|
Name |
Accession |
Description |
Interval |
E-value |
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-255 |
0e+00 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 499.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVEAE 240
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
250
....*....|....*
gi 556321685 241 IHPEPVSGRPMCVVK 255
Cdd:PRK11231 241 IHPEPVSGTPMCVVR 255
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-253 |
5.14e-140 |
|
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: 393.25 E-value: 5.14e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALL 81
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHHLSPEGITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKR-QGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVEAE 240
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|...
gi 556321685 241 IHPEPVSGRPMCV 253
Cdd:COG1120 241 VIEDPVTGRPLVL 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-253 |
2.39e-110 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 317.80 E-value: 2.39e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 4 RTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 H-HLSPEgITVRELVSYGRSPWLSlwGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:COG4604 83 EnHINSR-LTVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 163 DEPTTYLDINHQVELMRLmveLKR----QGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVE 238
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKL---LRRladeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTD 236
|
250
....*....|....*
gi 556321685 239 AEIHpePVSGRPMCV 253
Cdd:COG4604 237 IEVE--EIDGKRICV 249
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-251 |
3.87e-91 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 269.29 E-value: 3.87e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLP 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGITVRELVSYGRSPWlslwGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQ------D 156
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 157 TP-LILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVF 235
Cdd:COG4559 158 GPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
250
....*....|....*.
gi 556321685 236 SVEAEIHPEPVSGRPM 251
Cdd:COG4559 238 GADLRVLAHPEGGCPQ 253
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-253 |
2.80e-90 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 267.62 E-value: 2.80e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALL 81
Cdd:PRK10253 7 RLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHHLSPEGITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKR-QGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVEAE 240
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCM 246
|
250
....*....|...
gi 556321685 241 IHPEPVSGRPMCV 253
Cdd:PRK10253 247 IIDDPVAGTPLVV 259
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-251 |
1.08e-89 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 265.87 E-value: 1.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQH-HLS-PegITVRELVSYGRSPwlslWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQ--- 155
Cdd:PRK13548 81 LPQHsSLSfP--FTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 156 ---DTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELL 231
Cdd:PRK13548 155 pdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETL 234
|
250 260
....*....|....*....|
gi 556321685 232 KTVFSVEAEIHPEPVSGRPM 251
Cdd:PRK13548 235 RRVYGADVLVQPHPETGAPL 254
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-220 |
1.78e-88 |
|
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: 259.68 E-value: 1.78e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 4 RTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 hhlspegitvrelvsygrspwlslwgrlsaednervnvAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLD 163
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 164 EPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-235 |
2.86e-84 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 251.55 E-value: 2.86e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIagfsaRQLARRLALLP 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEG--ITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:COG1121 82 QRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLAsGRVMAQGAPEAVMKPELLKTVF 235
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVLTPENLSRAY 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-254 |
8.51e-84 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 251.25 E-value: 8.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 4 RTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 HHLSPEGITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLD 163
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 164 EPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVEAEIH 242
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGIL 252
|
250
....*....|..
gi 556321685 243 PEPVSGRPMCVV 254
Cdd:PRK10575 253 PHPAGAAPVSFV 264
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
3-251 |
3.14e-77 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 234.32 E-value: 3.14e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLP 82
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 163 DEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVEAEIH 242
Cdd:TIGR03873 162 DEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGVDATVL 241
|
....*....
gi 556321685 243 PEPVSGRPM 251
Cdd:TIGR03873 242 THPDTGRPI 250
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-250 |
7.54e-76 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 235.51 E-value: 7.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVEAE 240
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTA 241
|
250
....*....|
gi 556321685 241 IHPEPVSGRP 250
Cdd:PRK09536 242 VGTDPATGAP 251
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-220 |
3.47e-73 |
|
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: 222.41 E-value: 3.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 4 RTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDekpiaGFSARQLARRLALLPQ 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-----GKPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 HHLSPEG--ITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLAsGRVMAQG 220
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-232 |
8.77e-66 |
|
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: 204.10 E-value: 8.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY-GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALL 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHhlsPE----GITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDT 157
Cdd:COG1122 81 FQN---PDdqlfAPTVEEDVAFG----PENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 158 PLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK-PELLK 232
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSdYELLE 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-235 |
9.15e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 201.45 E-value: 9.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGfSARQLARRLALLP 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGITVRELVSYgrspWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:COG1131 80 QEPALYPDLTVRENLRF----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 163 DEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKpELLKTVF 235
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA-RLLEDVF 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-215 |
8.03e-64 |
|
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: 198.46 E-value: 8.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 4 RTENLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALL 81
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHhlsPE----GITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDT 157
Cdd:cd03225 81 FQN---PDdqffGPTVEEEVAFG----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 158 PLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGR 215
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-241 |
2.64e-63 |
|
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: 198.16 E-value: 2.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAgFSARQLARRLALLP 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGITVRELVSY-GRspwlsLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:COG4555 81 DERGLYDRLTVRENIRYfAE-----LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV--------MKPELLKT 233
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELreeigeenLEDAFVAL 235
|
....*...
gi 556321685 234 VFSVEAEI 241
Cdd:COG4555 236 IGSEEGEA 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-227 |
7.94e-58 |
|
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: 183.79 E-value: 7.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR----- 77
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 ---LALLPqhhlspeGITVRE------LVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAF 148
Cdd:cd03219 81 fqiPRLFP-------ELTVLEnvmvaaQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 149 LAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-251 |
1.04e-55 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 178.88 E-value: 1.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLtPDSGEILLDEKPIAGFSARQLARRLALLPQHHLSPEGITVRELv 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQY- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 98 sygrspwLSLWGRLSAEDNERVNVAMSQTRTRNLAD---RRLTQLSGGQRQRAFLAMVLAQDTP-------LILLDEPTT 167
Cdd:COG4138 90 -------LALHQPAGASSEAVEQLLAQLAEALGLEDklsRPLTQLSGGEWQRVRLAAVLLQVWPtinpegqLLLLDEPMN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 168 YLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVEAEIHpePVS 247
Cdd:COG4138 163 SLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRL--EVE 240
|
....
gi 556321685 248 GRPM 251
Cdd:COG4138 241 GHRW 244
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-216 |
1.24e-55 |
|
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: 176.05 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGfSARQLARRLALLP 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGITVRElvsygrspwlslwgrlsaednervnvamsqtrtrNLadrrltQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:cd03230 80 EEPSLYENLTVRE----------------------------------NL------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556321685 163 DEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-225 |
2.25e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 177.94 E-value: 2.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY-GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA---RRL 78
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHHLSPEGITVRELVSYGR----SPWLSLWGRLSAEDN-------ERVNVAmsqtrtrNLADRRLTQLSGGQRQRA 147
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRlgrtSTWRSLLGLFPPEDReralealERVGLA-------DKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 148 FLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-220 |
1.91e-54 |
|
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: 174.63 E-value: 1.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLP 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QH-----HLspegiTVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDT 157
Cdd:cd03259 79 QDyalfpHL-----TVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 158 PLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-226 |
4.36e-53 |
|
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: 179.33 E-value: 4.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY-----GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSA---RQL 74
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 75 ARRLALLPQ---HHLSPEgITVRELVSYGrspwLSLWGRLSAED-NERVNVAMSQTR-TRNLADRRLTQLSGGQRQRAFL 149
Cdd:COG1123 341 RRRVQMVFQdpySSLNPR-MTVGDIIAEP----LRLHGLLSRAErRERVAELLERVGlPPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 150 AMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVM 226
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-225 |
9.54e-53 |
|
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: 171.21 E-value: 9.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQ-AVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIA---GFSARQLARRL 78
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHHLSPEGITVRELVSYGR----SPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLA 154
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 155 QDTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-211 |
4.96e-52 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 167.41 E-value: 4.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 11 SYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEIlldekpiagfsARQLARRLALLPQHHLSPEG 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 91 --ITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTY 168
Cdd:NF040873 70 lpLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556321685 169 LDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYcDHLVVL 211
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-227 |
2.34e-51 |
|
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: 167.46 E-value: 2.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA---RRLALLP 82
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHhlspeG-----ITVRELVSYGrspwLSLWGRLSAED-NERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQD 156
Cdd:COG1127 89 QG-----GalfdsLTVFENVAFP----LREHTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 157 TPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-227 |
3.41e-51 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 167.52 E-value: 3.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR----- 77
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiart 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 ---LALLPqhhlspeGITVRE-----LVSYGRSPWLSLWGRLS------AEDNERVNVAMSQTRTRNLADRRLTQLSGGQ 143
Cdd:COG0411 85 fqnPRLFP-------ELTVLEnvlvaAHARLGRGLLAALLRLPrarreeREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 144 RQRAFLAMVLAQDTPLILLDEPTTYLdiNHQ--VELMRLMVELKR-QGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGL--NPEetEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
....*..
gi 556321685 221 APEAVMK 227
Cdd:COG0411 236 TPAEVRA 242
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-215 |
3.99e-51 |
|
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: 163.95 E-value: 3.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 4 RTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 hhlspegitvrelvsygrspwlslwgrlsaednervnvamsqtrtrnladrrltqLSGGQRQRAFLAMVLAQDTPLILLD 163
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556321685 164 EPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGR 215
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-225 |
1.12e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 169.12 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLP 82
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QH-----HLspegiTVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDT 157
Cdd:COG3842 84 QDyalfpHL-----TVAENVAFG----LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 158 PLILLDEPTTYLDINH----QVELMRLmveLKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:COG3842 155 RVLLLDEPLSALDAKLreemREELRRL---QRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-219 |
4.43e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 163.68 E-value: 4.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYG----AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA--R 76
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 RLAL---LPQHHLSPEgITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVL 153
Cdd:COG1136 85 RRHIgfvFQFFNLLPE-LTALENVALP----LLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 154 AQDTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASrYCDHLVVLASGRVMAQ 219
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-227 |
5.55e-50 |
|
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: 163.83 E-value: 5.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSA---RQLARRLALLP 82
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGITVRELVSYgrspWLSLWGRLSAED-NERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:cd03261 84 QSGALFDSLTVFENVAF----PLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 162 LDEPTTYLD-INHQVeLMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:cd03261 160 YDEPTAGLDpIASGV-IDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-225 |
5.84e-50 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 164.01 E-value: 5.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQ-AVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSA---RQLARRL 78
Cdd:TIGR02315 2 LEVENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHHLSPEGITVRELVSYGR----SPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLA 154
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 155 QDTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
1.22e-49 |
|
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: 162.68 E-value: 1.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY----GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA--- 75
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RRLALLPQH---HLSPeGITVRELVsygRSPwLSLWGRLSAEDNERVNVAMSQTR---TRNLADRRLTQLSGGQRQRAFL 149
Cdd:cd03257 82 KEIQMVFQDpmsSLNP-RMTIGEQI---AEP-LRIHGKLSKKEARKEAVLLLLVGvglPEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 150 AMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-227 |
1.90e-49 |
|
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: 162.66 E-value: 1.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGA----QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRL 78
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHhlsPEGI-----TVRELVSygrspwLSLWGRLSAEDNERVNVAMSQTR-TRNLADRRLTQLSGGQRQRAFLAMV 152
Cdd:COG1124 82 QMVFQD---PYASlhprhTVDRILA------EPLRIHGLPDREERIAELLEQVGlPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-255 |
2.39e-48 |
|
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: 166.62 E-value: 2.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPD---SGEILLDEKPIAGFSARQLARR 77
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 LALLPQhhlSPE----GITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVL 153
Cdd:COG1123 85 IGMVFQ---DPMtqlnPVTVGDQIAEA----LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 154 AQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK-PELL 231
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAaPQAL 237
|
250 260
....*....|....*....|....*..
gi 556321685 232 KTVFSVEA---EIHPEPVSGRPMCVVK 255
Cdd:COG1123 238 AAVPRLGAargRAAPAAAAAEPLLEVR 264
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-225 |
6.87e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.85 E-value: 6.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPI-AGFSARQlaRRLA 79
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE--RRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQH-----HLspegiTVRELVSYGrspwLSLWGRLSAEDNERVN-----VAMSQtrtrnLADRRLTQLSGGQRQRAFL 149
Cdd:COG1118 79 FVFQHyalfpHM-----TVAENIAFG----LRVRPPSKAEIRARVEellelVQLEG-----LADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 150 AMVLAQDTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-237 |
8.55e-48 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 159.22 E-value: 8.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPD--------SGEILLDEKPIAGFSARQL 74
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 75 ARRLALLPQHHLSPEGITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLA 154
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 155 Q---------DTPLILLDEPTTYLDINHQVELMRLMVELKRQGKT-VVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEA 224
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250
....*....|...
gi 556321685 225 VMKPELLKTVFSV 237
Cdd:PRK13547 242 VLTPAHIARCYGF 254
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-216 |
3.51e-47 |
|
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: 156.11 E-value: 3.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA----VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA--- 75
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 -RRLALLPQ-HHLSPEgITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVL 153
Cdd:cd03255 81 rRHIGFVFQsFNLLPD-LTALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 154 AQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDlNQASRYCDHLVVLASGRV 216
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-215 |
4.16e-47 |
|
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: 154.65 E-value: 4.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIA--GFSARQLARRLAL 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGITVRELVSYGrspwlslwgrlsaednervnvamsqtrtrnladrrltqLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGR 215
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-229 |
2.13e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 154.53 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVldGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLP 82
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 Q-----HHLspegiTVRELVSYGRSPWLslwgRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDT 157
Cdd:COG3840 78 QennlfPHL-----TVAQNIGLGLRPGL----KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 158 PLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPE 229
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
7.47e-46 |
|
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: 152.25 E-value: 7.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAgFSARQLARRLAL 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR-DAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGITVRELVSYgrspWLSLWGRlsAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRF----WAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHD 197
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-227 |
3.42e-45 |
|
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: 159.15 E-value: 3.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY-GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALL 81
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQH-HLsPEGiTVRElvsygrspWLSLwGRLSAEDnERVNVAMSQTrtrNLAD--RRLTQ------------LSGGQRQR 146
Cdd:COG4988 417 PQNpYL-FAG-TIRE--------NLRL-GRPDASD-EELEAALEAA---GLDEfvAALPDgldtplgeggrgLSGGQAQR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 147 AFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRqGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVM 226
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELL 559
|
.
gi 556321685 227 K 227
Cdd:COG4988 560 A 560
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-225 |
6.92e-45 |
|
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: 150.41 E-value: 6.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLL-----TPDSGEILLDEKPIAGFSARQLA-- 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RRLALLPQhHLSPEGITVRELVSYGrspwLSLWG-RLSAEDNERVNVAMSQTRTRNLADRRL--TQLSGGQRQRAFLAMV 152
Cdd:cd03260 81 RRVGMVFQ-KPNPFPGSIYDNVAYG----LRLHGiKLKEELDERVEEALRKAALWDEVKDRLhaLGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQgKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-167 |
1.38e-44 |
|
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: 147.02 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQH-HLSPEgITVREL 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDpQLFPR-LTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 97 VSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRL----TQLSGGQRQRAFLAMVLAQDTPLILLDEPTT 167
Cdd:pfam00005 80 LRLG----LLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-216 |
3.58e-44 |
|
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: 148.39 E-value: 3.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYG----AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGfsarqLARRL 78
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHHLSPEGITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTP 158
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALG----LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 159 LILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLAS--GRV 216
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-226 |
5.19e-44 |
|
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: 148.60 E-value: 5.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGA-QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRL--- 78
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIgyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ----ALLPqhHLspegiTVRELVsyGRSPWLSLWGRlsAEDNERVNVAMSQTR--TRNLADRRLTQLSGGQRQRAFLAMV 152
Cdd:cd03295 81 iqqiGLFP--HM-----TVEENI--ALVPKLLKWPK--EKIRERADELLALVGldPAEFADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVM 226
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-215 |
6.47e-44 |
|
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: 145.99 E-value: 6.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYG--AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQH-HLSPEgiTVRElvsygrspwlslwgrlsaednervnvamsqtrtrNLadrrltqLSGGQRQRAFLAMVLAQDTPL 159
Cdd:cd03228 81 VPQDpFLFSG--TIRE----------------------------------NI-------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 160 ILLDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNQAsRYCDHLVVLASGR 215
Cdd:cd03228 118 LILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-225 |
1.81e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 150.22 E-value: 1.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALL 81
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQH-----HLspegiTVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQD 156
Cdd:COG3839 81 FQSyalypHM-----TVYENIAFP----LKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 157 TPLILLDEPTTYLD----INHQVELMRLmveLKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:COG3839 152 PKVFLLDEPLSNLDaklrVEMRAEIKRL---HRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
1.03e-42 |
|
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: 152.61 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLA 79
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQH-HLSPEgiTVRE-LvsygrspwlsLWGRLSAEDnERVNVAMSQTRTRNLADR-------RL----TQLSGGQRQR 146
Cdd:COG4987 413 VVPQRpHLFDT--TLREnL----------RLARPDATD-EELWAALERVGLGDWLAAlpdgldtWLgeggRRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 147 AFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVM 226
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELL 557
|
.
