13548 135 ---LSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLH--------DLNl 203
|
250 260
....*....|....*....|....*..
gi 17647959 285 ------NVMLLADGRVAFTGSPQHALS 305
Cdd:PRK13548 204 aaryadRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
88-273 |
1.32e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTT-LMSTLAFRQP-AGTVVQGDILINGRriGPFMHRISGYVYQDDLFLGSLTV 165
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTtLRMLLGLTHPdAGSISLCGEPVPSR--ARHARQRVGVVPQFDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 166 LEHLN-FMAHLRLdrrvSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:PRK13537 98 RENLLvFGRYFGL----SAAAARALVPPLLEFAKLENKADAKVGE------LSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180
....*....|....*....|....*....
gi 17647959 245 GLDSYSAQQLVATLYELAQKGTTILCTIH 273
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
84-303 |
1.56e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.22 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 84 GQRMKRIINNSTGAIQPGTLMALMGSSGSGKT-TLMSTLAFrQPAGTVV--QGDILINGRRI----GPFMHRISG----Y 152
Cdd:PRK15134 18 QQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRL-LPSPPVVypSGDIRFHGESLlhasEQTLRGVRGnkiaM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 153 VYQDDLF-LGSLTVLEHlNFMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQtRIGsgDDKKVLSGGERKRLAFAVELL 231
Cdd:PRK15134 97 IFQEPMVsLNPLHTLEK-QLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAK-RLT--DYPHQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 232 NNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQPSS--QLFDnfnNVMLLADGRV-------AFTGSPQ 301
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIvrKLAD---RVAVMQNGRCveqnraaTLFSAPT 249
|
..
gi 17647959 302 HA 303
Cdd:PRK15134 250 HP 251
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
82-294 |
2.69e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.67 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 82 GSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqGDIlingRRIGPFMHRIS----------- 150
Cdd:PRK10584 17 GQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSS---GEV----SLVGQPLHQMDeearaklrakh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 151 -GYVYQDDLFLGSLTVLEHLNFMAHLRLDrrvSKEERRLIIKELLERTGLLS-----AAQtrigsgddkkvLSGGERKRL 224
Cdd:PRK10584 90 vGFVFQSFMLIPTLNALENVELPALLRGE---SSRQSRNGAKALLEQLGLGKrldhlPAQ-----------LSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 225 AFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQPssQLFDNFNNVMLLADGRV 294
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL--QLAARCDRRLRLVNGQL 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
72-269 |
4.46e-16 |
|
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: 81.65 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 72 RDLCVYTnvgGSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKT-TLMSTLAFRQPAGTVVQGDILINGRRIGPF----M 146
Cdd:COG4172 10 EDLSVAF---GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAHPSGSILFDGQDLLGLsereL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 147 HRISG----YVYQDDLflGSL----TVLEHLnfMAHLRLDRRVSKEERRLIIKELLERTGLlSAAQTRIGSgddkkvLSG 218
Cdd:COG4172 87 RRIRGnriaMIFQEPM--TSLnplhTIGKQI--AEVLRLHRGLSGAAARARALELLERVGI-PDPERRLDAyp--hqLSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17647959 219 GERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTIL 269
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALL 211
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
85-305 |
7.31e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.33 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 85 QRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFR-----QPAGTVVQGDILINGRRI----GPFMHRISGYVYQ 155
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggAPRGARVTGDVTLNGEPLaaidAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 156 --DDLFLGSLTVLEHLNFMAHLRLDRRVSKEERRlIIKELLERTGllsaAQTRIGSgdDKKVLSGGERKRLAFAVEL--- 230
Cdd:PRK13547 91 aaQPAFAFSAREIVLLGRYPHARRAGALTHRDGE-IAWQALALAG----ATALVGR--DVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 231 ------LNNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQPSSQLfDNFNNVMLLADGRVAFTGSPQHA 303
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPADV 242
|
..
gi 17647959 304 LS 305
Cdd:PRK13547 243 LT 244
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
88-303 |
1.10e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.83 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTL--AFRQPAGTVVQGDILINGRRIG------PFMHRISGYVYQDDLF 159
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGYRYSGDVLLGGRSIFnyrdvlEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 lgSLTVLEhlNFMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGsgDDKKVLSGGERKRLAFAVELLNNPVILFC 239
Cdd:PRK14271 114 --PMSIMD--NVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLS--DSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 240 DEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDnfNNVMLLADGRVAFTG-------SPQHA 303
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIS--DRAALFFDGRLVEEGpteqlfsSPKHA 256
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
105-305 |
1.14e-15 |
|
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: 78.99 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 105 ALMGSSGSGKTTLMSTLA--FRQPAGTV-VQGDILINGRRiGPFM--H--RIsGYVYQDD-LFLgSLTVLEHLNFmAHlr 176
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAglERPDSGRIrLGGEVLQDSAR-GIFLppHrrRI-GYVFQEArLFP-HLSVRGNLLY-GR-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 177 ldRRVSKEERRL----IIkELLERTGLLsaaqtrigsgdDKKV--LSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYS 250
Cdd:COG4148 103 --KRAPRAERRIsfdeVV-ELLGIGHLL-----------DRRPatLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 251 AQQLVATLYELAQK-GTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTGSPQHALS 305
Cdd:COG4148 169 KAEILPYLERLRDElDIPILYVSHSLDevARLAD---HVVLLEQGRVVASGPLAEVLS 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
88-305 |
1.19e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.36 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfRQpaGTVVQGDILINGRRIGPF----MHRISGYVYQDDLFLGSL 163
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RL--LTPQSGTVFLGDKPISMLssrqLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLNF--MAHLRLDRRVSKEERRLiIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDE 241
Cdd:PRK11231 92 TVRELVAYgrSPWLSLWGRLSAEDNAR-VNQAMEQTRINHLADRRLTD------LSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 242 PTTGLDSYSAQQLVATLYELAQKGTTILCTIH--QPSSQLFDnfnNVMLLADGRVAFTGSPQHALS 305
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlNQASRYCD---HLVVLANGHVMAQGTPEEVMT 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
90-305 |
1.37e-15 |
|
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: 80.18 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfrqpaG--TVVQGDILING--------RRIGPFMhrisGYVYQD-DL 158
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV-----GvwPPTAGSVRLDGadlsqwdrEELGRHI----GYLPQDvEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 159 FLGslTVLEhlNfMAhlrldrRVSKEERRLIIKellertgllsAAQ----------------TRIGSGDdkKVLSGGERK 222
Cdd:COG4618 418 FDG--TIAE--N-IA------RFGDADPEKVVA----------AAKlagvhemilrlpdgydTRIGEGG--ARLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 223 RLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSsqLFDNFNNVMLLADGRVAFTGSPQH 302
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDGRVQAFGPRDE 552
|
...
gi 17647959 303 ALS 305
Cdd:COG4618 553 VLA 555
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
63-280 |
1.81e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.85 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 63 TEQGATLVWRDLCVYTNVGgsgqrmKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqGDILI-NGRR 141
Cdd:COG4178 357 TSEDGALALEDLTLRTPDG------RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGS---GRIARpAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 142 IgpfmhrisgyvyqddLFL--------GSL-TVLehlnfmAHLRLDRRVSKEErrliIKELLERTGLlSAAQTRIGSGDD 212
Cdd:COG4178 428 V---------------LFLpqrpylplGTLrEAL------LYPATAEAFSDAE----LREALEAVGL-GHLAERLDEEAD 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 213 -KKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYElAQKGTTILCTIHQPSSQLF 280
Cdd:COG4178 482 wDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAF 549
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
98-300 |
2.57e-15 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 75.61 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLaFR--QPAGtvvqGDILINGR---RIGPFM--HRISGyVYQDD-LFLGSLtvlehl 169
Cdd:cd03244 27 IKPGEKVGIVGRTGSGKSSLLLAL-FRlvELSS----GSILIDGVdisKIGLHDlrSRISI-IPQDPvLFSGTI------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 nfmahlR--LD--RRVSKEErrliIKELLERTGLLSAAQTRIGSGDDK-----KVLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:cd03244 95 ------RsnLDpfGEYSDEE----LWQALERVGLKEFVESLPGGLDTVveeggENLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 241 EPTTGLDSYSAQQLVATLYElAQKGTTILCTIHQPSSQLfdNFNNVMLLADGRVAFTGSP 300
Cdd:cd03244 165 EATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTII--DSDRILVLDKGRVVEFDSP 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
88-304 |
2.77e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqGDILINGRRIgPFMHRIS----GYVYQDDLFLGSL 163
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA---GKITVLGVPV-PARARLArariGVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHL-NFMAHLRLDRRVSKEerrlIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:PRK13536 130 TVRENLlVFGRYFGMSTREIEA----VIPSLLEFARLESKADARVSD------LSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647959 243 TTGLDSYSAQQLVATLYELAQKGTTILCTIH--QPSSQLFDnfnNVMLLADGRVAFTGSPqHAL 304
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHfmEEAERLCD---RLCVLEAGRKIAEGRP-HAL 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
98-269 |
2.94e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQP-AGTvvqgdILINGRRIgpfmhRIS----------GYVYQDDLFLGSLTV 165
Cdd:COG3845 28 VRPGEIHALLGENGAGKSTLMKILYgLYQPdSGE-----ILIDGKPV-----RIRsprdaialgiGMVHQHFMLVPNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 166 LEhlNFM------AHLRLDRRvsKEERRliIKELLERTGLlsaaqtRIgsgD-DKKV--LSGGERKRlafaVE----LLN 232
Cdd:COG3845 98 AE--NIVlgleptKGGRLDRK--AARAR--IRELSERYGL------DV---DpDAKVedLSVGEQQR----VEilkaLYR 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 17647959 233 NPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTIL 269
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
88-247 |
4.14e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQP--AGTVVQGdilingrrigpfmHRIS-GYVYQD-DLFLGSL 163
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpdSGTVKLG-------------ETVKiGYFDQHqEELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLnfmahlrldRRVSKEERRLIIKELLERTGLlsaaqtrigSGDD--KKV--LSGGERKRLAFAVELLNNPVILFC 239
Cdd:COG0488 395 TVLDEL---------RDGAPGGTEQEVRGYLGRFLF---------SGDDafKPVgvLSGGEKARLALAKLLLSPPNVLLL 456
|
....*...
gi 17647959 240 DEPTTGLD 247
Cdd:COG0488 457 DEPTNHLD 464
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
98-305 |
4.94e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.13 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQpagTVVQGDILINGRRI-GP-----FMHRISGYVYQDDLFLGSLTVLEhlNF 171
Cdd:PRK09493 24 IDQGEVVVIIGPSGSGKSTLLRCINKLE---EITSGDLIVDGLKVnDPkvderLIRQEAGMVFQQFYLFPHLTALE--NV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 MAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSA 251
Cdd:PRK09493 99 MFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSE------LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 252 QQLVATLYELAQKGTTILCTIH------QPSSQLfdnfnnvMLLADGRVAFTGSPQHALS 305
Cdd:PRK09493 173 HEVLKVMQDLAEEGMTMVIVTHeigfaeKVASRL-------IFIDKGRIAEDGDPQVLIK 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
98-294 |
6.47e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.53 E-value: 6.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTL-AFRQPAGtvvqGDILINGRRIG-------PFMHRISGYVYQDDlflgsltvlehl 169
Cdd:PRK10908 25 MRPGEMAFLTGHSGAGKSTLLKLIcGIERPSA----GKIWFSGHDITrlknrevPFLRRQIGMIFQDH------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 nfmaHLRLDRRV-------------SKEERRLIIKELLERTGLLSAAQTRigsgddKKVLSGGERKRLAFAVELLNNPVI 236
Cdd:PRK10908 89 ----HLLMDRTVydnvaipliiagaSGDDIRRRVSAALDKVGLLDKAKNF------PIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 237 LFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFnNVMLLADGRV 294
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSY-RMLTLSDGHL 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
97-358 |
6.50e-15 |
|
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: 78.90 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTlmstlAFRQPAG--TVVQGDILINGRRIGPFM---HRISGYVYQDDLFLGSLTVLEHLNF 171
Cdd:TIGR01257 1961 GVRPGECFGLLGVNGAGKTT-----TFKMLTGdtTVTSGDATVAGKSILTNIsdvHQNMGYCPQFDAIDDLLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 MAHLRldrRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSA 251
Cdd:TIGR01257 2036 YARLR---GVPAEEIEKVANWSIQSLGLSLYADRLAGT------YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 252 QQLVATLYELAQKGTTILCTIHqpSSQLFDNF-NNVMLLADGRVAFTGSPQHALSFFANHGYYCPEAYNPADFLIGVLAT 330
Cdd:TIGR01257 2107 RMLWNTIVSIIREGRAVVLTSH--SMEECEALcTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDLLPDLNP 2184
|
250 260 270
....*....|....*....|....*....|...
gi 17647959 331 DPGYEQAS-----QRSAQHLCDQFAVSSAAKQR 358
Cdd:TIGR01257 2185 VEQFFQGNfpgsvQRERHYNMLQFQVSSSSLAR 2217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
96-302 |
6.98e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.83 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 96 GAIQPGTLMALMGSSGSGKTTLMSTL-AFRQPA-GTVVQGDILI----NGRRIGPFMHRIsGYVYQ---DDLFlgSLTVL 166
Cdd:PRK13634 28 VSIPSGSYVAIIGHTGSGKSTLLQHLnGLLQPTsGTVTIGERVItagkKNKKLKPLRKKV-GIVFQfpeHQLF--EETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 EH-----LNFmahlrldrRVSKEERRLIIKELLERTGLLSAAQTRigSGDDkkvLSGGERKRLAFAVELLNNPVILFCDE 241
Cdd:PRK13634 105 KDicfgpMNF--------GVSEEDAKQKAREMIELVGLPEELLAR--SPFE---LSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647959 242 PTTGLDSYSAQQLVATLYELAQKG--TTILCTiHQ--PSSQLFDnfnNVMLLADGRVAFTGSPQH 302
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKglTTVLVT-HSmeDAARYAD---QIVVMHKGTVFLQGTPRE 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
98-273 |
7.10e-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: 73.83 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIG--PFMHRISGYVYQDDLFLGSLTVLEHLNFMAH 174
Cdd:cd03301 23 IADGEFVVLLGPSGCGKTTTLRMIAgLEEPTS----GRIYIGGRDVTdlPPKDRDIAMVFQNYALYPHMTVYDNIAFGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 175 LR------LDRRVSKEERRLIIKELLERTgllsaaqtrigsgddKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDS 248
Cdd:cd03301 99 LRkvpkdeIDERVREVAELLQIEHLLDRK---------------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180
....*....|....*....|....*.