gi 556321685 227 K 227
Cdd:COG4987 558 A 558
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-216 |
1.09e-42 |
|
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: 143.94 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 4 RTENLTVSYG-AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIagfSARQLARRLALLP 82
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 Q---HHLSPEgiTVRELVSYGRspwlslwgRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPL 159
Cdd:cd03226 78 QdvdYQLFTD--SVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 160 ILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-222 |
1.92e-42 |
|
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: 143.80 E-value: 1.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYG--AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAgfSARQLARR-LA 79
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAARQsLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLSPEGITVRE-LVSYGRspwlsLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTP 158
Cdd:cd03263 79 YCPQFDALFDELTVREhLRFYAR-----LKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 159 LILLDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAP 222
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-216 |
2.60e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.03 E-value: 2.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLP 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGiTVRELVSYgrsPWLSlwgRLSAEDNERVNVAMSQ-TRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:COG4619 81 QEPALWGG-TVRDNLPF---PFQL---RERKFDRERALELLERlGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 162 LDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-220 |
2.95e-42 |
|
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: 143.10 E-value: 2.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQAVLDGLSLALPAGkITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGfSARQLARRLALLPQHH 85
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 86 LSPEGITVRELVSYgrSPWLSlwGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEP 165
Cdd:cd03264 82 GVYPNFTVREFLDY--IAWLK--GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 166 TTYLDINHQVELMRLMVELKrQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-223 |
2.97e-42 |
|
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: 143.92 E-value: 2.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLP 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHH-LSPEgITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:cd03300 79 QNYaLFPH-LTVFENIAFG----LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 162 LDEPTTYLDI----NHQVELMRLMVELkrqGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPE 223
Cdd:cd03300 154 LDEPLGALDLklrkDMQLELKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPE 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
1.70e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 142.54 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSY----GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSarqlaR 76
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----P 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 RLALLPQHHLSPEGITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQD 156
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALG----LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 157 TPLILLDEPTTYLD----INHQVELMRLmveLKRQGKTVVTVLHDLNQASRYCDHLVVLAS--GRV 216
Cdd:COG1116 157 PEVLLMDEPFGALDaltrERLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRI 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-251 |
2.03e-41 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 141.99 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 21 LSLALPAGKITALLGPNGCGKSTLLNCFSRLLtPDSGEILLDEKPIAGFSARQLARRLALLPQHHLSPEGITVRELVSYG 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 101 RSPwlslwGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTP-------LILLDEPTTYLDINH 173
Cdd:PRK03695 94 QPD-----KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 174 QVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVEAEIHpePVSGRPM 251
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRL--DVEGHPM 244
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-226 |
2.04e-41 |
|
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: 141.42 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR-LALL 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHHLSPEGITVRE---LVSYGRSPwlslwgRLSAEDNERVnVAMSqTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTP 158
Cdd:cd03224 81 PEGRRIFPELTVEEnllLGAYARRR------AKRKARLERV-YELF-PRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 159 LILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVM 226
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-234 |
2.87e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 142.59 E-value: 2.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGA-----QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIA---GFSARQLARR 77
Cdd:TIGR04521 4 KNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkKKKLKDLRKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 LALL---PQHHLSPEgiTVRELVSYG-RSPWLSLwgrlsAEDNERVNVAMSQTR-TRNLADRRLTQLSGGQRQRAFLAMV 152
Cdd:TIGR04521 84 VGLVfqfPEHQLFEE--TVYKDIAFGpKNLGLSE-----EEAEERVKEALELVGlDEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV-MKPEL 230
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVfSDVDE 236
|
....
gi 556321685 231 LKTV 234
Cdd:TIGR04521 237 LEKI 240
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-219 |
3.02e-41 |
|
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: 139.10 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlARRLallp 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 qhhlspeGItvrELVSygrspwlslwgrlsaednervnvamsqtrtrnladrrltQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:cd03216 76 -------GI---AMVY---------------------------------------QLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 163 DEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQ 219
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-232 |
7.33e-41 |
|
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: 140.12 E-value: 7.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR-LALL 81
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQ-HHLSPEgITVRE---LVSYGRSPwlslwGRLSAEDNERVnvamsQTRTRNLADRRL---TQLSGGQRQraFLAM--V 152
Cdd:COG0410 84 PEgRRIFPS-LTVEEnllLGAYARRD-----RAEVRADLERV-----YELFPRLKERRRqraGTLSGGEQQ--MLAIgrA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK-PELL 231
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAdPEVR 230
|
.
gi 556321685 232 K 232
Cdd:COG0410 231 E 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-231 |
1.33e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 140.64 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSY--GAQAvLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:PRK13647 8 EDLHFRYkdGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 hhlSPE----GITVRELVSYGrsPwLSLwGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPL 159
Cdd:PRK13647 87 ---DPDdqvfSSTVWDDVAFG--P-VNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 160 ILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELL 231
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-242 |
1.68e-40 |
|
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: 139.83 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGE--ILLDEKPiAGFSARQLARRLAL 80
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGERR-GGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 L-PQHHLS-PEGITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTP 158
Cdd:COG1119 83 VsPALQLRfPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 159 LILLDEPTTYLDINHQVELMRLMVELKRQG-KTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSV 237
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFGL 242
|
....*
gi 556321685 238 EAEIH 242
Cdd:COG1119 243 PVEVE 247
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-220 |
4.28e-40 |
|
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: 137.88 E-value: 4.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA----VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDekpiaGFSA----RQL 74
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-----GFDVvkepAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 75 ARRLALLPQHHLSPEGITVRELVSY-GRspwlsLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVL 153
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYfAG-----LYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 154 AQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-220 |
1.10e-39 |
|
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: 136.47 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVldGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAgfSARQLARRLALLP 82
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGITVRELVSYGRSPWLslwgRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGLSPGL----KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 163 DEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-220 |
2.31e-39 |
|
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: 135.87 E-value: 2.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAgFSARQlarRLALLP 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-IAARN---RIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHH-LSPEgITVRELVSYgrspWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:cd03269 77 EERgLYPK-MKVIDQLVY----LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-225 |
3.07e-39 |
|
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: 136.31 E-value: 3.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLAL 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGITVRELVSYG-----RSPWLSlwgrlSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQ 155
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGlrvkpRSERPP-----EAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 156 DTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-225 |
3.47e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 135.89 E-value: 3.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIaGFSARQLA---RRLA 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQH-----HLspegiTVRELVSYGrsPWLSL-WGRLSAEDN-----ERVNVAmsqtrtrNLADRRLTQLSGGQRQRAF 148
Cdd:COG1126 81 MVFQQfnlfpHL-----TVLENVTLA--PIKVKkMSKAEAEERamellERVGLA-------DKADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 149 LAMVLAQDTPLILLDEPTTYLD---INhqvELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-227 |
1.32e-38 |
|
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: 142.28 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYG--AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLA 79
Cdd:COG2274 473 DIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLSPEGiTVRELVSYGRsPWLSLwgrlsaednERVNVAMSQTrtrNLAD--RRL------------TQLSGGQRQ 145
Cdd:COG2274 553 VVLQDVFLFSG-TIRENITLGD-PDATD---------EEIIEAARLA---GLHDfiEALpmgydtvvgeggSNLSGGQRQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 146 RAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNQAsRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEEL 696
|
..
gi 556321685 226 MK 227
Cdd:COG2274 697 LA 698
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
2.53e-38 |
|
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: 140.11 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSY-GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGiTVRELVsygrspwlsLWGRLSAEDNERVNVAMS-------QTRTRNLA---DRRLTQLSGGQRQRAFLA 150
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENI---------RLARPDASDAEIREALERagldefvAALPQGLDtpiGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 151 MVLAQDTPLILLDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNQASRyCDHLVVL 211
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-238 |
4.66e-38 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 132.67 E-value: 4.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 23 LALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILldekpIAGFSARQLARRLALLPQHHL----SPegITVRELVS 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVK-----VAGASPGKGWRHIGYVPQRHEfawdFP--ISVAHTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 99 YGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELM 178
Cdd:TIGR03771 74 SGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 179 RLMVELKRQGKTVVTVLHDLNQASRYCDHlVVLASGRVMAQGAPEAVMKPELLKTVFSVE 238
Cdd:TIGR03771 154 ELFIELAGAGTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-250 |
9.29e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.08 E-value: 9.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIaGFSARqlaRRLALLp 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDR---RRIGYL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 qhhlsPE--GI----TVRELVSY-GRspwlsLWGrLSAEDN--------ERVNVAmsqtrtrNLADRRLTQLSGGQRQRA 147
Cdd:COG4152 77 -----PEerGLypkmKVGEQLVYlAR-----LKG-LSKAEAkrradewlERLGLG-------DRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 148 -FLAMVLAQdtP-LILLDEPTTYLD-INhqVELMR-LMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPE 223
Cdd:COG4152 139 qLIAALLHD--PeLLILDEPFSGLDpVN--VELLKdVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
250 260
....*....|....*....|....*..
gi 556321685 224 AVmKPELLKTVFSVEAEIHPEPVSGRP 250
Cdd:COG4152 215 EI-RRQFGRNTLRLEADGDAGWLRALP 240
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-249 |
1.04e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 134.16 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGfSARQLARRLALLP 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 Q-HHLSPEgITVRE-LVSYGRspwlsLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:PRK13537 87 QfDNLDPD-FTVREnLLVFGR-----YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVEAe 240
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEIYG- 239
|
....*....
gi 556321685 241 ihPEPVSGR 249
Cdd:PRK13537 240 --PDPVALR 246
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-227 |
1.10e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 132.26 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGfSARQLARRLALLPQ-HH 85
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 86 LSPEgITVRE-LVSYGRspwlslWGRLSAEDNERVNVAMSQ-TRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLD 163
Cdd:PRK13536 125 LDLE-FTVREnLLVFGR------YFGMSTREIEAVIPSLLEfARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 164 EPTTYLDiNHQVELM--RLMVELKRqGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:PRK13536 198 EPTTGLD-PHARHLIweRLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-223 |
1.35e-36 |
|
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: 130.07 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 22 SLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQL----ARRLALLPQHH-LSPEgITVREL 96
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFaLLPH-RTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 97 VSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLD----IN 172
Cdd:cd03294 123 VAFG----LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirRE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556321685 173 HQVELMRLMVELKRqgkTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPE 223
Cdd:cd03294 199 MQDELLRLQAELQK---TIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPE 246
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-227 |
1.40e-36 |
|
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: 129.38 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGaQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLP 82
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHH-LSPEgITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:cd03299 78 QNYaLFPH-MTVYKNIAYG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-217 |
5.63e-36 |
|
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: 126.99 E-value: 5.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLP 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHH-LSPEgITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:cd03301 79 QNYaLYPH-MTVYDNIAFG----LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 162 LDEPTTYLDINHQVElMRLmvELKR----QGKTVVTVLHDLNQASRYCDHLVVLASGRVM 217
Cdd:cd03301 154 MDEPLSNLDAKLRVQ-MRA--ELKRlqqrLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
4.86e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 126.50 E-value: 4.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY--GAQAvLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIaGFSAR---QLARR 77
Cdd:PRK13636 6 LKVEELNYNYsdGTHA-LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 LALL---PQHHLSpeGITVRELVSYGRspwLSLwGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLA 154
Cdd:PRK13636 84 VGMVfqdPDNQLF--SASVYQDVSFGA---VNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 155 QDTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAP-EAVMKPELLK 232
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPkEVFAEKEMLR 237
|
..
gi 556321685 233 TV 234
Cdd:PRK13636 238 KV 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-220 |
6.18e-35 |
|
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: 123.19 E-value: 6.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA--VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSArQLARRLAL 80
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQhhlspegitvrelvsygrSPWLslwgrlsaednervnvaMSQTRTRNLAdrrlTQLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:cd03247 80 LNQ------------------RPYL-----------------FDTTLRNNLG----RRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRqGKTVVTVLHDLnQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-230 |
6.99e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.14 E-value: 6.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlARRL-- 78
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQH-HLSPEgITVRE---LVSYGRSPWLSLWGRL---SAEDNERVNVAMSqtrtrnlADRRLTQLSGGQRQraflaM 151
Cdd:COG1129 82 AIIHQElNLVPN-LSVAEnifLGREPRRGGLIDWRAMrrrARELLARLGLDID-------PDTPVGDLSVAQQQ-----L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 152 V-----LAQDTPLILLDEPTTYLDiNHQVE-LMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:COG1129 149 VeiaraLSRDARVLILDEPTASLT-EREVErLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
....*
gi 556321685 226 MKPEL 230
Cdd:COG1129 228 TEDEL 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-233 |
1.42e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 130.28 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSY-GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQH 84
Cdd:COG1132 343 ENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 HLSPEGiTVRELVSYgrspwlslwGRLSAEDNERVNVAmsqtRTRNLAD--RRL------------TQLSGGQRQRAFLA 150
Cdd:COG1132 423 TFLFSG-TIRENIRY---------GRPDATDEEVEEAA----KAAQAHEfiEALpdgydtvvgergVNLSGGQRQRIAIA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 151 MVLAQDTPLILLDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNQAsRYCDHLVVLASGRVMAQGAPEavmkpEL 230
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHE-----EL 561
|
...
gi 556321685 231 LKT 233
Cdd:COG1132 562 LAR 564
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-216 |
1.96e-34 |
|
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: 123.02 E-value: 1.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSA--RQLARRLALLPQ 83
Cdd:cd03262 4 KNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELRQKVGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 H-HLSPEgITVRELVSYGRspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:cd03262 84 QfNLFPH-LTVLENITLAP---IKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556321685 163 DEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-220 |
2.11e-34 |
|
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: 122.71 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKpIAGFSARQLARRLALLP 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK-SYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEgITVRELVSYGrspwlslwGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:cd03268 80 APGFYPN-LTARENLRLL--------ARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 163 DEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-227 |
2.57e-34 |
|
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: 125.55 E-value: 2.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA----VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTP---DSGEILLDEKPIAGFSARQL- 74
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 75 ---ARRLALLPQ---HHLSPeGITVRELVSYGrspwLSLWGRLSAED-NERVNVAMSQTRTRNlADRRLT----QLSGGQ 143
Cdd:COG0444 82 kirGREIQMIFQdpmTSLNP-VMTVGDQIAEP----LRIHGGLSKAEaRERAIELLERVGLPD-PERRLDryphELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 144 RQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAP 222
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
....*
gi 556321685 223 EAVMK 227
Cdd:COG0444 236 EELFE 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-255 |
3.07e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 128.61 E-value: 3.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlARRL-- 78
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD-AIALgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHHLSPEGITVRELVSYGRSPWLSLWGRLSAEdNERVNVAMSQTrtrNLA---DRRLTQLSGGQRQRAFLAMVLAQ 155
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAA-RARIRELSERY---GLDvdpDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 156 DTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVF 235
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMV 238
|
250 260
....*....|....*....|...
gi 556321685 236 --SVEAEIHPEPVS-GRPMCVVK 255
Cdd:COG3845 239 grEVLLRVEKAPAEpGEVVLEVE 261
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-219 |
3.61e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 123.82 E-value: 3.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYG----AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlar 76
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 rlALLPQHH-LSPeGITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQ 155
Cdd:COG4525 79 --GVVFQKDaLLP-WLNVLDNVAFG----LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 156 DTPLILLDEPTTYLDI----NHQVELMRLMvelKRQGKTVVTVLHDLNQASRYCDHLVVLAS--GRVMAQ 219
Cdd:COG4525 152 DPRFLLMDEPFGALDAltreQMQELLLDVW---QRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-216 |
4.23e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 128.26 E-value: 4.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 5 TENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLdekpiagfsARQLarRLALLPQH 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGL--RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 HLSPEGITVRELVSYGRSPWLSLWGRLSA---------EDNERVNVAMSQ----------TRTRNLA----------DRR 135
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdEDLERLAELQEEfealggweaeARAEEILsglgfpeedlDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 136 LTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINhqvelmrlMVE-----LKRQGKTVVTVLHDlnqasRY-----C 205
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE--------SIEwleefLKNYPGTVLVVSHD-----RYfldrvA 216
|
250
....*....|.
gi 556321685 206 DHLVVLASGRV 216
Cdd:COG0488 217 TRILELDRGKL 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-225 |
7.46e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 123.26 E-value: 7.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY--GAQAvLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPI-----AGFSARQLA 75
Cdd:PRK13639 2 LETRDLKYSYpdGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RRLALLPQHHL-SPegiTVRELVSYGrsPwLSLwgRLSAEDNE-RVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVL 153
Cdd:PRK13639 81 GIVFQNPDDQLfAP---TVEEDVAFG--P-LNL--GLSKEEVEkRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 154 AQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-225 |
1.91e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 124.29 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRL-------A 79
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVntvfqsyA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPqhHLspegiTVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPL 159
Cdd:PRK09452 97 LFP--HM-----TVFENVAFG----LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 160 ILLDEPTTYLDIN----HQVELMRLMVELkrqGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK09452 166 LLLDESLSALDYKlrkqMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-223 |
1.99e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.68 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRL--LTPD---SGEILLDEKPI--AGFSARQL 74
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 75 ARRLALLPQhHLSPEGITVRELVSYGrspwLSLWGRLSAED-NERVNVAMSQTrtrNLADR---RL----TQLSGGQRQR 146
Cdd:COG1117 91 RRRVGMVFQ-KPNPFPKSIYDNVAYG----LRLHGIKSKSElDEIVEESLRKA---ALWDEvkdRLkksaLGLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 147 AFLAMVLAQDTPLILLDEPTTYLD-IN-HQVElmRLMVELKRQgKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPE 223
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDpIStAKIE--ELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-223 |
2.55e-33 |
|
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: 120.17 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 5 TENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILldekpIAGFS----ARQLARRLAL 80
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-----VAGHDvvrePREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGITVRE-LVSYGRspwlsLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPL 159
Cdd:cd03265 78 VFQDLSVDDELTGWEnLYIHAR-----LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 160 ILLDEPTTYLDINHQVELMRLMVELKR-QGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPE 223
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-227 |
2.76e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.05 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQhhlSPE----GITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQD 156
Cdd:PRK13635 86 VFQ---NPDnqfvGATVQDDVAFG----LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 157 TPLILLDEPTTYLDINHQVELMRLMVELKRQGK-TVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-220 |
6.88e-33 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 119.20 E-value: 6.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 22 SLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLPQHHLSPEGITVRELVSYGR 101
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 102 SPWLslwgRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLM 181
Cdd:TIGR01277 96 HPGL----KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556321685 182 VELKRQGK-TVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:TIGR01277 172 KQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-220 |
9.45e-33 |
|
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: 119.22 E-value: 9.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA----VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQL---A 75
Cdd:cd03258 2 IELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RRLALLPQHH--LSPEgiTVRELVSYgrsPwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVL 153
Cdd:cd03258 82 RRIGMIFQHFnlLSSR--TVFENVAL---P-LEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 154 AQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
6-236 |
1.82e-32 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 119.60 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSY--GAQAVLDGlSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEIlldekPIAGFSARQLARR--LALL 81
Cdd:PRK15056 10 NDVTVTWrnGHTALRDA-SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKnlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQhhlSPE-----GITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQD 156
Cdd:PRK15056 84 PQ---SEEvdwsfPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 157 TPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHlVVLASGRVMAQGAPEAVMKPELLKTVFS 236
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTVLASGPTETTFTAENLELAFS 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-227 |
3.96e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 120.59 E-value: 3.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ-----LARRLALL 81
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQrdicmVFQSYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PqhHLSpegitVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:PRK11432 91 P--HMS-----LGENVGYG----LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 162 LDEPTTYLDINhqveLMRLM----VELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:PRK11432 160 FDEPLSNLDAN----LRRSMrekiRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
4.35e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.09 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRL--LTPD---SGEILLDEKPIAGFSARQLAR 76
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 RLALLPQHHLSPEGITVRELVSYGrsPWLSLWGRLSAEDNERVNVAMSQTR----TRNLADRRLTQLSGGQRQRAFLAMV 152
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQgKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-235 |
7.36e-32 |
|
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: 116.87 E-value: 7.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR-LALL 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHHLSPEGITVRE---LVsygrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTP 158
Cdd:cd03218 81 PQEASIFRKLTVEEnilAV-------LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 159 LILLDEPTTYLD-INHQvELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVF 235
Cdd:cd03218 154 FLLLDEPFAGVDpIAVQ-DIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-242 |
1.28e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 119.03 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLAL 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGITVRELVSYGrspwLSLWGRL----SAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQD 156
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFG----LTVLPRRerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 157 TPLILLDEPTTYLDINHQVELMRLMVELKRQGK-TVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK-P------ 228
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWRePatrfvl 234
|
250
....*....|....
gi 556321685 229 ELLKTVFSVEAEIH 242
Cdd:PRK10851 235 EFMGEVNRLQGTIR 248
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-229 |
1.31e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 121.86 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQ--HHLSPegiTVRElvsygrspwlSLwgRLSAE--DNERVNVAMSQTRTRNLA--DRRLT--------QLSGGQRQR 146
Cdd:PRK11160 419 VSQrvHLFSA---TLRD----------NL--LLAAPnaSDEALIEVLQQVGLEKLLedDKGLNawlgeggrQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 147 AFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKrQGKTVVTVLHDLNQASRYcDHLVVLASGRVMAQGAPEAVM 226
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELL 561
|
...
gi 556321685 227 KPE 229
Cdd:PRK11160 562 AQQ 564
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-228 |
1.80e-31 |
|
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: 115.79 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGA-QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQH 84
Cdd:cd03253 4 ENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 H-LSPEgiTVRELVSYgrspwlslwGRLSAEDNERVN---VAMSQTRTRNLAD-------RRLTQLSGGQRQRAFLAMVL 153
Cdd:cd03253 84 TvLFND--TIGYNIRY---------GRPDATDEEVIEaakAAQIHDKIMRFPDgydtivgERGLKLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 154 AQDTPLILLDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMKP 228
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-227 |
3.42e-31 |
|
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: 115.02 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQA-VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:cd03254 2 EIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGiTVRELVSYgrspwlslwGRLSAEDnERVNVAMSQTRT----RNLADRRLTQ-------LSGGQRQRAFL 149
Cdd:cd03254 82 VLQDTFLFSG-TIMENIRL---------GRPNATD-EEVIEAAKEAGAhdfiMKLPNGYDTVlgenggnLSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 150 AMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNqASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-229 |
3.73e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.24 E-value: 3.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQA--VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:PRK13632 11 ENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 hhlSPE----GITVRELVSYGrspwlsLWGRL--SAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDT 157
Cdd:PRK13632 91 ---NPDnqfiGATVEDDIAFG------LENKKvpPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 158 PLILLDEPTTYLDINHQVELMRLMVELKRQG-KTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMKPE 229
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-220 |
4.20e-31 |
|
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: 113.80 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTV------SYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFS--RLLTPDSGEILLDEKPIagfSAR 72
Cdd:cd03213 2 VTLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 73 QLARRLALLPQH-HLSPEgITVRELVSYgrspwlslwgrlSAEdnervnvamsqtrtrnladrrLTQLSGGQRQRAFLAM 151
Cdd:cd03213 79 SFRKIIGYVPQDdILHPT-LTVRETLMF------------AAK---------------------LRGLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 152 VLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHdlnQAS----RYCDHLVVLASGRVMAQG 220
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH---QPSseifELFDKLLLLSQGRVIYFG 194
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-226 |
6.96e-31 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 114.90 E-value: 6.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIA----------GFSAR 72
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 73 QLAR---RLALLPQH-----HLspegiTVRELVSYGrsPwLSLWGRLSAEDNERvnvAMSQTRTRNLADRRLT---QLSG 141
Cdd:COG4598 89 QLQRirtRLGMVFQSfnlwsHM-----TVLENVIEA--P-VHVLGRPKAEAIER---AEALLAKVGLADKRDAypaHLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 142 GQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGA 221
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
....*
gi 556321685 222 PEAVM 226
Cdd:COG4598 238 PAEVF 242
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-235 |
7.88e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 114.36 E-value: 7.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR-LA 79
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLSPEGITVRE---LVsygrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQD 156
Cdd:COG1137 82 YLPQEASIFRKLTVEDnilAV-------LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 157 TPLILLDEPTTYLD---INhqvELMRLMVELKRQGktvVTVL---HDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPEL 230
Cdd:COG1137 155 PKFILLDEPFAGVDpiaVA---DIQKIIRHLKERG---IGVLitdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
....*
gi 556321685 231 LKTVF 235
Cdd:COG1137 229 VRKVY 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-220 |
8.60e-31 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 119.82 E-value: 8.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQ--AVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLA 79
Cdd:TIGR02203 330 DVEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQH-HLSPEgiTVRELVSYGRSpwlslwGRLSAEDNERVNVAMSQTRTRNLADRRLTQ--------LSGGQRQRAFLA 150
Cdd:TIGR02203 410 LVSQDvVLFND--TIANNIAYGRT------EQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvlLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 151 MVLAQDTPLILLDEPTTYLDINH----QVELMRLMvelkrQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQG 220
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESerlvQAALERLM-----QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-216 |
9.02e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.61 E-value: 9.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSY-GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA---RRLALL 81
Cdd:COG2884 5 ENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQ-HHLSPEgITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:COG2884 85 FQdFRLLPD-RTVYENVALP----LRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-229 |
1.56e-30 |
|
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: 113.40 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQHHLSPEGiTVREL 96
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDG-TIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 97 VSYGRSPwlslwgRLSAEDNERVNVAMSQTRTRNLADR-------RLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYL 169
Cdd:cd03249 97 IRYGKPD------ATDEEVEEAAKKANIHDFIMSLPDGydtlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 170 DIN--HQVE--LMRLMVelkrqGKTVVTVLHDLNqASRYCDHLVVLASGRVMAQGAPEAVMKPE 229
Cdd:cd03249 171 DAEseKLVQeaLDRAMK-----GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-238 |
1.93e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.47 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLP 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGITVRELVSYGRSPwlslwGRLS-AEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQ-----DKLPkAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 162 LDEPTTYLDINHQvELMRLMVE--LKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMkpELLKTVFSVE 238
Cdd:PRK11607 173 LDEPMGALDKKLR-DRMQLEVVdiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY--EHPTTRYSAE 248
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-201 |
2.69e-30 |
|
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: 111.75 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIaGFSARQLA---RRLALLPQhhlSPE---- 89
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLerrQRVGLVFQ---DPDdqlf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 90 GITVRELVSYGRspwLSLwGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYL 169
Cdd:TIGR01166 83 AADVDQDVAFGP---LNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 556321685 170 DINHQVELMRLMVELKRQGKTVVTVLHDLNQA 201
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-227 |
3.06e-30 |
|
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: 112.71 E-value: 3.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYG--AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGiTVRELVSYGRSpwlslwgRLSAEDNERV-NVAMSQTRTRNLAD-------RRLTQLSGGQRQRAFLAMV 152
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGRP-------GATREEVEEAaRAANAHEFIMELPEgydtvigERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 153 LAQDTPLILLDEPTTYLDINH----QVELMRLMvelkrQGKTVVTVLHDLNQAsRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:cd03251 153 LLKDPPILILDEATSALDTESerlvQAALERLM-----KNRTTFVIAHRLSTI-ENADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-216 |
3.44e-30 |
|
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: 110.77 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYG--AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGiTVRElvsygrspwlslwgrlsaednervNVamsqtrtrnladrrltqLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:cd03246 81 LPQDDELFSG-SIAE------------------------NI-----------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRyCDHLVVLASGRV 216
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-198 |
5.06e-30 |
|
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: 117.08 E-value: 5.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSY-GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQH-HLSpeGITVRELVsygrspwlsLWGRLSAEDNErVNVAMSQTRTRNLADRRL-----------TQLSGGQRQRAF 148
Cdd:TIGR02868 414 CAQDaHLF--DTTVRENL---------RLARPDATDEE-LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556321685 149 LAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKrQGKTVVTVLHDL 198
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHHL 530
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-226 |
5.79e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.11 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSAR-QLARRLA--LLPQ 83
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDeRLIRQEAgmVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 HHLSPEgITVRELVSYGrsPwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLD 163
Cdd:PRK09493 86 FYLFPH-LTALENVMFG--P-LRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 164 EPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVM 226
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-220 |
5.86e-30 |
|
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: 111.59 E-value: 5.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPD---SGEILLDEKPIagfSARQLARRLALLPQHHLSPEGITV 93
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 94 RELVSYgrSPWLSLwGRLSAEDNERVNVA---MSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLD 170
Cdd:cd03234 99 RETLTY--TAILRL-PRKSSDAIRKKRVEdvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556321685 171 INHQVELMRLMVELKRQGKTVVTVLH----DLnqaSRYCDHLVVLASGRVMAQG 220
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-227 |
9.95e-30 |
|
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: 116.39 E-value: 9.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLncfsRLLT----PDSGEILLDEKPIAGFSARQLA 75
Cdd:COG4618 330 RLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLLVgvwpPTAGSVRLDGADLSQWDREELG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RRLALLPQhhlSPE--GITVRELVSygrspwlslwgRLSAEDNERVnVAMSQtrtrnLAD-----RRLTQ---------- 138
Cdd:COG4618 406 RHIGYLPQ---DVElfDGTIAENIA-----------RFGDADPEKV-VAAAK-----LAGvhemiLRLPDgydtrigegg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 139 --LSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNqASRYCDHLVVLASGRV 216
Cdd:COG4618 466 arLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRV 544
|
250
....*....|.