gi 17647959 249 YSAQQLVATLYELAQK-GTTILCTIH 273
Cdd:cd03301 164 KLRVQMRAELKRLQQRlGTTTIYVTH 189
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
101-275 |
1.49e-14 |
|
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: 72.91 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 101 GTLMALMGSSGSGKTTLMSTLAFRQPAgtvVQGDILINGR---RIGPFMHRISGYVYQDDLFLGSLTVLEHLNFMAHLRL 177
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPP---LAGRVLLNGGpldFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 178 DRRvskeerrliIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVAT 257
Cdd:cd03231 103 DEQ---------VEEALARVGLNGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*...
gi 17647959 258 LYELAQKGTTILCTIHQP 275
Cdd:cd03231 168 MAGHCARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
98-301 |
2.43e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTL-AFRQPA-GTVVQGDILING----RRIGPFMHRIsGYVYQ---DDLFlgSLTVLEH 168
Cdd:PRK13649 30 IEDGSYTAFIGHTGSGKSTIMQLLnGLHVPTqGSVRVDDTLITStsknKDIKQIRKKV-GLVFQfpeSQLF--EETVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 169 LNFMAHlrlDRRVSKEERRLIIKELLERTGLLSAAQTRigsgdDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDS 248
Cdd:PRK13649 107 VAFGPQ---NFGVSQEEAEALAREKLALVGISESLFEK-----NPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 249 YSAQQLVATLYELAQKGTTILCTIHqpssqLFDNFNN----VMLLADGRVAFTGSPQ 301
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTH-----LMDDVANyadfVYVLEKGKLVLSGKPK 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
98-301 |
2.47e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.73 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTL-AFRQPagtvVQGDILINGR-----RIGPFMHRIS-GYVYQD-DLFLGSLTVLEHL 169
Cdd:PRK13636 29 IKKGEVTAILGGNGAGKSTLFQNLnGILKP----SSGRILFDGKpidysRKGLMKLRESvGMVFQDpDNQLFSASVYQDV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 NFMAhlrLDRRVSKEERRLIIKELLERTGllsaaqtrIGSGDDKKV--LSGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:PRK13636 105 SFGA---VNLKLPEDEVRKRVDNALKRTG--------IEHLKDKPThcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 248 SYSAQQLVATLYELAQK-GTTILCTIHQPSS-QLFdnFNNVMLLADGRVAFTGSPQ 301
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKElGLTIIIATHDIDIvPLY--CDNVFVMKEGRVILQGNPK 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
62-309 |
3.00e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.04 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 62 PTEQGATLVWRDLCVYTNVGgsgqrmKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPagtvVQGDILING-- 139
Cdd:PRK11174 343 ASNDPVTIEAEDLEILSPDG------KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP----YQGSLKINGie 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 140 -RRIGP--FMHRISgYVYQD-DLFLGSLtvlehlnfMAHLRLDRRVSKEERrliIKELLERTG-------LLSAAQTRIG 208
Cdd:PRK11174 413 lRELDPesWRKHLS-WVGQNpQLPHGTL--------RDNVLLGNPDASDEQ---LQQALENAWvseflplLPQGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 209 sgDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTiHQpSSQLfDNFNNVML 288
Cdd:PRK11174 481 --DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQ-LEDL-AQWDQIWV 555
|
250 260
....*....|....*....|....
gi 17647959 289 LADGRVAFTGSPQ---HALSFFAN 309
Cdd:PRK11174 556 MQDGQIVQQGDYAelsQAGGLFAT 579
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
88-305 |
3.05e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTlmstlAFRQPAGTVVQ--GDILINGRRIG--PFMHRIS---GYVYQDDLFL 160
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTT-----TFYMVVGIVPRdaGNIIIDDEDISllPLHARARrgiGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSLTVLEhlNFMAHLRLDRRVSKEERRLIIKELLERtglLSAAQTRIGSGddkKVLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:PRK10895 91 RRLSVYD--NLMAVLQIRDDLSAEQREDRANELMEE---FHIEHLRDSMG---QSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647959 241 EPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLfDNFNNVMLLADGRVAFTGSPQHALS 305
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
102-276 |
7.38e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.80 E-value: 7.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 102 TLMALMGSSGSGKTTLMST----LAFRQPAGtvVQGDILINGRRI-GPFMHRIS-----GYVYQDDLFLGSLTVLEhlNF 171
Cdd:PRK14267 31 GVFALMGPSGCGKSTLLRTfnrlLELNEEAR--VEGEVRLFGRNIySPDVDPIEvrrevGMVFQYPNPFPHLTIYD--NV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 MAHLRLDRRV-SKEERRLIIKELLERTGLLSAAQTRIGsgDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYS 250
Cdd:PRK14267 107 AIGVKLNGLVkSKKELDERVEWALKKAALWDEVKDRLN--DYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVG 184
|
170 180
....*....|....*....|....*.
gi 17647959 251 AQQLVATLYELAQKGTTILCTiHQPS 276
Cdd:PRK14267 185 TAKIEELLFELKKEYTIVLVT-HSPA 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
91-277 |
8.78e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.22 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLmstlaFRQPAGTV--VQGDILINGRRIGPFMHR-ISGYVYQDDLFLGSLTVL- 166
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTL-----FKALMGFVrlASGKISILGQPTRQALQKnLVAYVPQSEEVDWSFPVLv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 EHLNFMA---HLRLDRRVSKEERRlIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:PRK15056 98 EDVVMMGrygHMGWLRRAKKRDRQ-IVTAALARVDMVEFRHRQIGE------LSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|....
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGTTILCTIHQPSS 277
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGS 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
91-309 |
9.06e-14 |
|
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: 71.56 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfRQPAGTvvQGDILINGRRIGPF----MHRISGYVYQDDLFLGSLTVL 166
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN-RLIEPT--SGEIFIDGEDIREQdpveLRRKIGYVIQQIGLFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 EHLNFMAHLrldRRVSKEERRLIIKELLERTGLLSAAQTRIGSGDdkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGL 246
Cdd:cd03295 94 ENIALVPKL---LKWPKEKIRERADELLALVGLDPAEFADRYPHE----LSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 247 DSYSAQQLVATLYELAQK-GTTILCTIH--QPSSQLFDnfnNVMLLADGRVAFTGSPQHALSFFAN 309
Cdd:cd03295 167 DPITRDQLQEEFKRLQQElGKTIVFVTHdiDEAFRLAD---RIAIMKNGEIVQVGTPDEILRSPAN 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
90-294 |
1.60e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 70.19 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIG----PFMHRISGYVYQDD-LFLGSL 163
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnFYQPQG----GQVLLDGKPISqyehKYLHSKVSLVGQEPvLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TvlEHLNF-MAHLRLDRrvskeerrliIKELLER-------TGLLSAAQTriGSGDDKKVLSGGERKRLAFAVELLNNPV 235
Cdd:cd03248 105 Q--DNIAYgLQSCSFEC----------VKEAAQKahahsfiSELASGYDT--EVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 236 ILFCDEPTTGLDSYSAQQLVATLYELAQKgTTILCTIHQPSsqLFDNFNNVMLLADGRV 294
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLS--TVERADQILVLDGGRI 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
98-269 |
2.63e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqGDILINGRRIGPF------MHRISgYVYQDDLFLGSLTVLEHLnF 171
Cdd:COG1129 27 LRPGEVHALLGENGAGKSTLMKILSGVYQPDS---GEILLDGEPVRFRsprdaqAAGIA-IIHQELNLVPNLSVAENI-F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 MAHL-----RLDRRvsKEERRliIKELLERTGL-LSAAqTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTG 245
Cdd:COG1129 102 LGREprrggLIDWR--AMRRR--ARELLARLGLdIDPD-TPVGD------LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180
....*....|....*....|....
gi 17647959 246 LDSYSAQQLVATLYELAQKGTTIL 269
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQGVAII 194
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
98-305 |
2.66e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.00 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILING---RRIGPFMHRISGYVYQDDLFlGSLTVLEHLNFMA 173
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAgFLTPA----SGSLTLNGqdhTTTPPSRRPVSMLFQENNLF-SHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 174 H--LRLD----RRVSKEERRLIIKELLERtglLSAAqtrigsgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:PRK10771 97 NpgLKLNaaqrEKLHAIARQMGIEDLLAR---LPGQ------------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 248 SYSAQQLVATLYEL-AQKGTTILCTIHQ--------PSSqlfdnfnnvMLLADGRVAFTGSPQHALS 305
Cdd:PRK10771 162 PALRQEMLTLVSQVcQERQLTLLMVSHSledaariaPRS---------LVVADGRIAWDGPTDELLS 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
91-322 |
4.24e-13 |
|
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: 69.98 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTL-AFRQPAGtvvqGDILINGRRIGPF---------MHRISgYVYQDDLFL 160
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCInRLIEPTS----GKVLIDGQDIAAMsrkelrelrRKKIS-MVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSLTVLEHLNFMAHLRldrRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:cd03294 115 PHRTVLENVAFGLEVQ---GVPRAEREERAAEALELVGLEGWEHKYPDE------LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 241 EPTTGLDSYSAQQLVATLYEL-AQKGTTILCTIHQPSSQLFDNfNNVMLLADGRVAFTGSPQHALSffanhgyycpeayN 319
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLG-DRIAIMKDGRLVQVGTPEEILT-------------N 251
|
...
gi 17647959 320 PAD 322
Cdd:cd03294 252 PAN 254
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
72-271 |
5.14e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.42 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 72 RDLCVYTNvggsgqrMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfRQ----PAGTVVqGDILINGRRI-GPFM 146
Cdd:PRK14239 9 SDLSVYYN-------KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN-RMndlnPEVTIT-GSIVYNGHNIySPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 147 HRIS-----GYVYQD-DLFlgSLTVLEhlNFMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGsgDDKKVLSGGE 220
Cdd:PRK14239 80 DTVDlrkeiGMVFQQpNPF--PMSIYE--NVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLH--DSALGLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17647959 221 RKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCT 271
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
88-247 |
5.26e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqGDILI-NGRRIGpfmhrisgYVYQDDLFLGSLTVL 166
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDS---GEVSIpKGLRIG--------YLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 EHLnFMAHLRLdRRVSKEERRLIIK-----ELLERtglLSAAQTRIGSGD----------------------DKKV--LS 217
Cdd:COG0488 80 DTV-LDGDAEL-RALEAELEELEAKlaepdEDLER---LAELQEEFEALGgweaearaeeilsglgfpeedlDRPVseLS 154
|
170 180 190
....*....|....*....|....*....|
gi 17647959 218 GGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
98-299 |
5.44e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.50 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAfrqpaGTVV--QGDILINGRRigPFMHRISgYVYQDDLFLGS-------LTVLEH 168
Cdd:COG4586 45 IEPGEIVGFIGPNGAGKSTTIKMLT-----GILVptSGEVRVLGYV--PFKRRKE-FARRIGVVFGQrsqlwwdLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 169 LNFMAHL-RLDRRVSKEERRLIIkELLERTGLLsaaqtrigsgdDKKV--LSGGERKRLAFAVELLNNPVILFCDEPTTG 245
Cdd:COG4586 117 FRLLKAIyRIPDAEYKKRLDELV-ELLDLGELL-----------DTPVrqLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 246 LDSYSAQQLVATLYEL-AQKGTTILCTIHqpssqlfdNF-------NNVMLLADGRVAFTGS 299
Cdd:COG4586 185 LDVVSKEAIREFLKEYnRERGTTILLTSH--------DMddiealcDRVIVIDHGRIIYDGS 238
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
89-305 |
6.56e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 89 RIINNSTGAIQPGTLMALMGSSGSGKTTLMSTL--AFRQPAGTVVQGDILINGRRIGPFMHRISGyVYQDDLFLGSLTVL 166
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIngTLTPTAGTVLVAGDDVEALSARAASRRVAS-VPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 E--HLNFMAHL-RLDRRVSKEERrlIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:PRK09536 96 QvvEMGRTPHRsRFDTWTETDRA--AVERAMERTGVAQFADRPVTS------LSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGTTILCTIHqpSSQLFDNF-NNVMLLADGRVAFTGSPQHALS 305
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADGRVRAAGPPADVLT 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
101-328 |
8.39e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.84 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 101 GTLMALMGSSGSGKTTLMSTLAF-RQPAgtvvQGDILINGRRIGpFMHRISGYV-----YQDDLFLGSLT-VLEHLNFMA 173
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFlEKPS----EGSIVVNGQTIN-LVRDKDGQLkvadkNQLRLLRTRLTmVFQHFNLWS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 174 HLRLDRRV----------SKEERRLIIKELLERTGLLSAAQTRIGSGddkkvLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:PRK10619 106 HMTVLENVmeapiqvlglSKQEARERAVKYLAKVGIDERAQGKYPVH-----LSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNfNNVMLLADGRVAFTGSPQhalSFFANhgyycPEAYNPADF 323
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVS-SHVIFLHQGKIEEEGAPE---QLFGN-----PQSPRLQQF 251
|
....*
gi 17647959 324 LIGVL 328
Cdd:PRK10619 252 LKGSL 256
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
98-272 |
8.83e-13 |
|
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: 71.39 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLmSTLAFRqpAGTVVQGDILINGRRIGPF----MHRISGYVYQDdlflgslTVLehlnF-- 171
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTL-ARLLFR--FYDVTSGRILIDGQDIRDVtqasLRAAIGIVPQD-------TVL----Fnd 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 -----MAHLRLDrrVSKEE-----RRLIIKELLERT--GLlsaaQTRIGSGDDKkvLSGGERKRLAFAVELLNNPVILFC 239
Cdd:COG5265 447 tiaynIAYGRPD--ASEEEveaaaRAAQIHDFIESLpdGY----DTRVGERGLK--LSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|....*...