gi 556321685 217 MAQGAPEAVMK 227
Cdd:COG4618 545 QAFGPRDEVLA 555
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-216 |
1.31e-29 |
|
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: 111.02 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSY---GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRL 78
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHHLSPEGiTVRELVSYGrspwlslwgrLSAEDNERVNVAMSQTRTRNL-----------ADRRLTQLSGGQRQRA 147
Cdd:cd03248 91 SLVGQEPVLFAR-SLQDNIAYG----------LQSCSFECVKEAAQKAHAHSFiselasgydteVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 148 FLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQgKTVVTVLHDLNQASRyCDHLVVLASGRV 216
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-217 |
2.03e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 110.94 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ--LARRLAL 80
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERgvVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHhlspegiTVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:PRK11248 82 LPWR-------NVQDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLA--SGRVM 217
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVV 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-220 |
2.64e-29 |
|
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: 109.69 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 28 GKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIagFSARQLA------RRLALLPQHH-LSPEgITVRELVSYG 100
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL--FDSRKKInlppqqRKIGLVFQQYaLFPH-LNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 101 rspwlsLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRL 180
Cdd:cd03297 100 ------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556321685 181 MVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03297 174 LKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-226 |
2.98e-29 |
|
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: 112.89 E-value: 2.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 22 SLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIagFSARQL------ARRLALLPQH-----HLSpeg 90
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGiflpphRRRIGYVFQEarlfpHLS--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 91 itVRELVSYGRSPwlsLWGRLSAEDNERVnVAMsqTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLD 170
Cdd:COG4148 94 --VRGNLLYGRKR---APRAERRISFDEV-VEL--LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 171 INHQVELMRLMVELKRQGKT-VVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVM 226
Cdd:COG4148 166 LARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-227 |
1.23e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.46 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQhhlSPE----GITV 93
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQ---NPDnqfvGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 94 RELVSYGrspwlsLWGRLSAEDN--ERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDI 171
Cdd:PRK13648 102 KYDVAFG------LENHAVPYDEmhRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 172 NHQVELMRLMVELKRQGK-TVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-206 |
1.81e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 108.72 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRL--LTPD---SGEILLDEKPI--AGFSARQLA 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RRLALLPQHHlSPEGITVRELVSYGrSPWLSLWGRLsaedNERVNVAMSQTRTRNLADRRLTQ----LSGGQRQRAFLAM 151
Cdd:PRK14243 91 RRIGMVFQKP-NPFPKSIYDNIAYG-ARINGYKGDM----DELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 152 VLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQgKTVVTVLHDLNQASRYCD 206
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-225 |
4.60e-28 |
|
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: 111.70 E-value: 4.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGA----QAVLDGLSLALPAGKITALLGPNGCGKS----TLLncfsRLLTPD----SGEILLDEKPIAGFS 70
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSIL----RLLPDPaahpSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 71 ARQLaRRL--------------ALLPQHhlspegiTVRELVSYGrspwLSLWGRLSAED-NERVNVAMSQTRTRNlADRR 135
Cdd:COG4172 83 EREL-RRIrgnriamifqepmtSLNPLH-------TIGKQIAEV----LRLHRGLSGAAaRARALELLERVGIPD-PERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 136 LT----QLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVV 210
Cdd:COG4172 150 LDayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAV 229
|
250
....*....|....*
gi 556321685 211 LASGRVMAQGAPEAV 225
Cdd:COG4172 230 MRQGEIVEQGPTAEL 244
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-225 |
5.55e-28 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 106.46 E-value: 5.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR-LALL 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQhhlspegitvrelvsyGRSpwlsLWGRLSAEDNERVNVAMSQTRTRNLAD--------------RRLTQLSGGQRQRA 147
Cdd:TIGR03410 81 PQ----------------GRE----IFPRLTVEENLLTGLAALPRRSRKIPDeiyelfpvlkemlgRRGGDLSGGQQQQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 148 FLAMVLAQDTPLILLDEPT------TYLDInHQVeLMRLMvelKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGA 221
Cdd:TIGR03410 141 AIARALVTRPKLLLLDEPTegiqpsIIKDI-GRV-IRRLR---AEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
....
gi 556321685 222 PEAV 225
Cdd:TIGR03410 216 GDEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-216 |
5.82e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 5.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKpiagfsarqLarRLALLP 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET---------V--KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHH--LSPEgITVRELVSYGrspwlslwgrlsAEDNERVNVamsqtrtRNL----------ADRRLTQLSGGQRQRAFLA 150
Cdd:COG0488 385 QHQeeLDPD-KTVLDELRDG------------APGGTEQEV-------RGYlgrflfsgddAFKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 151 MVLAQDTPLILLDEPTTYLDInhqvELMRLMVE-LKR-QGkTVVTVLHDlnqasRY-----CDHLVVLASGRV 216
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDI----ETLEALEEaLDDfPG-TVLLVSHD-----RYfldrvATRILEFEDGGV 507
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-225 |
7.30e-28 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 108.74 E-value: 7.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 33 LLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLPQHH-LSPEgITVRELVSYGrspwLSLWGRL 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYaLFPH-MTVEENVAFG----LKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 112 SAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDIN----HQVELMRLMVELkrq 187
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQEQL--- 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 556321685 188 GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-227 |
7.70e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.50 E-value: 7.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSY-GAQ-AVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDekpiaGFSARQLA---- 75
Cdd:TIGR03375 463 EIEFRNVSFAYpGQEtPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLD-----GVDIRQIDpadl 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 -RRLALLPQHHLSPEGiTVRELVSYGRspwlslwgrLSAEDNERVNVAMS---QTRTRNLA---DRRLTQ----LSGGQR 144
Cdd:TIGR03375 538 rRNIGYVPQDPRLFYG-TLRDNIALGA---------PYADDEEILRAAELagvTEFVRRHPdglDMQIGErgrsLSGGQR 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 145 QRAFLAMVLAQDTPLILLDEPTTYLDinHQVElMRLMVELKR--QGKTVVTVLHDLnQASRYCDHLVVLASGRVMAQGAP 222
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMD--NRSE-ERFKDRLKRwlAGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPK 683
|
....*
gi 556321685 223 EAVMK 227
Cdd:TIGR03375 684 DQVLE 688
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-226 |
1.03e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.82 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLdgLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLP 82
Cdd:PRK10771 2 LKLTDITWLYHHLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 Q-HHLSPEgITVRELVSYGRSPWLslwgRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:PRK10771 78 QeNNLFSH-LTVAQNIGLGLNPGL----KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKRQGK-TVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVM 226
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-226 |
1.09e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 106.59 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPI----------AGFSA 71
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 72 RQLA---RRLALLPQHHLSPEGITVRELVSygRSPwLSLWGRLSAEDNERVNVAMSQTRTRNLA-DRRLTQLSGGQRQRA 147
Cdd:PRK10619 85 NQLRllrTRLTMVFQHFNLWSHMTVLENVM--EAP-IQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 148 FLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVM 226
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
1.24e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.81 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY-GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALL 81
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHH----LSPegiTVRELVSYGRSPwlslWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDT 157
Cdd:PRK13652 84 FQNPddqiFSP---TVEQDIAFGPIN----LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 158 PLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV-MKPELLKTV 234
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARV 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-229 |
1.27e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.87 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEIlldekPIAG----FSARQLAR 76
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-----NIAGhqfdFSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 RLALL--------PQHHLSPEgITVRE-LVSygrSPwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRA 147
Cdd:COG4161 76 AIRLLrqkvgmvfQQYNLWPH-LTVMEnLIE---AP-CKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 148 FLAMVLAQDTPLILLDEPTTYLD--INHQVelMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDpeITAQV--VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF 228
|
....
gi 556321685 226 MKPE 229
Cdd:COG4161 229 TQPQ 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-229 |
1.85e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.08 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRL--LTPDS---GEILLDEKPIAG--FSARQLA 75
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGRNIYSpdVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RRLALLPQHHLSPEGITVRELVSYGrspwLSLWGRLSAED--NERVNVAMSQTRTRNLADRRL----TQLSGGQRQRAFL 149
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG----VKLNGLVKSKKelDERVEWALKKAALWDEVKDRLndypSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 150 AMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQgKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK-P 228
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEnP 239
|
.
gi 556321685 229 E 229
Cdd:PRK14267 240 E 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-235 |
2.23e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 105.36 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR-LAL 80
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQhhlspEGITVRELVSYGR-SPWLSLWGRLSAED-NERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTP 158
Cdd:PRK10895 83 LPQ-----EASIFRRLSVYDNlMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 159 LILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVF 235
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-249 |
2.55e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.45 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEIlldekPIAGF---------SARQLARRLALL---PQHH 85
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI-----TIAGYhitpetgnkNLKKLRKKVSLVfqfPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 86 LSPEgiTVRELVSYGRSpwlslwgRLSAEDNERVNVAMSQTR----TRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:PRK13641 98 LFEN--TVLKDVEFGPK-------NFGFSEDEAKEKALKWLKkvglSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK-PELLKTVFSveae 240
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSdKEWLKKHYL---- 244
|
....*....
gi 556321685 241 ihPEPVSGR 249
Cdd:PRK13641 245 --DEPATSR 251
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-220 |
3.70e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 106.70 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSY----GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQL--ARR-- 77
Cdd:COG1135 5 ENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraARRki 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 ------LALLPQHhlspegiTVRELVSYgrsPwLSLWGRLSAEDNERVN-----VAMSqtrtrNLADRRLTQLSGGQRQR 146
Cdd:COG1135 85 gmifqhFNLLSSR-------TVAENVAL---P-LEIAGVPKAEIRKRVAellelVGLS-----DKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 147 AFLAMVLAQDtPLILL-DEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:COG1135 149 VGIARALANN-PKVLLcDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-216 |
5.01e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.15 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA--RRL- 78
Cdd:PRK10419 12 HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafRRDi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ---------ALLPQHhlspegiTVRELVsygRSPWLSLWGRLSAEDNERVNVAMSQTRTR-NLADRRLTQLSGGQRQRAF 148
Cdd:PRK10419 92 qmvfqdsisAVNPRK-------TVREII---REPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 149 LAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTV-VTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-224 |
6.10e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 104.71 E-value: 6.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSG-----EILLDEKPIAGFSARQLARR 77
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELLGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 LA----LLPQHHLSPEgITVRELV---SYGRSP-WLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFL 149
Cdd:PRK09984 85 RAntgyIFQQFNLVNR-LSVLENVligALGSTPfWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 150 AMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEA 224
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-220 |
6.16e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 104.33 E-value: 6.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEIlldekPIAG----FSA----- 71
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----NIAGnhfdFSKtpsdk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 72 --RQLARRLALL-PQHHLSPEgITVRE-LVsygRSPwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRA 147
Cdd:PRK11124 76 aiRELRRNVGMVfQQYNLWPH-LTVQQnLI---EAP-CRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 148 FLAMVLAQDTPLILLDEPTTYLD--INHQVelMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDpeITAQI--VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-216 |
7.69e-27 |
|
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: 103.59 E-value: 7.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYG----AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA--- 75
Cdd:TIGR02211 2 LKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 -RRLALLPQ-HHLSPEgITVRELVSYgrsPwlSLWGRLSAEDNERVNVAM-SQTRTRNLADRRLTQLSGGQRQRAFLAMV 152
Cdd:TIGR02211 82 nKKLGFIYQfHHLLPD-FTALENVAM---P--LLIGKKSVKEAKERAYEMlEKVGLEHRINHRPSELSGGERQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKR-QGKTVVTVLHDLNQASRYcDHLVVLASGRV 216
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNReLNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-216 |
1.08e-26 |
|
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: 102.87 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQ-AVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA---RRLALL 81
Cdd:cd03292 4 INVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHHLSPEGITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFA----LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-220 |
1.41e-26 |
|
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: 102.67 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQ--AVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:cd03245 6 RNVSFSYPNQeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 HHLSPEGiTVRELVSYgrspwlslwGRLSAEDNERVNVAMSQTRTrNLADR-----------RLTQLSGGQRQRAFLAMV 152
Cdd:cd03245 86 DVTLFYG-TLRDNITL---------GAPLADDERILRAAELAGVT-DFVNKhpngldlqigeRGRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKRqGKTVVTVLH-----DLnqasryCDHLVVLASGRVMAQG 220
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHrpsllDL------VDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-232 |
1.70e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.33 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 16 AVLDgLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPI-AGFSARQLaRRLA-------LLPQHHLS 87
Cdd:PRK13634 22 ALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKL-KPLRkkvgivfQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 88 PEgiTVRELVSYGRSPWlslwgRLSAEDNERVNVAMSQT--RTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEP 165
Cdd:PRK13634 100 EE--TVEKDICFGPMNF-----GVSEEDAKQKAREMIELvgLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 166 TTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVM-KPELLK 232
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFaDPDELE 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
3.44e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.49 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAl 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 lPQHHLSPEgITVRELvsygrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:PRK13539 80 -HRNAMKPA-LTVAEN--------LEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLH 196
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-224 |
4.31e-26 |
|
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: 101.74 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA----VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARrl 78
Cdd:COG4181 9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 aLLPQH--------HLSPEgitvrelvsygrspwlslwgrLSAEDN-----ERVNVAMSQTRTRNLADR-----RLT--- 137
Cdd:COG4181 87 -LRARHvgfvfqsfQLLPT---------------------LTALENvmlplELAGRRDARARARALLERvglghRLDhyp 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 138 -QLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKR-QGKTVVTVLHDLNQASRyCDHLVVLASGR 215
Cdd:COG4181 145 aQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
....*....
gi 556321685 216 VMAQGAPEA 224
Cdd:COG4181 224 LVEDTAATA 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-219 |
5.16e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 102.19 E-value: 5.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIA---GFSARQLARRL 78
Cdd:TIGR02769 11 TYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldRKQRRAFRRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHhlSPEGI----TVRELVsygRSPWLSLWGRLSAEDNERVNVAMSQTRTR-NLADRRLTQLSGGQRQRAFLAMVL 153
Cdd:TIGR02769 91 QLVFQD--SPSAVnprmTVRQII---GEPLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 154 AQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTV-VTVLHDLNQASRYCDHLVVLASGRVMAQ 219
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-227 |
5.86e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 106.34 E-value: 5.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 15 QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQHHLSPEGiTVR 94
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 95 ELVSYGRSpwlslwgrlSAEDNERVNVA-----------MSQTRTRNLADRRlTQLSGGQRQRAFLAMVLAQDTPLILLD 163
Cdd:TIGR00958 573 ENIAYGLT---------DTPDEEIMAAAkaanahdfimeFPNGYDTEVGEKG-SQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 164 EPTTYLDINHQVELMRLMvelKRQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:TIGR00958 643 EATSALDAECEQLLQESR---SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-201 |
8.07e-26 |
|
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: 100.26 E-value: 8.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIaGFSARQLARRLALLP 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGITVRELvsygrspwLSLWGRLSaeDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:cd03231 80 HAPGIKTTLSVLEN--------LRFWHADH--SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556321685 163 DEPTTYLDINHQVELMRLMV-ELKRQGKTVVTVLHDLNQA 201
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAgHCARGGMVVLTTHQDLGLS 189
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-239 |
8.70e-26 |
|
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: 103.65 E-value: 8.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 21 LSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIagFSARQLA------RRLALLPQH-----HLSpe 89
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL--FDSRKGIflppekRRIGYVFQEarlfpHLS-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 90 gitVRELVSYGRspwlslWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYL 169
Cdd:TIGR02142 92 ---VRGNLRYGM------KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 170 DINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVEA 239
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQ 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-227 |
9.31e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.05 E-value: 9.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYG-----AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSA--RQ 73
Cdd:PRK13637 1 MSIKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 74 LARRLALL---PQHHLSPEgiTVRELVSYGRSpwlslwgRLSAEDNE---RVNVAMSQT--RTRNLADRRLTQLSGGQRQ 145
Cdd:PRK13637 81 IRKKVGLVfqyPEYQLFEE--TIEKDIAFGPI-------NLGLSEEEienRVKRAMNIVglDYEDYKDKSPFELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 146 RAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGK-TVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEA 224
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
...