gi 17647959 240 DEPTTGLDSYSAQQLVATLYELAQKGTTI-----LCTI 272
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVARGRTTLviahrLSTI 556
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
88-299 |
1.77e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.76 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFR---QPAGTVVQGDILINGRRIGPF----MHRISGYVYQDDLFL 160
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKIKVDGKVLYFGKDIFQIdaikLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSLTVLEHLNFmaHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSGDDKkvLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:PRK14246 103 PHLSIYDNIAY--PLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQ--LSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 241 EPTTGLDSYSAQQLVATLYELAQKGTTILCTiHQPsSQLFDNFNNVMLLADGRVAFTGS 299
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNP-QQVARVADYVAFLYNGELVEWGS 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
98-294 |
2.51e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAfRQPAGTvvQGDILINGRRI-----GPFMHRISGYVYQDDLFLGSLTVLEHLNfM 172
Cdd:PRK11614 28 INQGEIVTLIGANGAGKTTLLGTLC-GDPRAT--SGRIVFDGKDItdwqtAKIMREAVAIVPEGRRVFSRMTVEENLA-M 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 173 AHLRLDRRvSKEERRLIIKELLERtgLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQ 252
Cdd:PRK11614 104 GGFFAERD-QFQERIKWVYELFPR--LHERRIQRAGT------MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17647959 253 QLVATLYELAQKGTTILcTIHQPSSQLFDNFNNVMLLADGRV 294
Cdd:PRK11614 175 QIFDTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
88-305 |
3.87e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.93 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQpagTVVQGDILINGRRIGPF----MHRISGYVYQDDLFLGSL 163
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM---TPAHGHVWLDGEHIQHYaskeVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHL--NFMAHLRLDRRVSKEERRLIIKELlERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDE 241
Cdd:PRK10253 97 TVQELVarGRYPHQPLFTRWRKEDEEAVTKAM-QATGITHLADQSVDT------LSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647959 242 PTTGLDSYSAQQLVATLYEL-AQKGTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSPQHALS 305
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELnREKGYTLAAVLHD-LNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
90-300 |
5.79e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.18 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTL--AFRQPAGTVVQGDILING-------------RRIGPF--MHRISGY 152
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFngLIKSKYGTIQVGDIYIGDkknnhelitnpysKKIKNFkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 153 VYQ-DDLFLGSLTVLEHLNFMAhlrLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSGddkkvLSGGERKRLAFAVELL 231
Cdd:PRK13631 121 VFQfPEYQLFKDTIEKDIMFGP---VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFG-----LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 232 NNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSP 300
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
89-301 |
7.28e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 89 RIINNSTGAIQPGTLMALMGSSGSGKTTLMstlafRQPAGTVVQ--GDILINGRRIGPfMH---RISGYVYQDDLFLGSL 163
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLL-----RIIAGLEHQtsGHIRFHGTDVSR-LHardRKVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLNF-MAHLRLDRRVSKEERRLIIKELLERTGLLSAAQtRIGSGddkkvLSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:PRK10851 90 TVFDNIAFgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLAD-RYPAQ-----LSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 243 TTGLDSYSAQQLVATLYELAQ--KGTTILCTIHQpsSQLFDNFNNVMLLADGRVAFTGSPQ 301
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQ--EEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
69-312 |
1.01e-11 |
|
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: 64.47 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 69 LVWRDLCVYtnVGGsgqrmKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRqPAGTVVQGDILINGR-------- 140
Cdd:cd03217 1 LEIKDLHVS--VGG-----KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEVTEGEILFKGEditdlppe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 141 ---RIGPFMH-----RISGyvyqddlflgsLTVLEHLNFmahlrldrrvskeerrliikellertgllsaaqtrIGSGdd 212
Cdd:cd03217 73 eraRLGIFLAfqyppEIPG-----------VKNADFLRY-----------------------------------VNEG-- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 213 kkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPssQLFDNF--NNVMLLA 290
Cdd:cd03217 105 ---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQ--RLLDYIkpDRVHVLY 179
|
250 260
....*....|....*....|..
gi 17647959 291 DGRVAFTGSPQHALSfFANHGY 312
Cdd:cd03217 180 DGRIVKSGDKELALE-IEKKGY 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
88-264 |
1.06e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTlmSTLAFRQPAGTvvQGDILING--------RRIGPFMHRISgYVYQDDLf 159
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLRLINS--QGEIWFDGqplhnlnrRQLLPVRHRIQ-VVFQDPN- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 lGSLTV-LEHLNFMAH-LRLDRR-VSKEERRLIIKELLERTGLLSAAQTRIGSGddkkvLSGGERKRLAFAVELLNNPVI 236
Cdd:PRK15134 373 -SSLNPrLNVLQIIEEgLRVHQPtLSAAQREQQVIAVMEEVGLDPETRHRYPAE-----FSGGQRQRIAIARALILKPSL 446
|
170 180
....*....|....*....|....*...
gi 17647959 237 LFCDEPTTGLDSYSAQQLVATLYELAQK 264
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
98-304 |
1.40e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 66.36 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTL-AFRQPAGtvvqGDILING---------------RRIGP-FMHrisgyvyqddlF- 159
Cdd:PRK11153 28 IPAGEIFGVIGASGAGKSTLIRCInLLERPTS----GRVLVDGqdltalsekelrkarRQIGMiFQH-----------Fn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 -LGSLTVLEHLNFmaHLRLDRrVSKEERRLIIKELLERTGLlsaaqtrigsgDDKK-----VLSGGERKRLAFAVELLNN 233
Cdd:PRK11153 93 lLSSRTVFDNVAL--PLELAG-TPKAEIKARVTELLELVGL-----------SDKAdrypaQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 234 PVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTGS-------PQHA 303
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDvvKRICD---RVAVIDAGRLVEQGTvsevfshPKHP 235
|
.
gi 17647959 304 L 304
Cdd:PRK11153 236 L 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
88-247 |
1.78e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.12 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIG--PFMHRISGYVYQDDLFLGSLT 164
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAgFETPD----SGRIMLDGQDIThvPAENRHVNTVFQSYALFPHMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 165 VLEHLNFmaHLRLdRRVSKEERRLIIKELLERTGLLSAAQTRIgsgddkKVLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:PRK09452 103 VFENVAF--GLRM-QKTPAAEITPRVMEALRMVQLEEFAQRKP------HQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
...
gi 17647959 245 GLD 247
Cdd:PRK09452 174 ALD 176
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
77-306 |
2.20e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.71 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 77 YTNVGGSGQR-MKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIGPF-------MH 147
Cdd:PRK10419 13 YAHGGLSGKHqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVgLESPS----QGNVSWRGEPLAKLnraqrkaFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 148 RISGYVYQDDL--FLGSLTVLEHLNF-MAHLrldRRVSKEERRLIIKELLERTGL-LSAAQTRIGSgddkkvLSGGERKR 223
Cdd:PRK10419 89 RDIQMVFQDSIsaVNPRKTVREIIREpLRHL---LSLDKAERLARASEMLRAVDLdDSVLDKRPPQ------LSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 224 LAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQPSsqLFDNF-NNVMLLADGRVAFTGSPQ 301
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLR--LVERFcQRVMVMDNGQIVETQPVG 237
|
....*
gi 17647959 302 HALSF 306
Cdd:PRK10419 238 DKLTF 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
88-275 |
2.65e-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: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfRQPAGTVVQGDILIngrrigpfmhrisgyvyQDDLFLGSLTVLE 167
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA-GALKGTPVAGCVDV-----------------PDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 168 HlnfmahlrLDRRVSKEErrliIKELLERTGLLSAAQTRigsgddKKV--LSGGERKRLAFAVELLNNPVILFCDEPTTG 245
Cdd:COG2401 105 A--------IGRKGDFKD----AVELLNAVGLSDAVLWL------RRFkeLSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|.
gi 17647959 246 LDSYSAQQLVATLYELAQK-GTTILCTIHQP 275
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRaGITLVVATHHY 197
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
88-294 |
3.03e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.67 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIGPF----MHRISGYVYQDD-LFLG 161
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnLYQPTG----GQVLLDGVPLVQYdhhyLHRQVALVGQEPvLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 162 SLTVlehlNFMAHLRldrRVSKEERRLIIKELLER---TGLLSAAQTRIGSGDDKkvLSGGERKRLAFAVELLNNPVILF 238
Cdd:TIGR00958 570 SVRE----NIAYGLT---DTPDEEIMAAAKAANAHdfiMEFPNGYDTEVGEKGSQ--LSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 239 CDEPTTGLDSYSAQqlvaTLYEL-AQKGTTILCTIHQPSsqLFDNFNNVMLLADGRV 294
Cdd:TIGR00958 641 LDEATSALDAECEQ----LLQESrSRASRTVLLIAHRLS--TVERADQILVLKKGSV 691
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
91-334 |
3.24e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.83 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTL-AFRQPAgtvvQGDILINGRRIGPF--------MHRISGYVYQDDLFLG 161
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLnRLIEPT----RGQVLIDGVDIAKIsdaelrevRRKKIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 162 SLTVLEHLNFMAHLRldrRVSKEERRLIIKELLERTGLLSAAQtriGSGDDkkvLSGGERKRLAFAVELLNNPVILFCDE 241
Cdd:PRK10070 120 HMTVLDNTAFGMELA---GINAEERREKALDALRQVGLENYAH---SYPDE---LSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 242 PTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFNNVMLLADGRVAFTGSPQHALSFFAN-------HGYYC 314
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANdyvrtffRGVDI 270
|
250 260
....*....|....*....|....
gi 17647959 315 PEAYNPADF----LIGVLATDPGY 334
Cdd:PRK10070 271 SQVFSAKDIarrtPNGLIRKTPGF 294
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
98-274 |
3.61e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIGPFMHRIS-----GYVYQDDLFLGSLTVLEHLnF 171
Cdd:PRK09700 28 VYPGEIHALLGENGAGKSTLMKVLSgIHEPT----KGTITINNINYNKLDHKLAaqlgiGIIYQELSVIDELTVLENL-Y 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 MAHLrLDRRV------SKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTG 245
Cdd:PRK09700 103 IGRH-LTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVAN------LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180
....*....|....*....|....*....
gi 17647959 246 LDSYSAQQLVATLYELAQKGTTILCTIHQ 274
Cdd:PRK09700 176 LTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
98-247 |
4.01e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.24 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGR---RIGPFMHRISgYVYQDDLFLGSLTVLEHLNFma 173
Cdd:PRK11607 42 IYKGEIFALLGASGCGKSTLLRMLAgFEQPT----AGQIMLDGVdlsHVPPYQRPIN-MMFQSYALFPHMTVEQNIAF-- 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647959 174 HLRLDRrVSKEERRLIIKELLERTGLLSAAQTRigsgddKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:PRK11607 115 GLKQDK-LPKAEIASRVNEMLGLVHMQEFAKRK------PHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
97-264 |
4.03e-11 |
|
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: 65.86 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLAFRQPAgtvvQGDILINGRRIGPFMHR----------IsgyVYQDDLflGSL--- 163
Cdd:COG4172 308 TLRRGETLGLVGESGSGKSTLGLALLRLIPS----EGEIRFDGQDLDGLSRRalrplrrrmqV---VFQDPF--GSLspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 -----TVLEHLNFmahlrLDRRVSKEERRLIIKELLERTGLLSAAQTRigsgddkkvLSGGERKRLAFAVELLNNPVILF 238
Cdd:COG4172 379 mtvgqIIAEGLRV-----HGPGLSAAERRARVAEALEEVGLDPAARHRyp-----heFSGGQRQRIAIARALILEPKLLV 448
|
170 180
....*....|....*....|....*..
gi 17647959 239 CDEPTTGLDSySAQ-QLVATLYELAQK 264
Cdd:COG4172 449 LDEPTSALDV-SVQaQILDLLRDLQRE 474
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
91-305 |
4.28e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.34 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTL-AFRQP-AGTV------------------VQGDILINGRRIGPF----- 145
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnALLLPdTGTIewifkdeknkkktkekekVLEKLVIQKTRFKKIkkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 146 MHRISGYVYQ---DDLFlgSLTVLEHLNFMAhlrLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSGddkkvLSGGERK 222
Cdd:PRK13651 103 IRRRVGVVFQfaeYQLF--EQTIEKDIIFGP---VSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFE-----LSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 223 RLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQpssqlFDNF----NNVMLLADGRVAFTG 298
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD-----LDNVlewtKRTIFFKDGKIIKDG 247
|
....*..
gi 17647959 299 SPQHALS 305
Cdd:PRK13651 248 DTYDILS 254
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
88-304 |
5.96e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.47 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA--FRQPAGTVVQGDILINGRRIGPFMHRIsGYVYQ--DDLFLGSl 163
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTglLKPQSGEIKIDGITISKENLKEIRKKI-GIIFQnpDNQFIGA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLNFMAHlrlDRRVSKEERRLIIKELLERTGLLSAAQTrigsgdDKKVLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:PRK13632 100 TVEDDIAFGLE---NKKVPPKKMKDIIDDLAKKVGMEDYLDK------EPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGT-TILCTIHQPSSQLfdNFNNVMLLADGRVAFTGSPQHAL 304
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI--LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
98-309 |
6.73e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.28 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMstlafRQPAG--TVVQGDILINGRRIG--PFMHRISGYVYQDDLFLGSLTVLEHLNFMA 173
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLL-----RMIAGleDITSGDLFIGEKRMNdvPPAERGVGMVFQSYALYPHLSVAENMSFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 174 HL------RLDRRVSKEERRLIIKELLERTgllsaaqtrigsgddKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:PRK11000 101 KLagakkeEINQRVNQVAEVLQLAHLLDRK---------------PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 248 SYSAQQLVATLYELAQK-GTTILCTIHqpsSQLfdnfnNVMLLAD-------GRVAFTGSPQHALSFFAN 309
Cdd:PRK11000 166 AALRVQMRIEISRLHKRlGRTMIYVTH---DQV-----EAMTLADkivvldaGRVAQVGKPLELYHYPAN 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
91-305 |
8.46e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.08 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTL-AFRQPAgtvvQGDILINGRRIGPF-----MHRISGYVYQ--DDLFLGS 162
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLnGLLRPQ----KGKVLVSGIDTGDFsklqgIRKLVGIVFQnpETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 163 lTVLEHLNF-MAHLRLDrrvSKEERRLIIKELLErTGLlsaAQTRIGSgddKKVLSGGERKRLAFAVELLNNPVILFCDE 241
Cdd:PRK13644 94 -TVEEDLAFgPENLCLP---PIEIRKRVDRALAE-IGL---EKYRHRS---PKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647959 242 PTTGLDSYSAQQLVATLYELAQKGTTILCTIHqpSSQLFDNFNNVMLLADGRVAFTGSPQHALS 305
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
89-301 |
8.68e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.97 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 89 RIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILING-----RRIgpfMHRISGYVYQddlflgS 162
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAgLEKPT----EGQIFIDGedvthRSI---QQRDICMVFQ------S 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 163 LTVLEHL----NFMAHLRLdRRVSKEERRLIIKELLERTGLlsaaqtriGSGDDKKV--LSGGERKRLAFAVELLNNPVI 236
Cdd:PRK11432 87 YALFPHMslgeNVGYGLKM-LGVPKEERKQRVKEALELVDL--------AGFEDRYVdqISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 237 LFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSPQ 301
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHD-QSEAFAVSDTVIVMNKGKIMQIGSPQ 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
98-302 |
1.10e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.73 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTL--AFRQPAGTVVQGDILINGRRIGPFMHRIsGYVYQ--DDLFLGSlTVLEHLNFMA 173
Cdd:PRK13635 30 VYEGEWVAIVGHNGSGKSTLAKLLngLLLPEAGTITVGGMVLSEETVWDVRRQV-GMVFQnpDNQFVGA-TVQDDVAFGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 174 HlrlDRRVSKEERRLIIKELLERTGLLSAAQtrigsgDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQ 253
Cdd:PRK13635 108 E---NIGVPREEMVERVDQALRQVGMEDFLN------REPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17647959 254 LVATLYEL-AQKGTTILCTIHQPSSQLFDnfNNVMLLADGRVAFTGSPQH 302
Cdd:PRK13635 179 VLETVRQLkEQKGITVLSITHDLDEAAQA--DRVIVMNKGEILEEGTPEE 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
105-313 |
1.38e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 105 ALMGSSGSGKTTLMSTLAFRQPagtVVQGDILINGRRIGPFMHRI----SGYVYQDDLFLGSltvlehlNFMAHLRLDRR 180
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYP---LTEGEIRLDGRPLSSLSHSVlrqgVAMVQQDPVVLAD-------TFLANVTLGRD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 181 VSKEErrliIKELLERTGLLSAAQ-------TRIgsGDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQ 253
Cdd:PRK10790 441 ISEEQ----VWQALETVQLAELARslpdglyTPL--GEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 254 LVATLYELAQKgTTILCTIHQPSSQLfdNFNNVMLLADGRVAFTGSPQHALsffANHGYY 313
Cdd:PRK10790 515 IQQALAAVREH-TTLVVIAHRLSTIV--EADTILVLHRGQAVEQGTHQQLL---AAQGRY 568
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
91-273 |
1.42e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.31 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRI-GPFMHRIS--GYV--YQDDLFLGSLT 164
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTgFYKPTG----GTILLRGQHIeGLPGHQIArmGVVrtFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 165 VLEHLNFMAHLRLD-------------RRVSKE--ERRLiikELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVE 229
Cdd:PRK11300 97 VIENLLVAQHQQLKtglfsgllktpafRRAESEalDRAA---TWLERVGLLEHANRQAGN------LAYGQQRRLEIARC 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17647959 230 LLNNPVILFCDEPTTGL---DSYSAQQLVATLYElaQKGTTILCTIH 273
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLnpkETKELDELIAELRN--EHNVTVLLIEH 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
98-252 |
2.08e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.44 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAfR--QPAGtvvqGDILINGRRIgpfmHRISG-----------YVYQDDLflGSL- 163
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLLL-RleEPTS----GEILFDGQDI----TGLSGrelrplrrrmqMVFQDPY--ASLn 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 ---TVLEHLnfMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIgsgddKKVLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:COG4608 110 prmTVGDII--AEPLRIHGLASKAERRERVAELLELVGLRPEHADRY-----PHEFSGGQRQRIGIARALALNPKLIVCD 182
|
170
....*....|...
gi 17647959 241 EPTTGLD-SYSAQ 252
Cdd:COG4608 183 EPVSALDvSIQAQ 195
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
72-301 |
2.54e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 61.74 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 72 RDLCvYTNVGGsgqrmKRIINNSTGAIQPGTLMALMGSSGSGKTTLmstlaFRQPAG--TVVQGDILINGRRIGPF---- 145
Cdd:PRK13652 7 RDLC-YSYSGS-----KEALNNINFIAPRNSRIAVIGPNGAGKSTL-----FRHFNGilKPTSGSVLIRGEPITKEnire 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 146 MHRISGYVYQ---DDLFlgSLTVLEHLNF-MAHLRLD-----RRVSKEERRLIIKELLERTgllsaaqtrigsgddKKVL 216
Cdd:PRK13652 76 VRKFVGLVFQnpdDQIF--SPTVEQDIAFgPINLGLDeetvaHRVSSALHMLGLEELRDRV---------------PHHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 217 SGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQPS--SQLFDnfnNVMLLADGR 293
Cdd:PRK13652 139 SGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDlvPEMAD---YIYVMDKGR 215
|
....*...
gi 17647959 294 VAFTGSPQ 301
Cdd:PRK13652 216 IVAYGTVE 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
97-299 |
2.60e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.44 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLafrQPAGTVVQGDILINGRRIGPF----MHRISGYVYQDDLFLGSlTVLEHLnfm 172
Cdd:PRK13657 357 EAKPGQTVAIVGPTGAGKSTLINLL---QRVFDPQSGRILIDGTDIRTVtrasLRRNIAVVFQDAGLFNR-SIEDNI--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 173 ahlrldrRVSK-----EERRLIIK-----ELLERTglLSAAQTRIgsGDDKKVLSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:PRK13657 430 -------RVGRpdatdEEMRAAAEraqahDFIERK--PDGYDTVV--GERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 243 TTGLDSYSAQQLVATLYELAQKGTTI-----LCTIHqpssqlfdNFNNVMLLADGRVAFTGS 299
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMKGRTTFiiahrLSTVR--------NADRILVFDNGRVVESGS 552
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
98-301 |
3.01e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 61.68 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLafrQPAGTVVQGDILINGRRIGP----FMHRISGYVYQD-DLFLGSLTVLEHLNF- 171
Cdd:PRK13647 28 IPEGSKTALLGPNGAGKSTLLLHL---NGIYLPQRGRVKVMGREVNAenekWVRSKVGLVFQDpDDQVFSSTVWDDVAFg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 MAHLRLDRrvskeerrliiKELLERTGllsAAQTRIGSGD--DKKV--LSGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:PRK13647 105 PVNMGLDK-----------DEVERRVE---EALKAVRMWDfrDKPPyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 248 SYSAQQLVATLYELAQKGTTILCTIH------QPSSQlfdnfnnVMLLADGRVAFTGSPQ 301
Cdd:PRK13647 171 PRGQETLMEILDRLHNQGKTVIVATHdvdlaaEWADQ-------VIVLKEGRVLAEGDKS 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
91-313 |
3.02e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.11 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQpagtVVQGDILINGrrigpfmHRISGYVY---QDDLFLGSLTVl 166
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTrFYD----IDEGEILLDG-------HDLRDYTLaslRNQVALVSQNV- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 eHL------NFMAHLRLDRrVSKEErrlIIK--------ELLER--TGLlsaaQTRIGsgDDKKVLSGGERKRLAFAVEL 230
Cdd:PRK11176 427 -HLfndtiaNNIAYARTEQ-YSREQ---IEEaarmayamDFINKmdNGL----DTVIG--ENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 231 LNNPVILFCDEPTTGLDSYSAQQLVATLYELaQKGTTILCTIHQPSSqlFDNFNNVMLLADGRVAFTGSpqHAlSFFANH 310
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEKADEILVVEDGEIVERGT--HA-ELLAQN 569
|
...
gi 17647959 311 GYY 313
Cdd:PRK11176 570 GVY 572
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
100-274 |
3.50e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.80 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 100 PGTLMALMGSSGSGKTTLMSTLAFRQpagTVVQGDILINGRRIGpFMHRIS-----------GYVYQDDLFLGSLTVLEH 168
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLE---TPDSGQLNIAGHQFD-FSQKPSekairllrqkvGMVFQQYNLWPHLTVMEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 169 LnFMAHLRLdRRVSKEERRLIIKELLERTGLlsaaqtrigsgDDKK-----VLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:COG4161 103 L-IEAPCKV-LGLSKEQAREKAMKLLARLRL-----------TDKAdrfplHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190
....*....|....*....|....*....|.
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGTTILCTIHQ 274
Cdd:COG4161 170 AALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
100-273 |
3.84e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 100 PGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqGDILINGRRIGPF----MHRISGYVYQDDLFLGSLTVLEHL---NFM 172
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSE---GEILLDAQPLESWsskaFARKVAYLPQQLPAAEGMTVRELVaigRYP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 173 AHLRLDRRVSKEERRliIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQ 252
Cdd:PRK10575 113 WHGALGRFGAADREK--VEEAISLVGLKPLAHRLVDS------LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180
....*....|....*....|..
gi 17647959 253 QLVATLYELAQ-KGTTILCTIH 273
Cdd:PRK10575 185 DVLALVHRLSQeRGLTVIAVLH 206
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
105-298 |
4.15e-10 |
|
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: 60.24 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 105 ALMGSSGSGKTTLMSTLAFRQPAGTvvqGDILINGRRIGPFmhrisgyvyqdDL---FLGSLTVLEHLNFMAHLrldRRV 181
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLAGIYPPDS---GTVTVRGRVSSLL-----------GLgggFNPELTGRENIYLNGRL---LGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 182 SKEERRLIIKELLERTGLLSAAQTRIgsgddkKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYEL 261
Cdd:cd03220 115 SRKEIDEKIDEIIEFSELGDFIDLPV------KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 17647959 262 AQKGTTILCTIHQPSSqLFDNFNNVMLLADGRVAFTG 298
Cdd:cd03220 189 LKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
91-274 |
4.17e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.41 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQ----------PGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqGDILINGRRI----------GPFMHRIS 150
Cdd:PRK11124 8 INCFYGAHQalfditldcpQGETLVLLGPSGAGKSSLLRVLNLLEMPRS---GTLNIAGNHFdfsktpsdkaIRELRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 151 GYVYQDDLFLGSLTVLEHLnFMAHLRLdRRVSKEERRLIIKELLERTGLLSAAqtrigsgdDK--KVLSGGERKRLAFAV 228
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNL-IEAPCRV-LGLSKDQALARAEKLLERLRLKPYA--------DRfpLHLSGGQQQRVAIAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17647959 229 ELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQ 274
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
88-281 |
5.76e-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: 58.70 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqgdilinGRRIGPFMHRIsgyvyqddLFL------- 160
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGS---------GRIGMPEGEDL--------LFLpqrpylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 -GSLtvlehlnfmahlrldrrvskeeRRLIIKELlertgllsaaqtrigsgddKKVLSGGERKRLAFAVELLNNPVILFC 239
Cdd:cd03223 77 lGTL----------------------REQLIYPW-------------------DDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17647959 240 DEPTTGLDsysaQQLVATLYELAQK-GTTILCTIHQPS-SQLFD 281
Cdd:cd03223 116 DEATSALD----EESEDRLYQLLKElGITVISVGHRPSlWKFHD 155
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
98-299 |
7.55e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqGDILINGRRIGPF----MHRISGY-VYQDDLFLGSLTVLEHLNFm 172
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS---GTLEIGGNPCARLtpakAHQLGIYlVPQEPLLFPNLSVKENILF- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 173 ahlRLDRRVSKEERrliIKELLERTG----LLSAAQTrigsgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDS 248
Cdd:PRK15439 110 ---GLPKRQASMQK---MKQLLAALGcqldLDSSAGS----------LEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17647959 249 YSAQQLVATLYELAQKGTTILCTIHQPSS--QLFDnfnNVMLLADGRVAFTGS 299
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHKLPEirQLAD---RISVMRDGTIALSGK 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
91-301 |
8.92e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.15 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTT---LMstLAFRQPAgtvvQGDILINGRRIGPfmHRIS------GYVYQ--DDLF 159
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTiakLM--IGIEKVK----SGEIFYNNQAITD--DNFEklrkhiGIVFQnpDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 LGSLTV------LEhlNFMahlrldrrVSKEERRLIIKELLERTGLLSAAQtrigsgDDKKVLSGGERKRLAFAVELLNN 233
Cdd:PRK13648 97 VGSIVKydvafgLE--NHA--------VPYDEMHRRVSEALKQVDMLERAD------YEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 234 PVILFCDEPTTGLDSYSAQQLVATLYEL-AQKGTTILCTIHQPSSQLFDNFnnVMLLADGRVAFTGSPQ 301
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAMEADH--VIVMNKGTVYKEGTPT 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
97-301 |
9.27e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLAfrqPAGTVVQGDILING---------RRIGPfmhRISgYVYQDdlfLG-----S 162
Cdd:NF033858 23 DIPAGCMVGLIGPDGVGKSSLLSLIA---GARKIQQGRVEVLGgdmadarhrRAVCP---RIA-YMPQG---LGknlypT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 163 LTVLEHLNFMAHLR-LDRRvskeERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDE 241
Cdd:NF033858 93 LSVFENLDFFGRLFgQDAA----ERRRRIDELLRATGLAPFADRPAGK------LSGGMKQKLGLCCALIHDPDLLILDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 242 PTTGLDSYSAQQ-----------------LVATLY-ELAQKgttilctihqpssqlFDnfnnvMLLA--DGRVAFTGSPQ 301
Cdd:NF033858 163 PTTGVDPLSRRQfwelidriraerpgmsvLVATAYmEEAER---------------FD-----WLVAmdAGRVLATGTPA 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
97-269 |
1.04e-09 |
|
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: 58.21 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIgpfmhriSGYVYQDDLFLGsltvlehlnfMAHL 175
Cdd:cd03215 22 EVRAGEIVGIAGLVGNGQTELAEALFgLRPPAS----GEITLDGKPV-------TRRSPRDAIRAG----------IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 176 RLDRRvskeerrliikelleRTGL---LSAAQ-TRIGSgddkkVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSA 251
Cdd:cd03215 81 PEDRK---------------REGLvldLSVAEnIALSS-----LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170
....*....|....*...