gi 556321685 225 VMK 227
Cdd:PRK13637 232 VFK 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-206 |
9.53e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.39 E-value: 9.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRL--LTPD---SGEILLDEKPIagFSAR----Q 73
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNI--YSPRtdtvD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 74 LARRLALLPQHHlSPEGITVRELVSYGrspwLSLWG-RLSAEDNERVNVAMSQTRTRNLADRRLTQ----LSGGQRQRAF 148
Cdd:PRK14239 84 LRKEIGMVFQQP-NPFPMSIYENVVYG----LRLKGiKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 149 LAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQgKTVVTVLHDLNQASRYCD 206
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISD 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-234 |
1.40e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.42 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 15 QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGE---ILLDEKPIAGFSARQLARRLALLPQHhlsPE-- 89
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREKVGIVFQN---PDnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 90 --GITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTT 167
Cdd:PRK13640 97 fvGATVGDDVAFG----LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 168 YLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASrYCDHLVVLASGRVMAQGAPEAVM-KPELLKTV 234
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFsKVEMLKEI 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-216 |
1.94e-25 |
|
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: 98.66 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSygaqAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ-LARRLAL 80
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPqhhlspegitvrelvsygrspwlslwgrlsaEDNERVNVAMSQTRTRNLADRRLtqLSGGQRQRAFLAMVLAQDTPLI 160
Cdd:cd03215 80 VP-------------------------------EDRKREGLVLDLSVAENIALSSL--LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 161 LLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-225 |
2.16e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.45 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR-LALL 81
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHHLSPEGITVRE--LVSYGR---SPWLS------LWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLA 150
Cdd:PRK11300 86 FQHVRLFREMTVIEnlLVAQHQqlkTGLFSgllktpAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 151 MVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-215 |
2.41e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 103.84 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY-GAQAvLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ-LARRLAL 80
Cdd:PRK11288 5 LSFDGIGKTFpGVKA-LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQH-HLSPEgITVRELVSYGRSPwlSLWGRLsaedNERVNVAMSQTRTRNLA-----DRRLTQLSGGQRQRAFLAMVLA 154
Cdd:PRK11288 84 IYQElHLVPE-MTVAENLYLGQLP--HKGGIV----NRRLLNYEAREQLEHLGvdidpDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 155 QDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGR 215
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-220 |
3.14e-25 |
|
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: 99.71 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEI-LLDEKPiagFSAR-QLARRLALLpqhhlspegitvr 94
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVP---WKRRkKFLRRIGVV------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 95 elvsYGRSPwlSLWGRLSAEDNERVNVAM-------SQTRTRNLA---------DRRLTQLSGGQRQRAFLAMVLAQDTP 158
Cdd:cd03267 100 ----FGQKT--QLWWDLPVIDSFYLLAAIydlpparFKKRLDELSelldleellDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 159 LILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
10-225 |
3.78e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 10 VSYGAQA-------VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSA----RQLARRL 78
Cdd:PRK13649 8 VSYTYQAgtpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALL---PQHHLSPEgiTVRELVSYGRSPWlslwgRLSAEDNERVN------VAMSQtrtrNLADRRLTQLSGGQRQRAFL 149
Cdd:PRK13649 88 GLVfqfPESQLFEE--TVLKDVAFGPQNF-----GVSQEEAEALAreklalVGISE----SLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 150 AMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-201 |
3.84e-25 |
|
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: 98.20 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGfSARQLARRLALLP 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 -QHHLSPEgITVRELvsygrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:TIGR01189 80 hLPGLKPE-LSALEN--------LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556321685 162 LDEPTTYLDINHQVELMRLMVE-LKRQGKTVVTVLHDLNQA 201
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLV 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-252 |
4.00e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.08 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIaGFSARQLarrLALLP 82
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGL---LALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHL---SPEGITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPL 159
Cdd:PRK13638 78 QVATvfqDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 160 ILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAP-EAVMKPELLKTVFSVE 238
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPgEVFACTEAMEQAGLTQ 237
|
250
....*....|....*..
gi 556321685 239 ---AEIHPEpvSGRPMC 252
Cdd:PRK13638 238 pwlVKLHTQ--LGLPLC 252
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-222 |
7.19e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 101.26 E-value: 7.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEK-----PIAGFSARQLARRLALL 81
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PqhHLSpegitVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:PRK11000 88 P--HLS-----VAENMSFG----LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 162 LDEPTTYLD----INHQVELMRLMvelKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAP 222
Cdd:PRK11000 157 LDEPLSNLDaalrVQMRIEISRLH---KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-240 |
1.91e-24 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 97.88 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILldekpiagfsaRQLARRLALLPQH- 84
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQKl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 HLSPE-GITVrelvsygrSPWLSLWGRLSAEDnerVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLD 163
Cdd:PRK09544 77 YLDTTlPLTV--------NRFLRLRPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 164 EPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLaSGRVMAQGAPEAV-MKPELLKTVFSVEAE 240
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVsLHPEFISMFGPRGAE 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-224 |
2.89e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.40 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPD---SGEILLDEKPIAGFSARQlaRRLA 79
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQ--RRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLspegitvreLVsygrsPWLSLWGRLS---------AEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLA 150
Cdd:COG4136 80 ILFQDDL---------LF-----PHLSVGENLAfalpptigrAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 151 MVLAQDTPLILLDEPTTYLDINHQVElMRLMV--ELKRQGKTVVTVLHDLNQAsrycdhlvvLASGRVMAQGAPEA 224
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALRAQ-FREFVfeQIRQRGIPALLVTHDEEDA---------PAAGRVLDLGNWQH 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
15-226 |
2.90e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.04 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 15 QAVlDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA---RRLALL---PQHHLSP 88
Cdd:COG4608 32 KAV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVfqdPYASLNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 89 EgITVRELVSYGrspwLSLWGRLSAED-NERVNVAMSQTRTR-NLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPT 166
Cdd:COG4608 111 R-MTVGDIIAEP----LRIHGLASKAErRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 167 TYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNqASRY-CDHLVVLASGRVMAQGAPEAVM 226
Cdd:COG4608 186 SALDVSIQAQVLNLLEDLQDElGLTYLFISHDLS-VVRHiSDRVAVMYLGKIVEIAPRDELY 246
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-215 |
7.24e-24 |
|
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: 93.28 E-value: 7.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFsarqlarrlallpqhh 85
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGY---------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 86 lspegitvrelvsygrspwlslwgrlsaednervnvamsqtrtrnladrrLTQLSGGQRQRAFLAMVLAQDTPLILLDEP 165
Cdd:cd03221 68 --------------------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556321685 166 TTYLDINHQVELMRLMVELKRqgkTVVTVLHD---LNQAsryCDHLVVLASGR 215
Cdd:cd03221 98 TNHLDLESIEALEEALKEYPG---TVILVSHDryfLDQV---ATKIIELEDGK 144
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-222 |
7.94e-24 |
|
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: 95.25 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:cd03244 6 KNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 HHLSPEGiTVRE-LVSYGRSPWLSLWGRLsaednERVNVAMSQTRTRNLADRRLT----QLSGGQRQRAFLAMVLAQDTP 158
Cdd:cd03244 86 DPVLFSG-TIRSnLDPFGEYSDEELWQAL-----ERVGLKEFVESLPGGLDTVVEeggeNLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 159 LILLDEPTTYLDinhqVELMRLMVELKRQ---GKTVVTVLHDLNqASRYCDHLVVLASGRVMAQGAP 222
Cdd:cd03244 160 ILVLDEATASVD----PETDALIQKTIREafkDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-220 |
1.19e-23 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 99.43 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQA--VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLA 79
Cdd:TIGR01846 455 AITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLSPEGiTVRELVSYGRSpwlslwgrlsAEDNERVNVA----------MSQTRTRN-LADRRLTQLSGGQRQRAF 148
Cdd:TIGR01846 535 VVLQENVLFSR-SIRDNIALCNP----------GAPFEHVIHAaklagahdfiSELPQGYNtEVGEKGANLSGGQRQRIA 603
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 149 LAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRqGKTVVTVLHDLNqASRYCDHLVVLASGRVMAQG 220
Cdd:TIGR01846 604 IARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESG 673
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-225 |
1.47e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.99 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQL--AR-RLALLPQ 83
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRkRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 HHLSPEGITVRELVSYgrsPwLSLWGRLSAED-NERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:PRK11831 92 SGALFTDMNVFDNVAY---P-LREHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 163 DEPTTYLD-INHQVeLMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK11831 168 DEPFVGQDpITMGV-LVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-226 |
1.79e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.80 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 22 SLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQL----ARRLALLPQHHLSPEGITVRELV 97
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 98 SYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVEL 177
Cdd:PRK10070 128 AFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556321685 178 MRLMVELK-RQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVM 226
Cdd:PRK10070 204 QDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-227 |
3.07e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEK---PI---AGFsarqlarrlallpqhhlSPEg 90
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLLelgAGF-----------------HPE- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 91 ITVRELV-SYGRspwlsLWGRLSAEDNERVN--VAMSQtrtrnL---ADRRLTQLSGGQRQR-AFlAMVLAQDTPLILLD 163
Cdd:COG1134 103 LTGRENIyLNGR-----LLGLSRKEIDEKFDeiVEFAE-----LgdfIDQPVKTYSSGMRARlAF-AVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 164 EPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:COG1134 172 EVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-206 |
3.11e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.72 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRlLTPDSGEILLDEKpIAGFSARQLARRLAL-- 80
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGR-VEFFNQNIYERRVNLnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 --------LPQHHLSPegITVRELVSYGRSpwLSLWgRLSAEDNERVNVAMSQT----RTRNLADRRLTQLSGGQRQRAF 148
Cdd:PRK14258 86 lrrqvsmvHPKPNLFP--MSVYDNVAYGVK--IVGW-RPKLEIDDIVESALKDAdlwdEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 149 LAMVLAQDTPLILLDEPTTYLD------INHQVELMRLMVELkrqgkTVVTVLHDLNQASRYCD 206
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDpiasmkVESLIQSLRLRSEL-----TMVIVSHNLHQVSRLSD 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-243 |
3.32e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.46 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQA-----VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGE-ILLDEKPIAGF----SARQLA 75
Cdd:PRK13645 10 DNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtIVGDYAIPANLkkikEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RRLALL---PQHHLSPEgiTVRELVSYGRspwLSLwgrlsAEDNERVNVAMSQ-----TRTRNLADRRLTQLSGGQRQRA 147
Cdd:PRK13645 90 KEIGLVfqfPEYQLFQE--TIEKDIAFGP---VNL-----GENKQEAYKKVPEllklvQLPEDYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 148 FLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAP-EAV 225
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPfEIF 239
|
250
....*....|....*...
gi 556321685 226 MKPELLKTVfsveaEIHP 243
Cdd:PRK13645 240 SNQELLTKI-----EIDP 252
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-233 |
3.64e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.69 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA-----VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDE-------------- 63
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 64 ----KPIAGFsaRQLARRLALL---PQHHLSPEgiTVRELVSYGrsPwlslwgrlsaednerVNVAMSQTRTRNLA---- 132
Cdd:PRK13631 102 npysKKIKNF--KELRRRVSMVfqfPEYQLFKD--TIEKDIMFG--P---------------VALGVKKSEAKKLAkfyl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 133 ----------DRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQAS 202
Cdd:PRK13631 161 nkmglddsylERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL 240
|
250 260 270
....*....|....*....|....*....|..
gi 556321685 203 RYCDHLVVLASGRVMAQGAP-EAVMKPELLKT 233
Cdd:PRK13631 241 EVADEVIVMDKGKILKTGTPyEIFTDQHIINS 272
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-234 |
4.28e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY--GAQAvLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRL-A 79
Cdd:PRK13644 2 IRLENVSYSYpdGTPA-LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQhhlSPE----GITVRELVSYGRSPwLSLwgrLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQ 155
Cdd:PRK13644 81 IVFQ---NPEtqfvGRTVEEDLAFGPEN-LCL---PPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 156 DTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQAsRYCDHLVVLASGRVMAQGAPEAVMKPELLKTV 234
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
12-227 |
4.29e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 4.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 12 YGAQAVLDgLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ----LARRLALL---PQH 84
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVfqfPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 HLSPEgiTVRELVSYGRSPWlslwgRLSAEDNERVNVAMSQT--RTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:PRK13643 96 QLFEE--TVLKDVAFGPQNF-----GIPKEKAEKIAAEKLEMvgLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 163 DEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:PRK13643 169 DEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-225 |
6.61e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 94.00 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVsYGAQAVLDGLSLALPAGKITALLGPNGCGKStlLNCFSRL------LTPDSGEILLDEKPIAGFSARqlA 75
Cdd:PRK10418 4 QIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALgilpagVRQTAGRVLLDGKPVAPCALR--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RRLALL---PQHHLSPegitVRELVSYGRSPWLSLwGRLSAEDnervnVAMSQTRTRNLADRRLT------QLSGGQRQR 146
Cdd:PRK10418 79 RKIATImqnPRSAFNP----LHTMHTHARETCLAL-GKPADDA-----TLTAALEAVGLENAARVlklypfEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 147 AFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKR-QGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-227 |
1.07e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.08 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSA----RQLARRLALL---PQHHLSPEG 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRPVRKRIGMVfqfPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 91 ITvRELVsYGRSpwlSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLD 170
Cdd:PRK13646 103 VE-REII-FGPK---NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 171 INHQVELMRLMVELK-RQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-227 |
1.13e-22 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 96.55 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQA--VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLA 79
Cdd:TIGR03796 477 YVELRNITFGYSPLEppLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLSPEGiTVRELvsygrspwLSLWGR-LSAEDNERV-------NVAMSqtRTRNLaDRRLTQ----LSGGQRQRA 147
Cdd:TIGR03796 557 MVDQDIFLFEG-TVRDN--------LTLWDPtIPDADLVRAckdaaihDVITS--RPGGY-DAELAEgganLSGGQRQRL 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 148 FLAMVLAQDTPLILLDEPTTYLDInhQVELmRLMVELKRQGKTVVTVLHDLNqASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:TIGR03796 625 EIARALVRNPSILILDEATSALDP--ETEK-IIDDNLRRRGCTCIIVAHRLS-TIRDCDEIIVLERGKVVQRGTHEELWA 700
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-222 |
1.22e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.62 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA---VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLA 79
Cdd:PRK13642 5 LEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQhhlSPE----GITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQ 155
Cdd:PRK13642 85 MVFQ---NPDnqfvGATVEDDVAFG----MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 156 DTPLILLDEPTTYLDINHQVELMRLMVELK-RQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAP 222
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-226 |
1.29e-22 |
|
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: 96.29 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY-----------GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLtPDSGEILLDEKPIAGFSA 71
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 72 RQLaRRL-------------ALLPQHhlspegiTVRELVSYGrspwLSLWGR-LSAED-NERVNVAMSQTR-TRNLADRR 135
Cdd:COG4172 355 RAL-RPLrrrmqvvfqdpfgSLSPRM-------TVGQIIAEG----LRVHGPgLSAAErRARVAEALEEVGlDPAARHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 136 LTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLnQASRY-CDHLVVLAS 213
Cdd:COG4172 423 PHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDL-AVVRAlAHRVMVMKD 501
|
250
....*....|...
gi 556321685 214 GRVMAQGAPEAVM 226
Cdd:COG4172 502 GKVVEQGPTEQVF 514
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-216 |
2.94e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQhhlSP-----EGI 91
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQ---DPmmgtaPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 92 TVRE--LVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRtRNLADrRLTQ----LSGGQRQRAFLAMVLAQDTPLILLDEP 165
Cdd:COG1101 98 TIEEnlALAYRRGKRRGLRRGLTKKRRELFRELLATLG-LGLEN-RLDTkvglLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556321685 166 TTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:COG1101 176 TAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-223 |
4.03e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPD---SGEILLDEKPIagfSARQLARRLALLPQHHLSPEGITVR 94
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 95 ELVSYgrSPWLSLWGRLSA-EDNERVNVAMSQTRTRNLADRRLTQ------LSGGQRQRAFLAMVLAQDTPLILLDEPTT 167
Cdd:TIGR00955 118 EHLMF--QAHLRMPRRVTKkEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 168 YLDINHQVELMRLMVELKRQGKTVVTVLHdlnQASR--YC--DHLVVLASGRVMAQGAPE 223
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIH---QPSSelFElfDKIILMAEGRVAYLGSPD 252
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-225 |
5.25e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.35 E-value: 5.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPI-AGFSARQLARRLALLPQH 84
Cdd:PRK11264 7 KNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIRQLRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 --------HLSPEGiTVRELVSYGrsPwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQD 156
Cdd:PRK11264 87 vgfvfqnfNLFPHR-TVLENIIEG--P-VIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 157 TPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
5-198 |
6.59e-22 |
|
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: 91.27 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 5 TENLTVSYGAQA-VLDGLSLALPaGKITALLGPNGCGKSTLLNCFSRLLTPDSGEilLDEKP-----IAGFSARQLARRL 78
Cdd:cd03236 3 EDEPVHRYGPNSfKLHRLPVPRE-GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRGSELQNYF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALL----------PQH-HLSPEGI--TVRELVSygrspwlslwgrlSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQ 145
Cdd:cd03236 80 TKLlegdvkvivkPQYvDLIPKAVkgKVGELLK-------------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556321685 146 RAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDL 198
Cdd:cd03236 147 RVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-215 |
9.10e-22 |
|
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: 90.19 E-value: 9.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEK----PIAGFSARQLarrLALLpqhhlspegit 92
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREI---LALR----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 93 vRELVSYgRSPWLSLWGRLSAED------NER-VNVAMSQTRTRNLADR-----RLTQL-----SGGQRQRAFLAMVLAQ 155
Cdd:COG4778 92 -RRTIGY-VSQFLRVIPRVSALDvvaeplLERgVDREEARARARELLARlnlpeRLWDLppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 156 DTPLILLDEPTTYLD-INHQVeLMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGR 215
Cdd:COG4778 170 DPPLLLLDEPTASLDaANRAV-VVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-222 |
1.89e-21 |
|
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: 93.54 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 12 YGAQAVlDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGfSARQLARRLALLPQHHLSPEGI 91
Cdd:TIGR01257 941 SGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 92 TVRELVSYgrspWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDI 171
Cdd:TIGR01257 1019 TVAEHILF----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556321685 172 NHQVELMRLMVELkRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAP 222
Cdd:TIGR01257 1095 YSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-220 |
2.08e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 92.88 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA-VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALL 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHHLSPEGiTVRELVSYGRSPWLS---LWGRLS-AEDNERVNvAMSQTRTRNLADRRlTQLSGGQRQRAFLAMVLAQDT 157
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKENVSqdeIWAACEiAEIKDDIE-NMPLGYQTELSEEG-SSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 158 PLILLDEPTTYLDINHQVELMRLMVELkrQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQG 220
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQG 690
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-203 |
2.11e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.49 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA----RRLALLPQ-HHLSPEgI 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQfHHLLPD-F 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 92 TVRELVSYgrsPWLsLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDI 171
Cdd:PRK11629 103 TALENVAM---PLL-IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190
....*....|....*....|....*....|...