gi 17647959 252 QQLVATLYELAQKGTTIL 269
Cdd:cd03215 141 AEIYRLIRELADAGKAVL 158
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
90-312 |
1.16e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfRQPAGTVVQGDILINGRRI---GPFMHRISGyvyqddLFLGSLTVL 166
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA-GHPAYKILEGDILFKGESIldlEPEERAHLG------IFLAFQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 E--HLNFMAHLRL---DRRVSKEERRL-------IIKELLERTGLLSAAQTR-IGSGddkkvLSGGERKR---LAFAvel 230
Cdd:CHL00131 95 EipGVSNADFLRLaynSKRKFQGLPELdplefleIINEKLKLVGMDPSFLSRnVNEG-----FSGGEKKRneiLQMA--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 231 LNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPssQLFD----NFNNVMllADGRVAFTGSPQHALSf 306
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ--RLLDyikpDYVHVM--QNGKIIKTGDAELAKE- 241
|
....*.
gi 17647959 307 FANHGY 312
Cdd:CHL00131 242 LEKKGY 247
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
88-305 |
1.17e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.84 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTL-AFRQPAgtvvQGDILINGRRIGP--------FMHRISGYVYQ--- 155
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFnALLKPS----SGTITIAGYHITPetgnknlkKLRKKVSLVFQfpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 156 DDLFlgSLTVLEHLNFMAhlrLDRRVSKEERRLIIKELLERTGLLSAAQTRigSGDDkkvLSGGERKRLAFAVELLNNPV 235
Cdd:PRK13641 96 AQLF--ENTVLKDVEFGP---KNFGFSEDEAKEKALKWLKKVGLSEDLISK--SPFE---LSGGQMRRVAIAGVMAYEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 236 ILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSPQHALS 305
Cdd:PRK13641 166 ILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
97-269 |
1.36e-09 |
|
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: 57.44 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLAfrqpaGTVV--QGDILINGRRI---GPFM---HRIsGYVYQddlflgsltvleh 168
Cdd:cd03216 22 SVRRGEVHALLGENGAGKSTLMKILS-----GLYKpdSGEILVDGKEVsfaSPRDarrAGI-AMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 169 lnfmahlrldrrvskeerrliikellertgllsaaqtrigsgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDS 248
Cdd:cd03216 83 -----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180
....*....|....*....|.
gi 17647959 249 YSAQQLVATLYELAQKGTTIL 269
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVI 136
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
181-294 |
2.17e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 181 VSKEERRLIIKELLERTGLLSAAqtrigsGDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYE 260
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAA------GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRS 189
|
90 100 110
....*....|....*....|....*....|....*....
gi 17647959 261 LAQKGTTILCTIH--QPSSQLFDNFNNV---MLLADGRV 294
Cdd:NF000106 190 MVRDGATVLLTTQymEEAEQLAHELTVIdrgRVIADGKV 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
88-300 |
3.79e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.27 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTT----LMSTLAFRQPAGTVVQGD-ILINGRRIGPFMHRIsGYVYQ--DDLFL 160
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTisklINGLLLPDDNPNSKITVDgITLTAKTVWDIREKV-GIVFQnpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSlTVLEHLNFMAHlrlDRRVSKEERRLIIKELLERTGLLSAAQTrigsgdDKKVLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:PRK13640 99 GA-TVGDDVAFGLE---NRAVPRPEMIKIVRDVLADVGMLDYIDS------EPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 241 EPTTGLDSYSAQQLVATLYELA-QKGTTILCTIHQ-PSSQLFDnfnNVMLLADGRVAFTGSP 300
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDiDEANMAD---QVLVLDDGKLLAQGSP 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
97-269 |
4.24e-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: 57.44 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTL-----------AFRQPAGTVvqgDI-------LINGRRigpfmHRIsGYVYQddl 158
Cdd:COG4778 33 SVAAGECVALTGPSGAGKSTLLKCIygnylpdsgsiLVRHDGGWV---DLaqaspreILALRR-----RTI-GYVSQ--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 159 FLGSLTVLEHLNFMAHLRLDRRVSKEERRLIIKELLERTGL------LSAAqTrigsgddkkvLSGGERKRLAFAVELLN 232
Cdd:COG4778 101 FLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLperlwdLPPA-T----------FSGGEQQRVNIARGFIA 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 17647959 233 NPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTIL 269
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
108-247 |
6.94e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 108 GSSGSGKTTLMSTLAFRQPA--GT-------VVQGDILINgRRIGpFMHR-ISGYvyqddlflGSLTVLEhlNFMAHLRL 177
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPAseGEawlfgqpVDAGDIATR-RRVG-YMSQaFSLY--------GELTVRQ--NLELHARL 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 178 dRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:NF033858 367 -FHLPAAEIAARVAEMLERFDLADVADALPDS------LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
88-269 |
9.70e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 54.38 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA--FRQPAGTVVQGDILingrrigpfmhRIsGYVYQddlflgsltv 165
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgeLEPDEGIVTWGSTV-----------KI-GYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 166 lehlnfmahlrldrrvskeerrliikellertgllsaaqtrigsgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTG 245
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180
....*....|....*....|....
gi 17647959 246 LDSYSAQQLVATLYELaqKGTTIL 269
Cdd:cd03221 101 LDLESIEALEEALKEY--PGTVIL 122
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
105-299 |
1.06e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.58 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 105 ALMGSSGSGKTTLMSTLAfrqpaGTVV--QGDILINGR---------RIGPFMHRIsGYVYQDD-LFlgsltvlEHLNFM 172
Cdd:PRK11144 28 AIFGRSGAGKTSLINAIS-----GLTRpqKGRIVLNGRvlfdaekgiCLPPEKRRI-GYVFQDArLF-------PHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 173 AHLRLD-RRVSKEE-----RRLIIKELLERTGLlsaaqtrigsgddkkVLSGGERKRLAFAVELLNNPVILFCDEPTTGL 246
Cdd:PRK11144 95 GNLRYGmAKSMVAQfdkivALLGIEPLLDRYPG---------------SLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 247 DSYSAQQLVATLYELAQK-GTTILCTIH--QPSSQLFDnfnNVMLLADGRVAFTGS 299
Cdd:PRK11144 160 DLPRKRELLPYLERLAREiNIPILYVSHslDEILRLAD---RVVVLEQGKVKAFGP 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
95-305 |
1.49e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 95 TGAIQPGTLMALMGSSGSGKTTLMSTLAfrqpaGTVV-QGDILINGRRIGPFMH----RISGYVYQDDLFLGSLTVLEHL 169
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMA-----GLLPgSGSIQFAGQPLEAWSAaelaRHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 NfmahLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGE--RKRLAfAVEL----LNNPV--ILFCDE 241
Cdd:PRK03695 91 T----LHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQ------LSGGEwqRVRLA-AVVLqvwpDINPAgqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 242 PTTGLDsySAQQ--LVATLYELAQKGTTILCTIHQPSSQLfDNFNNVMLLADGRVAFTGSPQHALS 305
Cdd:PRK03695 160 PMNSLD--VAQQaaLDRLLSELCQQGIAVVMSSHDLNHTL-RHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
97-305 |
1.59e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLAfrqpagtvvQGDILINGRRIGPFmHRISgyvyqddlflgsltvleHLNFMahlR 176
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALA---------GELPLLSGERQSQF-SHIT-----------------RLSFE---Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 177 LDRRVSKEERRL---IIKELLERTGLLS-----------------AAQTRIGSGDDK--KVLSGGERKRLAFAVELLNNP 234
Cdd:PRK10938 75 LQKLVSDEWQRNntdMLSPGEDDTGRTTaeiiqdevkdparceqlAQQFGITALLDRrfKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647959 235 VILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQpssqlFDNF----NNVMLLADGRVAFTGSPQHALS 305
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNR-----FDEIpdfvQFAGVLADCTLAETGEREEILQ 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
84-247 |
1.79e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 84 GQRmkRIINNSTGAIQPGTLMALMGSSGSGKTTLMS-TLAFRQP-AGTVVQGDILingrrigpfmhRIsGYVYQDdLFLG 161
Cdd:PRK09544 15 GQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAPdEGVIKRNGKL-----------RI-GYVPQK-LYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 162 SLTVLEHLNFMahlRLDRRVSKEErrliIKELLERTG---LLSAAQTRigsgddkkvLSGGERKRLAFAVELLNNPVILF 238
Cdd:PRK09544 80 TTLPLTVNRFL---RLRPGTKKED----ILPALKRVQaghLIDAPMQK---------LSGGETQRVLLARALLNRPQLLV 143
|
....*....
gi 17647959 239 CDEPTTGLD 247
Cdd:PRK09544 144 LDEPTQGVD 152
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
88-300 |
2.14e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.21 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTL-AFRQPAgtvvQGDILINGRRIG------PFMHRISGYVYQ---DD 157
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLnGLLKPT----SGKIIIDGVDITdkkvklSDIRKKVGLVFQypeYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 158 LFlgSLTVLEHLNF-MAHLRLdrrvSKEERRLIIKELLERTGLlsaaqtrigSGDDKK-----VLSGGERKRLAFAVELL 231
Cdd:PRK13637 96 LF--EETIEKDIAFgPINLGL----SEEEIENRVKRAMNIVGL---------DYEDYKdkspfELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 232 NNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIH--QPSSQLFDnfnNVMLLADGRVAFTGSP 300
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHsmEDVAKLAD---RIIVMNKGKCELQGTP 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
100-247 |
2.19e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.70 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 100 PGTLMALMGSSGSGKTTLMSTLAFRQP--AGTV-------VQGDILINGRRIGPFMHRIS-GYVYQddlflgsltvlehl 169
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLApdAGEVhyrmrdgQLRDLYALSEAERRRLLRTEwGFVHQ-------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 NFMAHLRLdrRVSK----EER------------RLIIKELLERTGLlsaAQTRIgsGDDKKVLSGGERKRLAFAVELLNN 233
Cdd:PRK11701 97 HPRDGLRM--QVSAggniGERlmavgarhygdiRATAGDWLERVEI---DAARI--DDLPTTFSGGMQQRLQIARNLVTH 169
|
170
....*....|....
gi 17647959 234 PVILFCDEPTTGLD 247
Cdd:PRK11701 170 PRLVFMDEPTGGLD 183
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
84-294 |
3.46e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.07 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 84 GQRmkRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQP-AGTVVQGDI-LINGRRIGPFMhrisgyvYQDDLFL 160
Cdd:PRK11247 23 GER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAgLETPsAGELLAGTApLAEAREDTRLM-------FQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSLTVLEhlNFMAHLRLDRRVSKEErrliikeLLERTGLLSAAqtrigsGDDKKVLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:PRK11247 94 PWKKVID--NVGLGLKGQWRDAALQ-------ALAAVGLADRA------NEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 241 EPTTGLDSYS---AQQLVATLYElaQKGTTILCTIHQPSSQ--LFDnfnNVMLLADGRV 294
Cdd:PRK11247 159 EPLGALDALTrieMQDLIESLWQ--QHGFTVLLVTHDVSEAvaMAD---RVLLIEEGKI 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
97-305 |
3.90e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.71 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKT-TLMSTLAFRQPAGTVVQGDILINGRRIGPFMHRisgyvyqddlflGSL--TVLEH----- 168
Cdd:PRK10418 25 TLQRGRVLALVGGSGSGKSlTCAAALGILPAGVRQTAGRVLLDGKPVAPCALR------------GRKiaTIMQNprsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 169 --LNFMAHLRLD--RRVSKEERRLIIKELLERTGLlsaaqtrigsGDDKKVL-------SGGERKRLAFAVELLNNPVIL 237
Cdd:PRK10418 93 npLHTMHTHAREtcLALGKPADDATLTAALEAVGL----------ENAARVLklypfemSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 238 FCDEPTTGLDSYSAQQLVATLYEL-AQKGTTILCTIHQPS--SQLFDnfnNVMLLADGRVAFTGS-------PQHALS 305
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGvvARLAD---DVAVMSHGRIVEQGDvetlfnaPKHAVT 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
98-293 |
4.73e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGR--RIGPFMHRISGYV---YQDDLFLGSLTVLEHLnF 171
Cdd:PRK11288 27 CRAGQVHALMGENGAGKSTLLKILSgNYQPD----AGSILIDGQemRFASTTAALAAGVaiiYQELHLVPEMTVAENL-Y 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 MAHLR-----LDRRVSKEERRliikELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNP-VILFcDEPTTG 245
Cdd:PRK11288 102 LGQLPhkggiVNRRLLNYEAR----EQLEHLGVDIDPDTPLKY------LSIGQRQMVEIAKALARNArVIAF-DEPTSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17647959 246 LDSYSAQQLVATLYELAQKGTTILCTIHQpSSQLFDNFNNVMLLADGR 293
Cdd:PRK11288 171 LSAREIEQLFRVIRELRAEGRVILYVSHR-MEEIFALCDAITVFKDGR 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
98-293 |
6.61e-08 |
|
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: 53.24 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAfrqpaG--TVVQGDILINGRRigpfmhrisGYVYQDDlFLGSLTVLEhlNFMAHL 175
Cdd:cd03250 28 VPKGELVAIVGPVGSGKSSLLSALL-----GelEKLSGSVSVPGSI---------AYVSQEP-WIQNGTIRE--NILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 176 RLDrrvskEER-RLIIK--ELLERTGLLSAA-QTRIGsgdDKKV-LSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYS 250
Cdd:cd03250 91 PFD-----EERyEKVIKacALEPDLEILPDGdLTEIG---EKGInLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17647959 251 AQQLV--ATLYELAQKGTTILCTiHQPssQLFDNFNNVMLLADGR 293
Cdd:cd03250 163 GRHIFenCILGLLLNNKTRILVT-HQL--QLLPHADQIVVLDNGR 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
98-307 |
6.85e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.93 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLafrqpAGTV--VQGDILINGrRIGPFMhrisgyvyqdDL---FLGSLTVLE--HLN 170
Cdd:COG1134 49 VERGESVGIIGRNGAGKSTLLKLI-----AGILepTSGRVEVNG-RVSALL----------ELgagFHPELTGREniYLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 171 FMAHlrldrRVSKEERRLIIKELLERTGLlsaaqtrigsGD--DKKV--LSGGERKRLAFAVELLNNPVILFCDEPT-TG 245
Cdd:COG1134 113 GRLL-----GLSRKEIDEKFDEIVEFAEL----------GDfiDQPVktYSSGMRARLAFAVATAVDPDILLVDEVLaVG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 246 lDSYSAQQLVATLYELAQKGTTILCTIHQPsSQLFDNFNNVMLLADGRVAFTGSPQHALSFF 307
Cdd:COG1134 178 -DAAFQKKCLARIRELRESGRTVIFVSHSM-GAVRRLCDRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-261 |
7.66e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 36 LDSTPKLSKRNSSE--RSLPLRSY---SKWSPTEQGATLV-------WRDLCVYTNV-GGSGQRMKR---IINNSTGAIQ 99
Cdd:PRK10261 269 LAAVPQLGAMKGLDypRRFPLISLehpAKQEPPIEQDTVVdgepilqVRNLVTRFPLrSGLLNRVTRevhAVEKVSFDLW 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 100 PGTLMALMGSSGSGK-TTLMSTLAFRQPAGtvvqGDILINGRRIGPF-------MHRISGYVYQDDLflGSLTVLEHLNF 171
Cdd:PRK10261 349 PGETLSLVGESGSGKsTTGRALLRLVESQG----GEIIFNGQRIDTLspgklqaLRRDIQFIFQDPY--ASLDPRQTVGD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 172 --MAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIgsgddKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSY 249
Cdd:PRK10261 423 siMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRY-----PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
250
....*....|..