gi 556321685 172 NHQVELMRLMVEL-KRQGKTVVTVLHDLNQASR 203
Cdd:PRK11629 179 RNADSIFQLLGELnRLQGTAFLVVTHDLQLAKR 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-216 |
2.18e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.74 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAgfSAR-------QLA 75
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA--EARedtrlmfQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RrlaLLPQHhlspegiTVRELVSYGrspwlsLWGRLSAEdnervnvAMSQTRTRNLADRRL---TQLSGGQRQRAFLAMV 152
Cdd:PRK11247 91 R---LLPWK-------KVIDNVGLG------LKGQWRDA-------ALQALAAVGLADRANewpAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-220 |
4.26e-21 |
|
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: 88.36 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 11 SYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSArqlarrlallpQHHLSPEg 90
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL-----------GGGFNPE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 91 ITVRELVSYGrspwLSLWGRLSAEDNERVN--VAMSQtrtrnL---ADRRLTQLSGGQRQR-AFlAMVLAQDTPLILLDE 164
Cdd:cd03220 99 LTGRENIYLN----GRLLGLSRKEIDEKIDeiIEFSE-----LgdfIDLPVKTYSSGMKARlAF-AIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 165 PTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-198 |
4.95e-21 |
|
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: 91.77 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 25 LPA---GKITALLGPNGCGKSTLLNCFSRLLTPDSGEIllDEKP-----IAGFSARQLAR----------RLALLPQH-H 85
Cdd:COG1245 93 LPVpkkGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEPswdevLKRFRGTELQDyfkklangeiKVAHKPQYvD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 86 LSPEGI--TVRELvsygrspwlslwgrLSAEDnERVNV--AMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:COG1245 171 LIPKVFkgTVREL--------------LEKVD-ERGKLdeLAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*..
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDL 198
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
7-225 |
1.10e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.25 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSYGA---QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:PRK13650 9 NLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 hhlSPE----GITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPL 159
Cdd:PRK13650 89 ---NPDnqfvGATVEDDVAFG----LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 160 ILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASrYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-214 |
1.16e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 87.14 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAgfsarqlarrlallpqhHLSPEGITVRElv 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-----------------EPGPDRMVVFQ-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 98 SYGRSPWLSLWGRLSAEDNeRVNVAMSQTRTRNL-------------ADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDE 164
Cdd:TIGR01184 62 NYSLLPWLTVRENIALAVD-RVLPDLSKSERRAIveehialvglteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556321685 165 PTTYLDI----NHQVELMRLMVElkrQGKTVVTVLHDLNQASRYCDHLVVLASG 214
Cdd:TIGR01184 141 PFGALDAltrgNLQEELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-240 |
1.21e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVsygaQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ-LARRLAL 80
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSpEGI----TVRELVSYGRSPWLSLWGRLS-AEDNERVNVAMSQ--TRTRNLaDRRLTQLSGGQRQRAFLAMVL 153
Cdd:COG1129 332 VPEDRKG-EGLvldlSIRENITLASLDRLSRGGLLDrRRERALAEEYIKRlrIKTPSP-EQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 154 AQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKT 233
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAIMAA 489
|
....*..
gi 556321685 234 VFSVEAE 240
Cdd:COG1129 490 ATGGAAA 496
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-210 |
1.90e-20 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 87.08 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKIT-----ALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAgfsarqlarrlaLLPQHHLSPEGIT 92
Cdd:cd03237 10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------------YKPQYIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 93 VRELvsygrspwlslwgrLSAEDNERVNVAMSQTRTRN------LADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPT 166
Cdd:cd03237 78 VRDL--------------LSSITKDFYTHPYFKTEIAKplqieqILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556321685 167 TYLDinhqVElMRLMVE--LKR----QGKTVVTVLHDLNQASRYCDHLVV 210
Cdd:cd03237 144 AYLD----VE-QRLMASkvIRRfaenNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-220 |
2.42e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 89.69 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGA--QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:PRK11176 345 RNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 H-HLSPEgiTVRELVSYGRSpwlslwGRLSAEDNERVNVAMSQTRTRNLADRRL--------TQLSGGQRQRAFLAMVLA 154
Cdd:PRK11176 425 NvHLFND--TIANNIAYART------EQYSREQIEEAARMAYAMDFINKMDNGLdtvigengVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 155 QDTPLILLDEPTTYLDINHQVELMRLMVELKRQgKTVVTVLHDLNQASRyCDHLVVLASGRVMAQG 220
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-203 |
2.73e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.78 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY----GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLAR-- 76
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 ---------RLALLPqhHLSPEGITVRELVSYGrspwlslwgrlsAEDNERVNVAMSQTRTRNLADR---RLTQLSGGQR 144
Cdd:PRK10535 85 rehfgfifqRYHLLS--HLTAAQNVEVPAVYAG------------LERKQRLLRAQELLQRLGLEDRveyQPSQLSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 145 QRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHD---LNQASR 203
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDpqvAAQAER 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-223 |
3.04e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.07 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTP-----DSGEILLDEKPIAGF-SARQLARRLAL 80
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHlSPEGITVRELVSYGRS-----PWLSLWGRLSAEDNErvnVAMSQTRTRNLADRRLtQLSGGQRQRAFLAMVLAQ 155
Cdd:PRK14271 106 LFQRP-NPFPMSIMDNVLAGVRahklvPRKEFRGVAQARLTE---VGLWDAVKDRLSDSPF-RLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 156 DTPLILLDEPTTYLDINHQVELMRLMVELKRQgKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPE 223
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTE 247
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-227 |
3.79e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 88.94 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLncfsRLLT----PDSGEILLDEKPIAGFSARQLA 75
Cdd:TIGR01842 316 HLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLA----RLIVgiwpPTSGSVRLDGADLKQWDRETFG 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 76 RRLALLPQHHLSPEGiTVRELVS-YGRSPwlslwgrlsaeDNERVNVA------------MSQTRTRNLADRRLTqLSGG 142
Cdd:TIGR01842 392 KHIGYLPQDVELFPG-TVAENIArFGENA-----------DPEKIIEAaklagvhelilrLPDGYDTVIGPGGAT-LSGG 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 143 QRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHD---LNQAsrycDHLVVLASGRVMAQ 219
Cdd:TIGR01842 459 QRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRpslLGCV----DKILVLQDGRIARF 534
|
....*...
gi 556321685 220 GAPEAVMK 227
Cdd:TIGR01842 535 GERDEVLA 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-232 |
4.06e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKpiagfSARQLARRLA--- 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI-----NYNKLDHKLAaql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 ---LLPQHHLSPEGITVRELVSYGRSPWLSLWGRLSAEDNE-RVNVAMSQTRT---RNLaDRRLTQLSGGQRQRAFLAMV 152
Cdd:PRK09700 81 gigIIYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREmRVRAAMMLLRVglkVDL-DEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 153 LAQDTPLILLDEPTTYLdINHQVE-LMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELL 231
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSL-TNKEVDyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
|
.
gi 556321685 232 K 232
Cdd:PRK09700 239 R 239
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-242 |
4.07e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.45 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 15 QAVlDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILldekpIAGFSARQlaRRLALLPQhhlspegITVr 94
Cdd:COG4586 36 EAV-DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR-----VLGYVPFK--RRKEFARR-------IGV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 95 elVSYGRSpwlSLWGRLSAEDNERVNVAM-----SQTRTR-----------NLADRRLTQLSGGQRQRAFLAMVLAQDTP 158
Cdd:COG4586 100 --VFGQRS---QLWWDLPAIDSFRLLKAIyripdAEYKKRldelvelldlgELLDTPVRQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 159 LILLDEPTTYLDINHQVELMRLMVELKRQGKTvvTVL---HDLNQASRYCDHLVVLASGRVMAQGAPEAvmkpelLKTVF 235
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGT--TILltsHDMDDIEALCDRVIVIDHGRIIYDGSLEE------LKERF 246
|
....*..
gi 556321685 236 SVEAEIH 242
Cdd:COG4586 247 GPYKTIV 253
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-221 |
4.26e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.55 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQL--ARR-LALLPQHH--LSPEgiT 92
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkARRqIGMIFQHFnlLSSR--T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 93 VRELVSYgrsPwLSLWGRLSAEDNERVN-----VAMSqtrtrNLADRRLTQLSGGQRQRAFLAMVLAQDtPLILL-DEPT 166
Cdd:PRK11153 99 VFDNVAL---P-LELAGTPKAEIKARVTellelVGLS-----DKADRYPAQLSGGQKQRVAIARALASN-PKVLLcDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 167 TYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGA 221
Cdd:PRK11153 169 SALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-220 |
4.50e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.13 E-value: 4.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEK-----PIAGFSARQLaRR 77
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAER-RR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 LA-----LLPQHHLspEGItvRELVS----------------YGR-----SPWLslwgrlsaednERVNVAMSQTrtrnl 131
Cdd:PRK11701 86 LLrtewgFVHQHPR--DGL--RMQVSaggnigerlmavgarhYGDirataGDWL-----------ERVEIDAARI----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 132 aDRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVV 210
Cdd:PRK11701 146 -DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLV 224
|
250
....*....|
gi 556321685 211 LASGRVMAQG 220
Cdd:PRK11701 225 MKQGRVVESG 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-225 |
4.67e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 4.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY-----------GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLtPDSGEILLDEKPIAGFSA 71
Cdd:PRK15134 276 LDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 72 RQL---ARRLALL---PQHHLSPEgITVRELVSYG---RSPWLSlwgrlSAEDNERVNVAMSQT----RTRNladRRLTQ 138
Cdd:PRK15134 355 RQLlpvRHRIQVVfqdPNSSLNPR-LNVLQIIEEGlrvHQPTLS-----AAQREQQVIAVMEEVgldpETRH---RYPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 139 LSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGK-TVVTVLHDLNQASRYCDHLVVLASGRVM 217
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
....*...
gi 556321685 218 AQGAPEAV 225
Cdd:PRK15134 506 EQGDCERV 513
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-222 |
8.57e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 84.39 E-value: 8.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQ--AVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLA 79
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLSPEGiTVR-ELVSYGRspwlslwgrlsaEDNERVNVAMSQTRTRNladrrltQLSGGQRQRAFLAMVLAQDTP 158
Cdd:cd03369 86 IIPQDPTLFSG-TIRsNLDPFDE------------YSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 159 LILLDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAP 222
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-223 |
1.28e-19 |
|
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: 83.73 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNC---FSRlLTPDSGEILLDEKPIAGFSARQLARR-L 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTimgHPK-YEVTEGEILFKGEDITDLPPEERARLgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHHLSPEGITVRELVSYgrspwlslwgrlsaednerVNVAmsqtrtrnladrrltqLSGGQRQRAFLAMVLAQDTP 158
Cdd:cd03217 80 FLAFQYPPEIPGVKNADFLRY-------------------VNEG----------------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 159 LILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLH-----DLNQAsrycDHLVVLASGRVMAQGAPE 223
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyqrllDYIKP----DRVHVLYDGRIVKSGDKE 190
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-225 |
1.51e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 85.79 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLlncfSRLLT----PDSGEILLDEKPIAGFS--ARQLARRLALL----PQHHLS 87
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL----ARLLTmietPTGGELYYQGQDLLKADpeAQKLLRQKIQIvfqnPYGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 88 PegitvRELVSYGRSPWLSLWGRLS-AEDNERVNVAMSQTRTR-NLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEP 165
Cdd:PRK11308 107 P-----RKKVGQILEEPLLINTSLSaAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 166 TTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-202 |
1.70e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.31 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAgfSAR-QLARRLALL 81
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--RQRdEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 pqHHLSpeGITvRELvsygrSPW--LSLWGRLSAE-DNERVNVAMSQTrtrNLADRRLT---QLSGGQRQRAFLAMVLAQ 155
Cdd:PRK13538 80 --GHQP--GIK-TEL-----TALenLRFYQRLHGPgDDEALWEALAQV---GLAGFEDVpvrQLSAGQQRRVALARLWLT 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556321685 156 DTPLILLDEPTTYLDINHQVELMRLMVE-LKRQGKTVVTVLHDLNQAS 202
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTHQDLPVAS 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-225 |
2.26e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTV-SYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR-LA 79
Cdd:COG3845 257 VLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLP---QHH-LSPEgITVRE--LVSYGRSPWLSLWGRLS---AEDN-----ERVNVamsqtRTRNlADRRLTQLSGGQRQ 145
Cdd:COG3845 337 YIPedrLGRgLVPD-MSVAEnlILGRYRRPPFSRGGFLDrkaIRAFaeeliEEFDV-----RTPG-PDTPARSLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 146 RAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-223 |
2.99e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.58 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLlncfSRLL------TPDSGEILLDEKPIAGFSARQLAR 76
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTL----AKVLmghpkyEVTSGSILLDGEDILELSPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 R-LALLPQHHLSPEGITVRELV--SYG--RSPWLSLwgrlsAEDNERVNVAMSQTR-TRNLADRRLTQ-LSGGQRQRAFL 149
Cdd:COG0396 77 AgIFLAFQYPVEIPGVSVSNFLrtALNarRGEELSA-----REFLKLLKEKMKELGlDEDFLDRYVNEgFSGGEKKRNEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 150 AMVLAQDTPLILLDEPTTYLDInhqvELMRLMVE----LKRQGKTVVTVLH-----DLNQAsrycDHLVVLASGRVMAQG 220
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDI----DALRIVAEgvnkLRSPDRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSG 223
|
...
gi 556321685 221 APE 223
Cdd:COG0396 224 GKE 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-225 |
3.10e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.28 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSY-GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQlaRRLALLPQHH 85
Cdd:PRK11650 8 AVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 86 -LSPEgITVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRafLAM--VLAQDTPLILL 162
Cdd:PRK11650 86 aLYPH-MSVRENMAYG----LKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQR--VAMgrAIVREPAVFLF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 163 DEPTTYLDINHQVElMRLmvELK----RQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK11650 159 DEPLSNLDAKLRVQ-MRL--EIQrlhrRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-172 |
3.44e-19 |
|
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: 86.14 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEkpiagfsARQLA----RRL 78
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-------TVKLAyvdqSRD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHhlspegiTVRELVSYGrspwlslwgrlsaedNERVNVAMSQTRTRNLADR----------RLTQLSGGQRQRAF 148
Cdd:TIGR03719 396 ALDPNK-------TVWEEISGG---------------LDIIKLGKREIPSRAYVGRfnfkgsdqqkKVGQLSGGERNRVH 453
|
170 180
....*....|....*....|....