gi 17647959 250 SAQQLVATLYEL 261
Cdd:PRK10261 498 IRGQIINLLLDL 509
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
83-254 |
8.33e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.59 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 83 SGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTL--MSTLAFRQPAGT-VVQG-DILINGRRIGPFMHRISGYVYQDDL 158
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLarLLTMIETPTGGElYYQGqDLLKADPEAQKLLRQKIQIVFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 159 flGSL-------TVLEhlnfmAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIgsgddKKVLSGGERKRLAFAVELL 231
Cdd:PRK11308 103 --GSLnprkkvgQILE-----EPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY-----PHMFSGGQRQRIAIARALM 170
|
170 180
....*....|....*....|....
gi 17647959 232 NNPVILFCDEPTTGLD-SYSAQQL 254
Cdd:PRK11308 171 LDPDVVVADEPVSALDvSVQAQVL 194
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
84-301 |
9.66e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.00 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 84 GQRMkrIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvvqGDILINGRRIgPFMHRISGY--------VYQ 155
Cdd:PRK11831 18 GNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH---GEILFDGENI-PAMSRSRLYtvrkrmsmLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 156 DDLFLGSLTVLEHLNFmaHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPV 235
Cdd:PRK11831 92 SGALFTDMNVFDNVAY--PLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSE------LSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 236 ILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSPQ 301
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHD-VPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
91-276 |
1.01e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.33 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTlafrqpaGTVVQGDILINGRRigpfmhriSGYVYQDDLFLGSLTVLEHLN 170
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-------GLYASGKARLISFL--------PKFSRNKLIFIDQLQFLIDVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 171 fMAHLRLDRrvskeerrliikellertgllsAAQTrigsgddkkvLSGGERKRLAFAVELLNNP---VILFcDEPTTGLD 247
Cdd:cd03238 76 -LGYLTLGQ----------------------KLST----------LSGGELQRVKLASELFSEPpgtLFIL-DEPSTGLH 121
|
170 180
....*....|....*....|....*....
gi 17647959 248 SYSAQQLVATLYELAQKGTTILCTIHQPS 276
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
91-302 |
1.72e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKT-TLMSTLAFRQPAGTVVQGDILINGRR------IGPF----MHRISG----YVYQ 155
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLVQCDKMLLRRRsrqvieLSEQsaaqMRHVRGadmaMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 156 DDLflGSL----TVLEHLnfMAHLRLDRRVSKEERRLIIKELLERTgLLSAAQTRIGSGDDKkvLSGGERKRLAFAVELL 231
Cdd:PRK10261 112 EPM--TSLnpvfTVGEQI--AESIRLHQGASREEAMVEAKRMLDQV-RIPEAQTILSRYPHQ--LSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 232 NNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFNNVMLLADGRVAFTGS-------PQH 302
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSveqifhaPQH 262
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
98-264 |
1.82e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.87 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRI--GPFMHRISG--YVYQDDlfLGSLT----VLEH 168
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAgMIEPTS----GELLIDDHPLhfGDYSYRSQRirMIFQDP--STSLNprqrISQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 169 LNFmaHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIgsgddKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDS 248
Cdd:PRK15112 110 LDF--PLRLNTDLEPEQREKQIIETLRQVGLLPDHASYY-----PHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170
....*....|....*.
gi 17647959 249 YSAQQLVATLYELAQK 264
Cdd:PRK15112 183 SMRSQLINLMLELQEK 198
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
216-307 |
2.37e-07 |
|
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: 53.65 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 216 LSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQ-KGTTILCTIHQPSSqLFDNFNNVMLLADGRV 294
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEV-IEDLSDKAIWLENGEI 247
|
90
....*....|...
gi 17647959 295 AFTGSPQHALSFF 307
Cdd:TIGR03269 248 KEEGTPDEVVAVF 260
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
100-300 |
2.91e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 100 PGTLMALMGSSGSGKTTLMSTLA--FRQPAGTVV-QGDILINGRRIGPFMHRISGYVYQD-DLFLGSLTVLEHLNFmaHL 175
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLSglLRPQKGAVLwQGKPLDYSKRGLLALRQQVATVFQDpEQQIFYTDIDSDIAF--SL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 176 RlDRRVSKEErrlIIKELLERTGLLSAAQTRigsGDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLV 255
Cdd:PRK13638 104 R-NLGVPEAE---ITRRVDEALTLVDAQHFR---HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17647959 256 ATLYELAQKGTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSP 300
Cdd:PRK13638 177 AIIRRIVAQGNHVIISSHD-IDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
91-273 |
3.29e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.80 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKT----TLMSTLAfrqpAGTVVQGDILINGRRIGPF----MHRISG----YVYQDDL 158
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA----ANGRIGGSATFNGREILNLpekeLNKLRAeqisMIFQDPM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 159 flGSLT----VLEHLnfMAHLRLDRRVSKEErrliikELLERTGLLSA-----AQTRIGSGDDKkvLSGGERKRLAFAVE 229
Cdd:PRK09473 108 --TSLNpymrVGEQL--MEVLMLHKGMSKAE------AFEESVRMLDAvkmpeARKRMKMYPHE--FSGGMRQRVMIAMA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17647959 230 LLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIH 273
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITH 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
97-301 |
4.35e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.09 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTL-AFRQPA-GTVVQGDILINGR----RIGPFMHRIsGYVYQ---DDLFLGSL---T 164
Cdd:PRK13646 29 EFEQGKYYAIVGQTGSGKSTLIQNInALLKPTtGTVTVDDITITHKtkdkYIRPVRKRI-GMVFQfpeSQLFEDTVereI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 165 VLEHLNFMAHLRldrRVSKEERRLIIKELLERTGL-LSAAQtrigsgddkkvLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:PRK13646 108 IFGPKNFKMNLD---EVKNYAHRLLMDLGFSRDVMsQSPFQ-----------MSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 244 TGLDSYSAQQLVATLYELA-QKGTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSPQ 301
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtDENKTIILVSHD-MNEVARYADEVIVMKEGSIVSQTSPK 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
88-301 |
4.82e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMstlafRQPAGTVV--QGDILINGRRIGP-----FMHRIsGYVYQ--DDL 158
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTV-----RLIDGLLEaeSGQIIIDGDLLTEenvwdIRHKI-GMVFQnpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 159 FLGSlTVLEHLNFMAHlrlDRRVSKEERRLIIKELLERTGlLSAAQTRigsgdDKKVLSGGERKRLAFAVELLNNPVILF 238
Cdd:PRK13650 94 FVGA-TVEDDVAFGLE---NKGIPHEEMKERVNEALELVG-MQDFKER-----EPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 239 CDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQpssqlFDNF---NNVMLLADGRVAFTGSPQ 301
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHD-----LDEValsDRVLVMKNGQVESTSTPR 225
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
216-273 |
5.08e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 5.08e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 216 LSGGERKRLAFAVELLN---NPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIH 273
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
216-275 |
8.27e-07 |
|
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: 49.28 E-value: 8.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647959 216 LSGGERKRLAFAVEL---LNNPVILFC-DEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQP 275
Cdd:cd03227 78 LSGGEKELSALALILalaSLKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
89-267 |
1.01e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 89 RIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvVQGDILINGRRIGPFMHRIS---GYV--YQDDLFLGSL 163
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGT-YEGEIIFEGEELQASNIRDTeraGIAiiHQELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEHLnFMAH-LRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEP 242
Cdd:PRK13549 98 SVLENI-FLGNeITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGN------LGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180
....*....|....*....|....*
gi 17647959 243 TTGLDSYSAQQLVATLYELAQKGTT 267
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAHGIA 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
88-268 |
1.17e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA--FRQPAGTVVQGDiliNGRrigpfmhriSGYVYQD--DLFLGSL 163
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVgeLEPDSGTVKWSE---NAN---------IGYYAQDhaYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 164 TVLEhlnFMAHLRldrrvSKEERRLIIKELLERtgLLSaaqtrigSGDD--K--KVLSGGERKRLAFAVELLNNPVILFC 239
Cdd:PRK15064 400 TLFD---WMSQWR-----QEGDDEQAVRGTLGR--LLF-------SQDDikKsvKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180
....*....|....*....|....*....
gi 17647959 240 DEPTTGLDSYSAQQLVATLYELaqKGTTI 268
Cdd:PRK15064 463 DEPTNHMDMESIESLNMALEKY--EGTLI 489
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
89-309 |
1.20e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 89 RIINNSTGAIQPGTLMALMGSSGSGKTT---LMSTLAFRQPAGTVVqGDILI--NGRRIGPF--MHRISGYVYQ-DDLFL 160
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTmiqLTNGLIISETGQTIV-GDYAIpaNLKKIKEVkrLRKEIGLVFQfPEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSLTVLEHLNF-MAHLRLDrrvsKEERRLIIKELLERTGLLSAAQTRigsgdDKKVLSGGERKRLAFAVELLNNPVILFC 239
Cdd:PRK13645 104 FQETIEKDIAFgPVNLGEN----KQEAYKKVPELLKLVQLPEDYVKR-----SPFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 240 DEPTTGLDSYSAQQLVATLYEL-AQKGTTILCTIHQpSSQLFDNFNNVMLLADGRVAFTGSPqhaLSFFAN 309
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHN-MDQVLRIADEVIVMHEGKVISIGSP---FEIFSN 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
98-269 |
1.54e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTL-AFRQP-AGTVVQGDILINGRRIGPFMHRisGYVY------QDDLFLG-------- 161
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLyGLRPArGGRIMLNGKEINALSTAQRLAR--GLVYlpedrqSSGLYLDaplawnvc 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 162 SLTVLEhLNFMAHLRLDRRVSKEERRLI-IKellertglLSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:PRK15439 364 ALTHNR-RGFWIKPARENAVLERYRRALnIK--------FNHAEQAART------LSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190
....*....|....*....|....*....|...
gi 17647959 241 EPTTGLDsYSAQqlvATLYEL----AQKGTTIL 269
Cdd:PRK15439 429 EPTRGVD-VSAR---NDIYQLirsiAAQNVAVL 457
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
111-269 |
1.70e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 111 GSGKTTLMSTLAFRQPAgtvVQGDILINGRRIGP------FMHRIsGYVYQDD----LFLG-------SLTVLEHlnFMA 173
Cdd:COG1129 288 GAGRTELARALFGADPA---DSGEIRLDGKPVRIrsprdaIRAGI-AYVPEDRkgegLVLDlsireniTLASLDR--LSR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 174 HLRLDRRvskEERRLI---IKELLERTgllSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYS 250
Cdd:COG1129 362 GGLLDRR---RERALAeeyIKRLRIKT---PSPEQPVGN------LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGA 429
|
170
....*....|....*....
gi 17647959 251 AQQLVATLYELAQKGTTIL 269
Cdd:COG1129 430 KAEIYRLIRELAAEGKAVI 448
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
88-273 |
1.84e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 49.33 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIG---PFMHR--ISgYVYQDDLFLG 161
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVAsLISPT----SGTLLFEGEDIStlkPEIYRqqVS-YCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 162 SlTVLEHLNFMAHLRLDRrvsKEERRLIikELLERTGL-LSAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:PRK10247 95 D-TVYDNLIFPWQIRNQQ---PDPAIFL--DDLERFALpDTILTKNIAE------LSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....