gi 556321685 149 LAMVLAQDTPLILLDEPTTYLDIN 172
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-198 |
3.58e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 86.40 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 25 LPA---GKITALLGPNGCGKSTLLNCFSRLLTPDSGEilLDEKP-----IAGFSARQLAR----------RLALLPQH-H 85
Cdd:PRK13409 93 LPIpkeGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPswdevLKRFRGTELQNyfkklyngeiKVVHKPQYvD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 86 LSPEGI--TVRELVSygrspwlslwgrlSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLD 163
Cdd:PRK13409 171 LIPKVFkgKVRELLK-------------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*
gi 556321685 164 EPTTYLDINHQVELMRLMVELKrQGKTVVTVLHDL 198
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDL 271
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-215 |
6.81e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 85.37 E-value: 6.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLtPD---SGEILLDEKPIAGFSARQLARR-- 77
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAgi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 ------LALLPQhhLS-PEGITV-RELVSYGRSPWLSLWGRlSAEDNERVNVAMSqtrtrnlADRRLTQLSGGQRQRAFL 149
Cdd:PRK13549 85 aiihqeLALVKE--LSvLENIFLgNEITPGGIMDYDAMYLR-AQKLLAQLKLDIN-------PATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 150 AMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGR 215
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-225 |
8.00e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.79 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 15 QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTP-DS-----GEILLDEKPIAGFSARQLARRLALLPQHHLSP 88
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSkikvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 89 EGITVRELVSYgrsPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRL----TQLSGGQRQRAFLAMVLAQDTPLILLDE 164
Cdd:PRK14246 103 PHLSIYDNIAY---PLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspaSQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 165 PTTYLDINHQVELMRLMVELKRQgKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-220 |
8.30e-19 |
|
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: 82.53 E-value: 8.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQA--VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:cd03252 4 EHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 HHLSPEGiTVRELVSYGRSpwlslwgrlsAEDNERV----NVAMSQTRTRNLAD-------RRLTQLSGGQRQRAFLAMV 152
Cdd:cd03252 84 ENVLFNR-SIRDNIALADP----------GMSMERVieaaKLAGAHDFISELPEgydtivgEQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKrQGKTVVTVLHDLNqASRYCDHLVVLASGRVMAQG 220
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQG 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-243 |
9.14e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.60 E-value: 9.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQA-----VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEI---LLDEKPIAGFS-- 70
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 71 -------------------ARQLARRLALLPQ---HHLSPEgiTVRE-----LVSYGRSPwlslwgrlsAEDNERVN--- 120
Cdd:PRK13651 81 ekvleklviqktrfkkikkIKEIRRRVGVVFQfaeYQLFEQ--TIEKdiifgPVSMGVSK---------EEAKKRAAkyi 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 121 --VAMSQtrtrNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDL 198
Cdd:PRK13651 150 elVGLDE----SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 556321685 199 NQASRYCDHLVVLASGRVMAQGAPEAVMKpellKTVFSVEAEIHP 243
Cdd:PRK13651 226 DNVLEWTKRTIFFKDGKIIKDGDTYDILS----DNKFLIENNMEP 266
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-221 |
1.04e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.67 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 13 GAQAvLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIA--GFSARQLA------RRLALLPQh 84
Cdd:PRK10762 16 GVKA-LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEAgigiihQELNLIPQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 hlspegITVRELVSYGR---SPWLSL-WGRLSAEDNE---RVNVAMSqtrtrnlADRRLTQLSGGQRQRAFLAMVLAQDT 157
Cdd:PRK10762 94 ------LTIAENIFLGRefvNRFGRIdWKKMYAEADKllaRLNLRFS-------SDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 158 PLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGA 221
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAERE 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-226 |
1.07e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 4 RTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ-LARRLALLP 82
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRaVCPRIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 Q---HHLSPEgITVRELVSY-GRspwlsLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTP 158
Cdd:NF033858 83 QglgKNLYPT-LSVFENLDFfGR-----LFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 159 LILLDEPTTYLDinhqvELMR-----LMVELK--RQGKTVVTVLHDLNQASRYcDHLVVLASGRVMAQGAPEAVM 226
Cdd:NF033858 157 LLILDEPTTGVD-----PLSRrqfweLIDRIRaeRPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-227 |
1.30e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.51 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTV-SYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLtPDSGEILLDEKPIAGFSARQLARRLALLPQH 84
Cdd:PRK11174 353 EDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQN 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 HLSPEGiTVRELVSYGRSpwlslwgrlSAEDnERVNVAMSQTrtrNLAD--RRLTQ------------LSGGQRQRAFLA 150
Cdd:PRK11174 432 PQLPHG-TLRDNVLLGNP---------DASD-EQLQQALENA---WVSEflPLLPQgldtpigdqaagLSVGQAQRLALA 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 151 MVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKrQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQ 572
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
6-226 |
1.85e-18 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 84.24 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQA--VLDGLSLALPAGKITALLGPNGCGKSTLLncfsRLL----TPDSGEILLDEKPIAGFSARQLARRLA 79
Cdd:TIGR03797 455 DRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLL----RLLlgfeTPESGSVFYDGQDLAGLDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQH-HLSP----EGITVRELVSYGRSpWLSLwgRLS--AEDNERVNVAMsqtrtRNLADRRLTQLSGGQRQRAFLAMV 152
Cdd:TIGR03797 531 VVLQNgRLMSgsifENIAGGAPLTLDEA-WEAA--RMAglAEDIRAMPMGM-----HTVISEGGGTLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRlmvELKRQGKTVVTVLHDLNQAsRYCDHLVVLASGRVMAQGAPEAVM 226
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSE---SLERLKVTRIVIAHRLSTI-RNADRIYVLDAGRVVQQGTYDELM 672
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-216 |
1.87e-18 |
|
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: 84.08 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 21 LSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIagfSARQLA--RRL--ALLPQHHLSPEgitvrel 96
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREayRQLfsAVFSDFHLFDR------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 97 vsygrspwlsLWGRLSAEDNERVNVAMS----QTRTRnLADRRL--TQLSGGQRQRafLAMVLA--QDTPLILLDE---- 164
Cdd:COG4615 421 ----------LLGLDGEADPARARELLErlelDHKVS-VEDGRFstTDLSQGQRKR--LALLVAllEDRPILVFDEwaad 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 165 --PtTYLDINHQVELMrlmvELKRQGKTVVTVLHDlnqaSRY---CDHLVVLASGRV 216
Cdd:COG4615 488 qdP-EFRRVFYTELLP----ELKARGKTVIAISHD----DRYfdlADRVLKMDYGKL 535
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-213 |
1.89e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.30 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGfsarqlarrlal 80
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 lpqhhLSPEgiTVRELVSY-GRSPwlSLWGRlSAEDN------------ERVNVAMSQTR---TRNLADRRLTQLSGGQR 144
Cdd:PRK10247 74 -----LKPE--IYRQQVSYcAQTP--TLFGD-TVYDNlifpwqirnqqpDPAIFLDDLERfalPDTILTKNIAELSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 145 QRAFLAMVLaQDTP-LILLDEPTTYLDINHQVELMRLMVELKR-QGKTVVTVLHDLNQASrYCDHLVVLAS 213
Cdd:PRK10247 144 QRISLIRNL-QFMPkVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEIN-HADKVITLQP 212
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-172 |
2.77e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 83.63 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEkpiagfsarqlARRLALLPQHH 85
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE-----------TVKLAYVDQSR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 86 --LSPEGiTVRELVSYGrspwlslwgrlsaedNERVNVAMSQTRTR------NL--AD--RRLTQLSGGQRQRAFLAMVL 153
Cdd:PRK11819 397 daLDPNK-TVWEEISGG---------------LDIIKVGNREIPSRayvgrfNFkgGDqqKKVGVLSGGERNRLHLAKTL 460
|
170
....*....|....*....
gi 556321685 154 AQDTPLILLDEPTTYLDIN 172
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLDVE 479
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-221 |
2.97e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 11 SYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFS---ARQLArrLALLPQH-HL 86
Cdd:PRK15439 20 QYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLG--IYLVPQEpLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 87 SPEgITVRELVSYGRSPWLSLWGRLS---AEDNERVNVAMsQTRTRNLADRRLTQLSGGqrqraflamvLAQDTPLILLD 163
Cdd:PRK15439 98 FPN-LSVKENILFGLPKRQASMQKMKqllAALGCQLDLDS-SAGSLEVADRQIVEILRG----------LMRDSRILILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 164 EPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGA 221
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-198 |
3.28e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 83.32 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGaqavldGLSLALPAGKI-----TALLGPNGCGKSTllncFSRLL----TPDSGEILLDEKpiagfsarqlar 76
Cdd:PRK13409 344 PDLTKKLG------DFSLEVEGGEIyegevIGIVGPNGIGKTT----FAKLLagvlKPDEGEVDPELK------------ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 rLALLPQHHLSPEGITVRELVS-----YGRSPWLSlwgrlsaEDNERVNVAmsqtrtrNLADRRLTQLSGGQRQRAFLAM 151
Cdd:PRK13409 402 -ISYKPQYIKPDYDGTVEDLLRsitddLGSSYYKS-------EIIKPLQLE-------RLLDKNVKDLSGGELQRVAIAA 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556321685 152 VLAQDTPLILLDEPTTYLDINHQVE---LMRLMVELKrqGKTVVTVLHDL 198
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDVEQRLAvakAIRRIAEER--EATALVVDHDI 514
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-231 |
6.09e-18 |
|
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: 82.57 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDS--GEILLDEKPIAGFSARQLARR-LA 79
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLSPEGITVRELVSYGRSpwLSLWGRLSAEDN--ERVNVAMSQTRTRNLAD-RRLTQLSGGQRQRAFLAMVLAQD 156
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNE--ITLPGGRMAYNAmyLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 157 TPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELL 231
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDII 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-198 |
6.47e-18 |
|
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: 82.52 E-value: 6.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKI-----TALLGPNGCGKSTllncFSRLL----TPDSGEILLDEKpiagfsarqlarrLALLPQHhLSP 88
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTT----FAKILagvlKPDEGEVDEDLK-------------ISYKPQY-ISP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 89 E-GITVRELvsygrspwlslwgrLSAEDNERVNVAMSQT------RTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:COG1245 413 DyDGTVEEF--------------LRSANTDDFGSSYYKTeiikplGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556321685 162 LDEPTTYLDINHQVELMRLmveLKR----QGKTVVTVLHDL 198
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKA---IRRfaenRGKTAMVVDHDI 516
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-215 |
6.55e-18 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 79.05 E-value: 6.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYG-----AQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCfsrLLtpdsGEIlldeKPIAGFSarQLARR 77
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSA---LL----GEL----EKLSGSV--SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 LALLPQhhlspegitvrelvsygrSPWLS--------LWGrlSAEDNERVNVAMS----QTRTRNLADRRLTQ------- 138
Cdd:cd03250 68 IAYVSQ------------------EPWIQngtireniLFG--KPFDEERYEKVIKacalEPDLEILPDGDLTEigekgin 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 139 LSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDI---NHQVElmRLMVELKRQGKTVVTVLHDLnQASRYCDHLVVLASGR 215
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAhvgRHIFE--NCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-225 |
1.40e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.54 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQ-----AVLDgLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPD---SGEILLDEKPIAGFSARQL 74
Cdd:PRK09473 13 LDVKDLRVTFSTPdgdvtAVND-LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 75 ----ARRLALL---PQHHLSPEGITVRELVSYgrspwLSLWGRLSAED--NERVN----VAMSQTRtrnladRRLT---- 137
Cdd:PRK09473 92 nklrAEQISMIfqdPMTSLNPYMRVGEQLMEV-----LMLHKGMSKAEafEESVRmldaVKMPEAR------KRMKmyph 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 138 QLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKT-VVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRT 240
|
....*....
gi 556321685 217 MAQGAPEAV 225
Cdd:PRK09473 241 MEYGNARDV 249
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
3-223 |
1.82e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 78.84 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCF----SRLLTpdSGEILLDEKPIAGFSARQLARR- 77
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSYEVT--SGTILFKGQDLLELEPDERARAg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 LALLPQHHLSPEGITVRELVsygRSpwlSLWGRLSAEDNERVNVA-----MSQTRT-----RNLADRRLTQ-LSGGQRQR 146
Cdd:TIGR01978 79 LFLAFQYPEEIPGVSNLEFL---RS---ALNARRSARGEEPLDLLdfeklLKEKLAlldmdEEFLNRSVNEgFSGGEKKR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 147 AFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDlNQASRYC--DHLVVLASGRVMAQGAPE 223
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHY-QRLLNYIkpDYVHVLLDGRIVKSGDVE 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-220 |
1.90e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.46 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 9 TVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDS--GEILLDEKPIAgfsaRQLARRLALLPQHHL 86
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 87 SPEGITVRE---LVSYGRSP-WLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:PLN03211 151 LYPHLTVREtlvFCSLLRLPkSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 163 DEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHdlNQASR---YCDHLVVLASGRVMAQG 220
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH--QPSSRvyqMFDSVLVLSEGRCLFFG 289
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-234 |
2.04e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILL------DEKPIagFSARQLARRLALLPQHHLSpeG 90
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldtsDEENL--WDIRNKAGMVFQNPDNQIV--A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 91 ITVRELVSYGRSPWlslwGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLD 170
Cdd:PRK13633 101 TIVEEDVAFGPENL----GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 171 INHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMKP-ELLKTV 234
Cdd:PRK13633 177 PSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEvEMMKKI 241
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-220 |
2.12e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.16 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYG--AQAVlDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:PRK13657 338 DDVSFSYDnsRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 HhlspEGI---TVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRN-LADRRLTQLSGGQRQRAFLAMVLAQDTPL 159
Cdd:PRK13657 417 D----AGLfnrSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDtVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 160 ILLDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNQAsRYCDHLVVLASGRVMAQG 220
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTV-RNADRILVFDNGRVVESG 551
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-224 |
3.20e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA----VLDGLSLALPAGKITALLGPNGCGKS-TLLNCFSRLLTPD----SGEILL--------DEKP 65
Cdd:PRK15134 6 LAIENLSVAFRQQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFhgesllhaSEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 66 IAGFSARQLAR-----RLALLPQHHLSPEgitVRELVSYGRSpwlslWGRLSAEDN-----ERVNVamsqtrtRNlADRR 135
Cdd:PRK15134 86 LRGVRGNKIAMifqepMVSLNPLHTLEKQ---LYEVLSLHRG-----MRREAARGEilnclDRVGI-------RQ-AAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 136 LT----QLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVV 210
Cdd:PRK15134 150 LTdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAV 229
|
250
....*....|....
gi 556321685 211 LASGRVMAQGAPEA 224
Cdd:PRK15134 230 MQNGRCVEQNRAAT 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-216 |
3.58e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY-GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ---LARRL 78
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQ-HHLSPEGiTVRELVSYGrspwLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDT 157
Cdd:PRK10908 82 GMIFQdHHLLMDR-TVYDNVAIP----LIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 158 PLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-233 |
3.59e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTvsygAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARR-LA 79
Cdd:PRK11288 256 VRLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLSpEGI----TVRELVSYGRSPWLSLWGRLSAEDNERVN----VAMSQTRTRNlADRRLTQLSGGQRQRAFLAM 151
Cdd:PRK11288 332 LCPEDRKA-EGIipvhSVADNINISARRHHLRAGCLINNRWEAENadrfIRSLNIKTPS-REQLIMNLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 152 VLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVM-----AQGAPEAVM 226
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQAL 489
|
....*..