gi 17647959 241 EPTTGLDSYSAQQLVATLYELA-QKGTTILCTIH 273
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVrEQNIAVLWVTH 196
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
273-388 |
1.99e-06 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 50.67 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 273 HQPSSQLFDNFNNVMLLAD-GRVAFTGSPQHALSFFANHGYYCPEAYNPADFLIGVLA------TDPG--YEQASQRSAQ 343
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEgivkpsTSSGvdYKQLPVRWML 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17647959 344 HlcDQFAVSSaakqrDMLVNLEIHMAQSG-------NFPFDTEVESFRGVAW 388
Cdd:pfam19055 81 H--NGYPVPP-----DMLQNADGIAASSGenssngtNPGVGSEEQSFAGELW 125
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
86-294 |
2.27e-06 |
|
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: 50.59 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 86 RMKRIiNNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGtvVQGDILINGRRIG------PFMHRISgYVYQD--- 156
Cdd:TIGR02633 272 HRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGK--FEGNVFINGKPVDirnpaqAIRAGIA-MVPEDrkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 157 -----DLFLGSLTVLEHLN-FMAHLRLDRRVSKEERRLIIKELLERTgllSAAQTRIGSgddkkvLSGGERKRLAFAVEL 230
Cdd:TIGR02633 348 hgivpILGVGKNITLSVLKsFCFKMRIDAAAELQIIGSAIQRLKVKT---ASPFLPIGR------LSGGNQQKAVLAKML 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647959 231 LNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTihqpSSQLFDNF---NNVMLLADGRV 294
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVV----SSELAEVLglsDRVLVIGEGKL 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
97-247 |
3.76e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 97 AIQPGTLMALMGSSGSGKTTLMSTLAFRQP-------------------------AGTVV---------QGDILINgrri 142
Cdd:PRK11147 25 HIEDNERVCLVGRNGAGKSTLMKILNGEVLlddgriiyeqdlivarlqqdpprnvEGTVYdfvaegieeQAEYLKR---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 143 gpfMHRISGYVYQD--DLFLGSLT----VLEHLNFMahlRLDRRvskeerrliIKELLERTGLlsAAQTRIGSgddkkvL 216
Cdd:PRK11147 101 ---YHDISHLVETDpsEKNLNELAklqeQLDHHNLW---QLENR---------INEVLAQLGL--DPDAALSS------L 157
|
170 180 190
....*....|....*....|....*....|.
gi 17647959 217 SGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
133-311 |
4.07e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 133 GDILINGRRIGPF----MHRISGYVYQDDLfLGSLTVLEHLNFMAHLRLDRRVSKEERRLIIKELLErtGLLSAAQTRIG 208
Cdd:PTZ00265 1277 GKILLDGVDICDYnlkdLRNLFSIVSQEPM-LFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIE--SLPNKYDTNVG 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 209 SGDdkKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKG-TTILCTIHQPSSqlfdnfnnvM 287
Cdd:PTZ00265 1354 PYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIAS---------I 1422
|
170 180
....*....|....*....|....
gi 17647959 288 LLADGRVAFTgSPQHALSFFANHG 311
Cdd:PTZ00265 1423 KRSDKIVVFN-NPDRTGSFVQAHG 1445
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
85-269 |
5.09e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 85 QRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLaFRQPAGtVVQGDILINGRRIgpfmhRISG----------YVY 154
Cdd:PRK13549 272 NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCL-FGAYPG-RWEGEIFIDGKPV-----KIRNpqqaiaqgiaMVP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 155 QD--------DLFLG---SLTVLEhlNFMAHLRLDRrvSKEER--RLIIKELLERTgllSAAQTRIGSgddkkvLSGGER 221
Cdd:PRK13549 345 EDrkrdgivpVMGVGkniTLAALD--RFTGGSRIDD--AAELKtiLESIQRLKVKT---ASPELAIAR------LSGGNQ 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17647959 222 KRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTIL 269
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAII 459
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
100-276 |
6.50e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 100 PGTLMALMGSSGSGKTTLMSTLA-FRQPAGTVVqgdILINGRRIgpfmhrisgyvyqddlflgsltvlehlnfmahlrld 178
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALArELGPPGGGV---IYIDGEDI------------------------------------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 179 RRVSKEERRLIIkellertgllsaaqtrigSGDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATL 258
Cdd:smart00382 42 LEEVLDQLLLII------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
170 180
....*....|....*....|....
gi 17647959 259 Y------ELAQKGTTILCTIHQPS 276
Cdd:smart00382 104 ElrllllLKSEKNLTVILTTNDEK 127
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
88-271 |
1.03e-05 |
|
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: 48.78 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMstlafRQPAGTvvqgDILINGR-RIGPFMHRisGYVYQDDLFLGSLTVL 166
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGV----DKDFNGEaRPQPGIKV--GYLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 EhlNFMAHLRLDRRVSKEERRLIIK---------ELLERTGLLsaaQTRIGSGD--------------------DKKV-- 215
Cdd:TIGR03719 87 E--NVEEGVAEIKDALDRFNEISAKyaepdadfdKLAAEQAEL---QEIIDAADawdldsqleiamdalrcppwDADVtk 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17647959 216 LSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELaqKGTTILCT 271
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVT 215
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
216-274 |
1.19e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.22 E-value: 1.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647959 216 LSGGERKRLAFAVELLN---NPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQ 274
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
100-292 |
1.54e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 100 PGTLMALMGSSGSGKTTLMSTLA--FRQPAGTvvqgdILINGRRI---GPfmhRIS-----GYVYQDDLFLGSLTVLEHL 169
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTgiYTRDAGS-----ILYLGKEVtfnGP---KSSqeagiGIIHQELNLIPQLTIAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 ----NFMAHL-RLDRRVSKEErrliIKELLERTGLLSAAQTRIGSgddkkvLSGGERKRLAFAVEL-LNNPVILFcDEPT 243
Cdd:PRK10762 101 flgrEFVNRFgRIDWKKMYAE----ADKLLARLNLRFSSDKLVGE------LSIGEQQMVEIAKVLsFESKVIIM-DEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17647959 244 TGLDSYSAQQLVATLYELAQKGTTILCTIHQpSSQLFDNFNNVMLLADG 292
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIVYISHR-LKEIFEICDDVTVFRDG 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
88-299 |
1.69e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTL--AFRQPAGTVvqgdilingrrigpFMHRISGYVYQDDLFLGSlTV 165
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlsQFEISEGRV--------------WAERSIAYVPQQAWIMNA-TV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 166 LEHLNFMAHLRLDR-----RVSKEERRLiikellertGLLSAA-QTRIGsgdDKKV-LSGGERKRLAFAVELLNNPVILF 238
Cdd:PTZ00243 738 RGNILFFDEEDAARladavRVSQLEADL---------AQLGGGlETEIG---EKGVnLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 239 CDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQpsSQLFDNFNNVMLLADGRVAFTGS 299
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDGRVEFSGS 864
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
82-260 |
1.98e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 82 GSGQRMkrIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAfrqpaGTV--VQGDI-LINGRRIGPFMHRISGYVYQDDl 158
Cdd:PRK10636 321 GYGDRI--ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA-----GELapVSGEIgLAKGIKLGYFAQHQLEFLRADE- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 159 flgslTVLEHLnfmahLRLDRRVSKEERRliikELLERTGLLSAAQTrigsgDDKKVLSGGERKRLAFAVELLNNPVILF 238
Cdd:PRK10636 393 -----SPLQHL-----ARLAPQELEQKLR----DYLGGFGFQGDKVT-----EETRRFSGGEKARLVLALIVWQRPNLLL 453
|
170 180
....*....|....*....|..
gi 17647959 239 CDEPTTGLDSYSAQQLVATLYE 260
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALID 475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-305 |
2.15e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 16 RVEQHELQVMPVGSTIEVPSldSTPKLSKRNSSERSLPLRSYSKWspteQGATLVWRdlcvytnvggsgQRMKRIINNST 95
Cdd:PLN03232 1195 KAENSLNSVERVGNYIDLPS--EATAIIENNRPVSGWPSRGSIKF----EDVHLRYR------------PGLPPVLHGLS 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 96 GAIQPGTLMALMGSSGSGKTTLMSTLaFRqpAGTVVQGDILINGRRIGPF----MHRISGYVYQDDLfLGSLTVLEHLN- 170
Cdd:PLN03232 1257 FFVSPSEKVGVVGRTGAGKSSMLNAL-FR--IVELEKGRIMIDDCDVAKFgltdLRRVLSIIPQSPV-LFSGTVRFNIDp 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 171 FMAHLrlDRRVSKEERRLIIKELLERTGLlsaaqtrigsGDDKKVLSGGE------RKRLAFAVELLNNPVILFCDEPTT 244
Cdd:PLN03232 1333 FSEHN--DADLWEALERAHIKDVIDRNPF----------GLDAEVSEGGEnfsvgqRQLLSLARALLRRSKILVLDEATA 1400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 245 GLDSYSAQQLVATLYElAQKGTTILCTIHQPSSQLfdNFNNVMLLADGRVAFTGSPQHALS 305
Cdd:PLN03232 1401 SVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTII--DCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
89-305 |
2.35e-05 |
|
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: 47.49 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 89 RIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGT----VVQGDILINGRRIGPFMH----RISGYVYQD-DLF 159
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSgevnVRVGDEWVDMTKPGPDGRgrakRYIGILHQEyDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 LGSlTVLEHLNFMAHLRLDRRVSKeeRRLIIkeLLERTGLlsaaqtrigsgDDKKV----------LSGGERKRLAFAVE 229
Cdd:TIGR03269 378 PHR-TVLDNLTEAIGLELPDELAR--MKAVI--TLKMVGF-----------DEEKAeeildkypdeLSEGERHRVALAQV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 230 LLNNPVILFCDEPTTGLDSYSAQQLVATLY----ELAQkgtTILCTIHQpssqlFDNFNNV----MLLADGRVAFTGSPQ 301
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQ---TFIIVSHD-----MDFVLDVcdraALMRDGKIVKIGDPE 513
|
....
gi 17647959 302 HALS 305
Cdd:TIGR03269 514 EIVE 517
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
204-295 |
2.61e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 204 QTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLD---SYSAQQLVAtlyELAQKGTTILcTIHQPSSQLF 280
Cdd:PRK10982 386 RTQIGS------LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgaKFEIYQLIA---ELAKKDKGII-IISSEMPELL 455
|
90
....*....|....*
gi 17647959 281 DNFNNVMLLADGRVA 295
Cdd:PRK10982 456 GITDRILVMSNGLVA 470
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
91-265 |
2.69e-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: 47.13 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 91 INNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTvVQGDILINGRRIGPFMHRIS-----GYVYQDDLFLGSLTV 165
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT-WDGEIYWSGSPLKASNIRDTeragiVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 166 LEHLnFMAH-LRLD-RRVSKEERRLIIKELLERTGLLSAAQTRiGSGDdkkvLSGGERKRLAFAVELLNNPVILFCDEPT 243
Cdd:TIGR02633 96 AENI-FLGNeITLPgGRMAYNAMYLRAKNLLRELQLDADNVTR-PVGD----YGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180
....*....|....*....|..
gi 17647959 244 TGLDSYSAQQLVATLYELAQKG 265
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAHG 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
108-269 |
2.77e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.33 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 108 GSSGSGKTTLMSTLA-FRQPAGtvvqGDILINGRRIGPF--MHRIS---GYVYQDDLFLG---SLTVLEHL--------N 170
Cdd:COG3845 291 GVAGNGQSELAEALAgLRPPAS----GSIRLDGEDITGLspRERRRlgvAYIPEDRLGRGlvpDMSVAENLilgryrrpP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 171 FMAHLRLDRRVSKEERRLIIKELLERTGllsAAQTRIGSgddkkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYS 250
Cdd:COG3845 367 FSRGGFLDRKAIRAFAEELIEEFDVRTP---GPDTPARS------LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGA 437
|
170
....*....|....*....
gi 17647959 251 AQQLVATLYELAQKGTTIL 269
Cdd:COG3845 438 IEFIHQRLLELRDAGAAVL 456
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
98-241 |
4.42e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 46.71 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA-FRQPagtvVQGDILINGRRIGPfmHRISGY------VYQD-DLFlgsltvlEHL 169
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTgLYRP----ESGEILLDGQPVTA--DNREAYrqlfsaVFSDfHLF-------DRL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 170 NFMAHLRLDRRVskeerrliiKELLERTGLlsaaqtrigsgdDKKV-----------LSGGERKRLAFAVELLNN-PVIL 237
Cdd:COG4615 422 LGLDGEADPARA---------RELLERLEL------------DHKVsvedgrfsttdLSQGQRKRLALLVALLEDrPILV 480
|
....
gi 17647959 238 FcDE 241
Cdd:COG4615 481 F-DE 483
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
108-262 |
4.60e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.00 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 108 GSSGSGKTTLM------------------STLAFRQPAGTVVQGDILINGRR---------IGPFMHRISGYVYQddlFL 160
Cdd:COG0419 30 GPNGAGKSTILeairyalygkarsrsklrSDLINVGSEEASVELEFEHGGKRyrierrqgeFAEFLEAKPSERKE---AL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 161 GSLTVLEHL-NFMAHLRlDRRVSKEERrliIKELLERTGLLSAAQTRIGSGDDKKVLSGGERKRLAFAvELLNnpviLFC 239
Cdd:COG0419 107 KRLLGLEIYeELKERLK-ELEEALESA---LEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALA-DLLS----LIL 177
|
170 180
....*....|....*....|...
gi 17647959 240 DepTTGLDSYSAQQLVATLYELA 262
Cdd:COG0419 178 D--FGSLDEERLERLLDALEELA 198
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
98-264 |
7.05e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTtlMSTLAFR---QPAGTVVQGDILINGR---RIGPFMHR-ISG----YVYQDDLflGSLTVL 166
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKS--VSSLAIMgliDYPGRVMAEKLEFNGQdlqRISEKERRnLVGaevaMIFQDPM--TSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 167 EHLNF--MAHLRLDRRVSKEERRLIIKELLERTGLlSAAQTRIGSGDDKkvLSGGERKRLAFAVELLNNPVILFCDEPTT 244
Cdd:PRK11022 106 YTVGFqiMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRLDVYPHQ--LSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180
....*....|....*....|
gi 17647959 245 GLDSYSAQQLVATLYELAQK 264
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQK 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
79-247 |
9.23e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 79 NVGGSGqrmkriINNSTGAIQPGTLMALMGSSGSGKTTLMSTLafrQPAGTVVQGDILINGRRIGPFMHR---ISGYVY- 154
Cdd:PRK10762 262 NLSGPG------VNDVSFTLRKGEILGVSGLMGAGRTELMKVL---YGALPRTSGYVTLDGHEVVTRSPQdglANGIVYi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 155 -----QDDLFLG-------SLTVLEHL-NFMAHLRldrrvSKEERRLI---IKELLERTGllSAAQTrIGsgddkkVLSG 218
Cdd:PRK10762 333 sedrkRDGLVLGmsvkenmSLTALRYFsRAGGSLK-----HADEQQAVsdfIRLFNIKTP--SMEQA-IG------LLSG 398
|
170 180
....*....|....*....|....*....
gi 17647959 219 GERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
179-284 |
1.13e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 179 RRVSKEERRLIikELLERTGLlsaaqtrigsGDDKKV-------LSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSA 251
Cdd:PRK15093 127 QRFGWRKRRAI--ELLHRVGI----------KDHKDAmrsfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQ 194
|
90 100 110
....*....|....*....|....*....|....*.
gi 17647959 252 QQLVATLYELAQ-KGTTILCTIH--QPSSQLFDNFN 284
Cdd:PRK15093 195 AQIFRLLTRLNQnNNTTILLISHdlQMLSQWADKIN 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
216-273 |
1.51e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 216 LSGGERKRLAFAVELL---NNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIH 273
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
105-292 |
1.63e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.00 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 105 ALMGSSGSGKTTL------MSTL--AFRQpAGTVVQGDILINGRRIGPF-MHRISGYVYQD-DLFLGSltVLEHLNFMAH 174
Cdd:PRK14243 40 AFIGPSGCGKSTIlrcfnrLNDLipGFRV-EGKVTFHGKNLYAPDVDPVeVRRRIGMVFQKpNPFPKS--IYDNIAYGAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 175 LR-----LDRRVSKEERRLI----IKELLERTGLlsaaqtrigsgddkkVLSGGERKRLAFAVELLNNPVILFCDEPTTG 245
Cdd:PRK14243 117 INgykgdMDELVERSLRQAAlwdeVKDKLKQSGL---------------SLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17647959 246 LDSYSAQQLVATLYELAQKGTTILCTiH--QPSSQLFD--NFNNVMLLADG 292
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYTIIIVT-HnmQQAARVSDmtAFFNVELTEGG 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
98-271 |
1.67e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLAFRQPAgtVVQGDILINGRrigpfmhriSGYVYQDDLFLGSlTVLEHLNFMAHLRL 177
Cdd:PLN03130 640 VPVGSLVAIVGSTGEGKTSLISAMLGELPP--RSDASVVIRGT---------VAYVPQVSWIFNA-TVRDNILFGSPFDP 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 178 DRRvskeERRLIIKELLERTGLLSAA-QTRIGsgdDKKV-LSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLV 255
Cdd:PLN03130 708 ERY----ERAIDVTALQHDLDLLPGGdLTEIG---ERGVnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
|
170
....*....|....*...
gi 17647959 256 ATLY--ELAQKgTTILCT 271
Cdd:PLN03130 781 DKCIkdELRGK-TRVLVT 797
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
90-274 |
2.35e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.63 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 90 IINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA-FRQPAgtvvQGDILINGRRIgpfmhRISGYVYQDDL-FLG------ 161
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAgLLNPE----KGEILFERQSI-----KKDLCTYQKQLcFVGhrsgin 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 162 -SLTVLEHLNFMAHLrldrrvskEERRLIIKELLERTGLLSAAQTRIGsgddkkVLSGGERKRLAFAVELLNNPVILFCD 240
Cdd:PRK13540 87 pYLTLRENCLYDIHF--------SPGAVGITELCRLFSLEHLIDYPCG------LLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....
gi 17647959 241 EPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQ 274
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
98-247 |
2.47e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.91 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 98 IQPGTLMALMGSSGSGKTTLMSTLA--FRQPAGTV-VQGDILINGRRIgpfmhRISGYVYQDDLFLGSLTVLEHLNFMAH 174
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAglLHVESGQIqIDGKTATRGDRS-----RFMAYLGHLPGLKADLSTLENLHFLCG 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647959 175 LRLDRRVSKEERRLIIkellerTGLLSAAQTRIgsgddkKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLD 247
Cdd:PRK13543 109 LHGRRAKQMPGSALAI------VGLAGYEDTLV------RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
214-271 |
3.12e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 3.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647959 214 KVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSaqqlVATLyE--LAQ-KGTTILCT 271
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWL-EqfLHDyPGTVVAVT 217
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
163-300 |
3.36e-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: 43.85 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 163 LTVLEHLNFMAHLRLDRRvSKEERRLIIKELLERTGLL-----------SAAQTrigsgddkkvLSGGERKRLAFAVEL- 230
Cdd:TIGR00630 436 LSIREAHEFFNQLTLTPE-EKKIAEEVLKEIRERLGFLidvgldylslsRAAGT----------LSGGEAQRIRLATQIg 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 231 --LNNpVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSqlfdnfnnvMLLAD-------------GRVA 295
Cdd:TIGR00630 505 sgLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDT---------IRAADyvidigpgagehgGEVV 574
|
....*
gi 17647959 296 FTGSP 300
Cdd:TIGR00630 575 ASGTP 579
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
88-247 |
3.54e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLA--------------------FRQ------PAGTVVQG------DI 135
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLgqlqadsgrihcgtklevayFDQhraeldPEKTVMDNlaegkqEV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 136 LINGRRigpfmHRISGYVyQDDLFlgsltvlehlnfmahlrldrrvskEERRliikellertgllsaAQTRIgsgddkKV 215
Cdd:PRK11147 412 MVNGRP-----RHVLGYL-QDFLF------------------------HPKR---------------AMTPV------KA 440
|
170 180 190
....*....|....*....|....*....|....
gi 17647959 216 LSGGERKRLAFAVELL--NNPVILfcDEPTTGLD 247
Cdd:PRK11147 441 LSGGERNRLLLARLFLkpSNLLIL--DEPTNDLD 472
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
88-255 |
3.77e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGtvVQGDILINGRRIGpfmhriSGYVYQDdlflgsltVLE 167
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQG--YSNDLTLFGRRRG------SGETIWD--------IKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 168 HLNFMA-HLRLDRRVSKEERRLIIKELLERTGL---LSAAQTRIGS------GDDKKV-------LSGGERKRLAFAVEL 230
Cdd:PRK10938 337 HIGYVSsSLHLDYRVSTSVRNVILSGFFDSIGIyqaVSDRQQKLAQqwldilGIDKRTadapfhsLSWGQQRLALIVRAL 416
|
170 180
....*....|....*....|....*
gi 17647959 231 LNNPVILFCDEPTTGLDSYSaQQLV 255
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLN-RQLV 440
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
88-140 |
4.05e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 4.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 17647959 88 KRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAgTVVQGDILINGR 140
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY-EVTGGTVEFKGK 65
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
66-305 |
4.34e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.59 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 66 GATLVWRDLCV-YTNvggsgqRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLmsTLAFRQPAgTVVQGDILINGRRIGP 144
Cdd:cd03288 17 GGEIKIHDLCVrYEN------NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMV-DIFDGKIVIDGIDISK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 145 F-MH----RISgYVYQDD-LFLGSLtvlehlnfmaHLRLDRRVSKEERRLIikELLERTGLLSAAQTRIGsGDDKKVLSG 218
Cdd:cd03288 88 LpLHtlrsRLS-IILQDPiLFSGSI----------RFNLDPECKCTDDRLW--EALEIAQLKNMVKSLPG-GLDAVVTEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 219 GE------RKRLAFAVELLNNPVILFCDEPTTGLDSYSA---QQLVATlyelAQKGTTILCTIHQPSSQLfdNFNNVMLL 289
Cdd:cd03288 154 GEnfsvgqRQLFCLARAFVRKSSILIMDEATASIDMATEnilQKVVMT----AFADRTVVTIAHRVSTIL--DADLVLVL 227
|
250
....*....|....*.
gi 17647959 290 ADGRVAFTGSPQHALS 305
Cdd:cd03288 228 SRGILVECDTPENLLA 243
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
178-282 |
4.65e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 178 DRRVSKEERRLIIKELLerTGLLSAAQTRIGSGDDKkvLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVAT 257
Cdd:PTZ00265 546 DSEVVDVSKKVLIHDFV--SALPDKYETLVGSNASK--LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
90 100
....*....|....*....|....*.
gi 17647959 258 LYELAQKGTTILCTI-HQPSSQLFDN 282
Cdd:PTZ00265 622 INNLKGNENRITIIIaHRLSTIRYAN 647
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
160-301 |
1.30e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 160 LGSLTVLEHLNFMAHLRLDRRvSKEERRLIIKELLERTGLLS-----------AAQTrigsgddkkvLSGGE--RKRLAF 226
Cdd:COG0178 430 LTALSIDEALEFFENLELTER-EAEIAERILKEIRSRLGFLVdvgldyltldrSAGT----------LSGGEaqRIRLAT 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 227 AV--ELLNnpV--ILfcDEPTTGL---DSysaQQLVATLYELAQKGTTILCTIHQPssqlfdnfnNVMLLAD-------- 291
Cdd:COG0178 499 QIgsGLVG--VlyVL--DEPSIGLhqrDN---DRLIETLKRLRDLGNTVIVVEHDE---------DTIRAADyiidigpg 562
|
170
....*....|....*
gi 17647959 292 -----GRVAFTGSPQ 301
Cdd:COG0178 563 agehgGEVVAQGTPE 577
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
76-305 |
1.51e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.84 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 76 VYTNVGGSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTL---MSTLAFRQPAGTVVQGDILINGRRIGPFMHRiSGY 152
Cdd:PRK13633 11 SYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSEGKVYVDGLDTSDEENLWDIRNK-AGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 153 VYQD-DLFLGSLTVLEHLNFMAHlrlDRRVSKEERRLIIKELLERTGLLsaaqtrigsgDDKK----VLSGGERKRLAFA 227
Cdd:PRK13633 90 VFQNpDNQIVATIVEEDVAFGPE---NLGIPPEEIRERVDESLKKVGMY----------EYRRhaphLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 228 VELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQK-GTTILCTIHQPSSQLfdNFNNVMLLADGRVAFTGSPQHALS 305
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAV--EADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
190-269 |
1.54e-03 |
|
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: 41.69 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 190 IKELLERT---GLLSAAQTRIGSGD--DKKV--LSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYsaQQL-VA-TLYE 260
Cdd:COG1245 180 VRELLEKVderGKLDELAEKLGLENilDRDIseLSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY--QRLnVArLIRE 257
|
....*....
gi 17647959 261 LAQKGTTIL 269
Cdd:COG1245 258 LAEEGKYVL 266
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
216-269 |
1.73e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 17647959 216 LSGGERKRLAFAVELLNNPV-----ILfcDEPTTGLDSYSAQQLVATLYELAQKGTTIL 269
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktlyIL--DEPTTGLHFEDIRKLLEVLHRLVDKGNTVV 887
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
193-293 |
2.60e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.89 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 193 LLERTGLLSAAQtrigsgDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTtgldSYSAQQLVATLYELAQK-GTTILCT 271
Cdd:TIGR00954 566 ILEREGGWSAVQ------DWMDVLSGGEKQRIAMARLFYHKPQFAILDECT----SAVSVDVEGYMYRLCREfGITLFSV 635
|
90 100
....*....|....*....|..
gi 17647959 272 IHQPSsqLFdNFNNVMLLADGR 293
Cdd:TIGR00954 636 SHRKS--LW-KYHEYLLYMDGR 654
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
216-273 |
2.66e-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: 40.04 E-value: 2.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647959 216 LSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIH 273
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
216-304 |
3.20e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 216 LSGGERKRLAFA----VELLNNPVILfcDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQpssqlfdnfNNVMLLAD 291
Cdd:PRK00635 477 LSGGEQERTALAkhlgAELIGITYIL--DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD---------EQMISLAD 545
|
90 100
....*....|....*....|....*.
gi 17647959 292 -------------GRVAFTGSPQHAL 304
Cdd:PRK00635 546 riidigpgagifgGEVLFNGSPREFL 571
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
216-299 |
8.45e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 216 LSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYeLAQKGttiLCTIHQPSSQLFDNFNNVMLLADGRVA 295
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQGG---VLMVSHDEHLISGSVDELWVVSEGKVT 703
|
....*
gi 17647959 296 -FTGS 299
Cdd:PLN03073 704 pFHGT 708
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
482-587 |
8.63e-03 |
|
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: 38.91 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 482 STGQYYAANILALLPGMIIEPLIFVIICYwltGLRSTFYAFGVTAMCVVLVMNVATACGCFFSTAFNSVPLAMAYLVPLD 561
Cdd:pfam12698 201 SPLQYWLGKILGDFLVGLLQLLIILLLLF---GIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVI 277
|
90 100
....*....|....*....|....*..
gi 17647959 562 YIFMITSGIFIQVNSLPVAF-WWTQFL 587
Cdd:pfam12698 278 LLLSGFFGGLFPLEDPPSFLqWIFSII 304
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
503-600 |
9.72e-03 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 37.87 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647959 503 LIFVIICYWLTGLRSTFYAFGVTAMCVVLVMNVATACGCFFSTAFNSVPLAMAYLVPLDYIFMITSGIFIQVNSLPvafW 582
Cdd:COG0842 65 LLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLP---G 141
|
90 100
....*....|....*....|.
gi 17647959 583 WTQFLSWML---YANEAMTAA 600
Cdd:COG0842 142 WLQAIAYLNpltYFVEALRAL 162
|
|
| |