gi 556321685 227 KPELLKT 233
Cdd:PRK11288 490 SLALPRT 496
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-229 |
4.51e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.41 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 13 GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQHHLSPEGiT 92
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-T 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 93 VR-ELVSYGRSPWLSLWGRLsaednERVNVAMSQTRTRNLADRRLTQ----LSGGQRQRAFLAMVLAQDTPLILLDEPTT 167
Cdd:PLN03232 1326 VRfNIDPFSEHNDADLWEAL-----ERAHIKDVIDRNPFGLDAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 168 YLDINHQVELMRLMVElKRQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMKPE 229
Cdd:PLN03232 1401 SVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-197 |
5.32e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 79.94 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFsarqlarrlalLP 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGY-----------YA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLS--PEGITVRElvsygrspWLSLW--------------GRL--SAED-NERVNVamsqtrtrnladrrltqLSGGQ 143
Cdd:PRK15064 389 QDHAYdfENDLTLFD--------WMSQWrqegddeqavrgtlGRLlfSQDDiKKSVKV-----------------LSGGE 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556321685 144 RQRAFLAMVLAQDTPLILLDEPTTYLDInHQVELMRLMVElKRQGkTVVTVLHD 197
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDM-ESIESLNMALE-KYEG-TLIFVSHD 494
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-214 |
1.03e-16 |
|
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: 75.74 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPD--SGEILLDEKPIagfsARQLARRLALLPQHHLSPEGITVRE 95
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL----DKNFQRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 96 lvsygrspwlSLwgRLSAednervnvamsqtrtrnladrRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQV 175
Cdd:cd03232 99 ----------AL--RFSA---------------------LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556321685 176 ELMRLMVELKRQGKTVVTVLHdlnQAS----RYCDHLVVLASG 214
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIH---QPSasifEKFDRLLLLKRG 185
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-220 |
2.25e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 77.94 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQ-AVLDGLSLALPAGKITALLGPNGCGKSTLlncfSRLLT----PDSGEILLDEKPIAGFSARQLAR 76
Cdd:COG5265 357 EVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTL----ARLLFrfydVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 RLALLPQHhlspegiTV------RELVSYGRspwlslwgrLSAEDNERVNVA-MSQTRT--RNLADRRLTQ-------LS 140
Cdd:COG5265 433 AIGIVPQD-------TVlfndtiAYNIAYGR---------PDASEEEVEAAArAAQIHDfiESLPDGYDTRvgerglkLS 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 141 GGQRQRAFLAMVLAQDTPLILLDEPTTYLD------InhQVELMRLmvelkRQGKTVVTVLHDLnqaS--RYCDHLVVLA 212
Cdd:COG5265 497 GGEKQRVAIARTLLKNPPILIFDEATSALDsrteraI--QAALREV-----ARGRTTLVIAHRL---StiVDADEILVLE 566
|
....*...
gi 556321685 213 SGRVMAQG 220
Cdd:COG5265 567 AGRIVERG 574
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-230 |
4.03e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 77.36 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 22 SLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQHH----LSPE----GITV 93
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNntdmLSPGeddtGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 94 RELVsygrspwlslwgRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINH 173
Cdd:PRK10938 103 AEII------------QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 174 QVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPEL 230
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQAL 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-235 |
4.44e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGF-SARQLARRLALL 81
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHHLSPEGITVRELVSYGrspwlslwGRLSAEDNERVNVAMSQTRTRNLADRRLTQ---LSGGQRQRAFLAMVLAQDTP 158
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMG--------GFFAERDQFQERIKWVYELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 159 LILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMKPELLKTVF 235
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-243 |
5.93e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.07 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 23 LALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIagFSARQ---LA---RRLALLPQ-HHLSPEgITVRE 95
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEKgicLPpekRRIGYVFQdARLFPH-YKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 96 LVSYGrspwlslwgrLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQV 175
Cdd:PRK11144 96 NLRYG----------MAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 176 ELMRLMVELKRQGKT-VVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV-----MKPELLK----TVFSVE-AEIHP 243
Cdd:PRK11144 166 ELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVwassaMRPWLPKeeqsSILKVTvLEHHP 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-220 |
2.33e-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: 75.44 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA--VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGfSARQLARRLAL 80
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGITVRElvsygrspWLSLWGRLS---AEDNERV-NVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQD 156
Cdd:TIGR01257 2017 CPQFDAIDDLLTGRE--------HLYLYARLRgvpAEEIEKVaNWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 157 TPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-226 |
4.09e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGA-QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:PRK10790 340 RIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQHHLSPEGiTVRELVSYGRSpwLS---LWGRLsaednERVNVAmsqTRTRNLAD---RRLTQ----LSGGQRQRAFLA 150
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLGRD--ISeeqVWQAL-----ETVQLA---ELARSLPDglyTPLGEqgnnLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 151 MVLAQdTPLIL-LDEPTTYLDINHQVELMRLMVELkRQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVM 226
Cdd:PRK10790 489 RVLVQ-TPQILiLDEATANIDSGTEQAIQQALAAV-REHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-218 |
6.37e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 6.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLT---VSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNC-FSRLLTPDSGEILLDEKPIAGFS-ARQLARR 77
Cdd:TIGR02633 258 LEARNLTcwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQAlFGAYPGKFEGNVFINGKPVDIRNpAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 LALLPQ----HHLSP-----EGITVRELVSYgrspwlSLWGRLSAEDNER-VNVAMSQTRTRNLA-DRRLTQLSGGQRQR 146
Cdd:TIGR02633 338 IAMVPEdrkrHGIVPilgvgKNITLSVLKSF------CFKMRIDAAAELQiIGSAIQRLKVKTASpFLPIGRLSGGNQQK 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 147 AFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMA 218
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-225 |
7.74e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.82 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 15 QAVlDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQL-ARRLALL-----PQHHLSP 88
Cdd:PRK15079 35 KAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWrAVRSDIQmifqdPLASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 89 EgITVRELVSygrSPWLSLWGRLSAED-NERVNVAMSQTRTR-NLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPT 166
Cdd:PRK15079 114 R-MTIGEIIA---EPLRTYHPKLSRQEvKDRVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 167 TYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
3.42e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.76 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY-----GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEI---LLDE-----KPiaGF 69
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrVGDEwvdmtKP--GP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 70 SARQLARR-LALLPQHH-LSPEGITVRELVsygRSPWLSL---WGRLSAEDNERVnVAMSQTRTRNLADRRLTQLSGGQR 144
Cdd:TIGR03269 358 DGRGRAKRyIGILHQEYdLYPHRTVLDNLT---EAIGLELpdeLARMKAVITLKM-VGFDEEKAEEILDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 145 QRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPE 223
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
...
gi 556321685 224 AVM 226
Cdd:TIGR03269 514 EIV 516
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-216 |
4.67e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTvSYGAQAVLDgLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ-LARRLALLPQ-- 83
Cdd:PRK09700 270 NVT-SRDRKKVRD-ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAYITEsr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 ------HHLS-PEGITVRELVSYGRspWLSLWGRLSAEDNERVnvAMSQTRTRNLA----DRRLTQLSGGQRQRAFLAMV 152
Cdd:PRK09700 348 rdngffPNFSiAQNMAISRSLKDGG--YKGAMGLFHEVDEQRT--AENQRELLALKchsvNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-196 |
4.67e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 1 MRLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTpdSGEILLDEKpIAGFSARQ--LARRL 78
Cdd:TIGR00956 762 WRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDR-LVNGRPLDssFQRSI 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHHLSPEGITVRELVSYgrSPWLSLWGRLS-AEDNERVNVAMSQTRTRNLADRRL----TQLSGGQRQRAFLAMVL 153
Cdd:TIGR00956 839 GYVQQQDLHLPTSTVRESLRF--SAYLRQPKSVSkSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVEL 916
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556321685 154 AQDTPLIL-LDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLH 196
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-197 |
5.34e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDG-LSLALPAGKITALLGPNGCGKSTllncFSRLLT----PDSGEILLDEKPIAGfSARQLAR 76
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKST----LAMLLTglyqPQSGEILLDGKPVTA-EQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 RL--AL-----LPQHHLSPEGITVR-ELVsygrSPWLSLWG---RLSAEDNERVNvamsqtrtrnladrrlTQLSGGQRQ 145
Cdd:PRK10522 397 KLfsAVftdfhLFDQLLGPEGKPANpALV----EKWLERLKmahKLELEDGRISN----------------LKLSKGQKK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556321685 146 RAFLAMVLAQDTPLILLDEPTTYLDINHQVELMR-LMVELKRQGKTVVTVLHD 197
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQDPHFRREFYQvLLPLLQEMGKTIFAISHD 509
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-211 |
5.50e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTV-SYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEkpiagfsarqlARRLAL 80
Cdd:COG4178 362 ALALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-----------GARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LPQH-HLsPEGiTVRELVSYGRSPwlslwgrlSAEDNERVNVAMSQTRTRNLADrRLTQ-------LSGGQRQR-AFlAM 151
Cdd:COG4178 431 LPQRpYL-PLG-TLREALLYPATA--------EAFSDAELREALEAVGLGHLAE-RLDEeadwdqvLSLGEQQRlAF-AR 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 152 VLAQDTPLILLDEPTTYLDINHQVELMRLMVElKRQGKTVVTVLH--DLNQasrYCDHLVVL 211
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHrsTLAA---FHDRVLEL 556
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-226 |
5.71e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.43 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 21 LSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALL---PQHHLSPegitvRELV 97
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIfqdPSTSLNP-----RQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 98 SYGRSPWLSLWGRLSAEDNE-RVNVAMSQTRTR-NLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQV 175
Cdd:PRK15112 107 SQILDFPLRLNTDLEPEQREkQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556321685 176 ELMRLMVELK-RQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVM 226
Cdd:PRK15112 187 QLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-227 |
1.62e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGA-QAVlDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAgfsarqlarrlallpqh 84
Cdd:NF033858 270 RGLTMRFGDfTAV-DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD----------------- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 hlsPEGITVRELVSYgRSPWLSLWGRLS----------------AEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAF 148
Cdd:NF033858 332 ---AGDIATRRRVGY-MSQAFSLYGELTvrqnlelharlfhlpaAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLS 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 149 LAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKtvVTVL---HDLNQASRyCDHLVVLASGRVMAQGAPEAV 225
Cdd:NF033858 408 LAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDG--VTIFistHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
..
gi 556321685 226 MK 227
Cdd:NF033858 485 VA 486
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-204 |
1.84e-13 |
|
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: 69.58 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLA-LPAGKItALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFsarqlarrlalLPQH-HLSPEgITVR 94
Cdd:TIGR03719 20 ILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGY-----------LPQEpQLDPT-KTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 95 ELVSYGRSPWLSLWGRL-------SAEDNERVNVAMSQTRTRNL--------ADRRL----------------TQLSGGQ 143
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRFneisakyAEPDADFDKLAAEQAELQEIidaadawdLDSQLeiamdalrcppwdadvTKLSGGE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 144 RQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLmveLKRQGKTVVTVLHDlnqasRY 204
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH---LQEYPGTVVAVTHD-----RY 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-215 |
5.47e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.89 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDS--GEILLDEKPIAGFSARQLARR--- 77
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 -----LALLPQhhLS-PEGITV-RELVSYGRSPWlslwgrlsAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLA 150
Cdd:NF040905 82 iihqeLALIPY--LSiAENIFLgNERAKRGVIDW--------NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 151 MVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGR 215
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-216 |
7.77e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 67.58 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 32 ALLGPNGCGKSTLLNCFSRLLTPDSGEILldekpiagfsaRQLARRLALLPQHHLSPEGITVRELVSYGRS-PWLslwgr 110
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCfPGV----- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 111 lsAEDNERVNVAmSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELkrQGKt 190
Cdd:PLN03073 603 --PEQKLRAHLG-SFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF--QGG- 676
|
170 180
....*....|....*....|....*.
gi 556321685 191 VVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PLN03073 677 VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
138-227 |
8.06e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.07 E-value: 8.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 138 QLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
90
....*....|.
gi 556321685 217 MAQGAPEAVMK 227
Cdd:PRK11022 233 VETGKAHDIFR 243
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-216 |
8.56e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.50 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLdEKPIagfsarqlarRLALLP 82
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI----------KLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLspegitvrELVSYGRSPwLSLWGRLSAEDNERvnvamsQTRTR----NLADRRLT----QLSGGQRQRAFLAMVLA 154
Cdd:PRK10636 382 QHQL--------EFLRADESP-LQHLARLAPQELEQ------KLRDYlggfGFQGDKVTeetrRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 155 QDTPLILLDEPTTYLDINHQVELMRLMVELkrQGKTVVtVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVV-VSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-229 |
1.33e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQHHLSPEGiTVR-E 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TVRfN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 96 LVSYGRSPWLSLWGRLsaednERVNVAMSQTRTRNLADRRLTQ----LSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDI 171
Cdd:PLN03130 1333 LDPFNEHNDADLWESL-----ERAHLKDVIRRNSLGLDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 172 NHQVELMRLMVELKRQGkTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMKPE 229
Cdd:PLN03130 1408 RTDALIQKTIREEFKSC-TMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-209 |
1.48e-12 |
|
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: 63.92 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCfsrlltpdsgeILLdekpIAGFSARQLARRLALLPQHhlspegitvrelv 97
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDA-----------IGL----ALGGAQSATRRRSGVKAGC------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 98 sygrspwlslwgrlsaednervNVAmSQTRTRNLAdrrLTQLSGGQRQRAFLAMVLA----QDTPLILLDEPTTYLDINH 173
Cdd:cd03227 63 ----------------------IVA-AVSAELIFT---RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRD 116
|
170 180 190
....*....|....*....|....*....|....*.
gi 556321685 174 QVELMRLMVELKRQGKTVVTVLHDLNQASRYcDHLV 209
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIVITHLPELAELA-DKLI 151
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-197 |
1.95e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEK-PIAGFSarqlarrlallpQH 84
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFD------------QH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 H--LSPEGiTVRELVsygrspwlslwgrlsAEDNERVnvaMSQTRTRN----LAD------RRLT---QLSGGQRQRAFL 149
Cdd:PRK11147 391 RaeLDPEK-TVMDNL---------------AEGKQEV---MVNGRPRHvlgyLQDflfhpkRAMTpvkALSGGERNRLLL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556321685 150 AMVLAQDTPLILLDEPTTYLDInhqvELMRLMVEL--KRQGkTVVTVLHD 197
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDV----ETLELLEELldSYQG-TVLLVSHD 496
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-196 |
2.02e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 66.79 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTpdSGEILLDEKpIAGFSARQ--LARRLALLPQHHLSPEGITVR 94
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKT--GGYIEGDIR-ISGFPKKQetFARISGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 95 ELVSYgrSPWLSLWGRLSAEDNER-VNVAMSQTRTRNLADR-----RLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTY 168
Cdd:PLN03140 972 ESLIY--SAFLRLPKEVSKEEKMMfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180
....*....|....*....|....*...
gi 556321685 169 LDINHQVELMRLMVELKRQGKTVVTVLH 196
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-222 |
2.19e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.51 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLA 79
Cdd:TIGR00957 1284 RVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLSPEGITVRELVSYGRSPWLSLWGRLSaednervnVAMSQTRTRNLADRRLTQ-------LSGGQRQRAFLAMV 152
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALE--------LAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQvELMRLMVELKRQGKTVVTVLHDLNQASRYCdHLVVLASGRVMAQGAP 222
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETD-NLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAP 1503
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-219 |
2.95e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQA---VLDGLSLALPAGKITALLGPNGCGKSTLLNC-FSRLLTPDSGEILLDEKPIAGFSARQ-LARR 77
Cdd:PRK13549 260 LEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQClFGAYPGRWEGEIFIDGKPVKIRNPQQaIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 78 LALLP----QHHLSP-----EGITvreLVSYGRspwLSLWGRLSAEDNER-VNVAMSQTRTRNL-ADRRLTQLSGGQRQR 146
Cdd:PRK13549 340 IAMVPedrkRDGIVPvmgvgKNIT---LAALDR---FTGGSRIDDAAELKtILESIQRLKVKTAsPELAIARLSGGNQQK 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 147 AFLA-MVLAQDTPLIlLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQ 219
Cdd:PRK13549 414 AVLAkCLLLNPKILI-LDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-214 |
3.25e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 63.89 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 16 AVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRlallpqhhlspegitVRE 95
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSR---------------NRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 96 LVSYG-RSPWLSlwgRLSAEDNERVNVAMSQTRTRNLAD--------------------RRLTQLSGGQRQRAFLAMVLA 154
Cdd:cd03290 80 SVAYAaQKPWLL---NATVEENITFGSPFNKQRYKAVTDacslqpdidllpfgdqteigERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556321685 155 QDTPLILLDEPTTYLDINHQVELMR--LMVELKRQGKTVVTVLHDLnQASRYCDHLVVLASG 214
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-215 |
4.72e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ-LARRLALLPQH 84
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 HLSPEGITVRELVSYGRSPW--------------LSLWGRLSAEDNERVNVAmsqtrtrnladrrltQLSGGQRQRAFLA 150
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTkgmfvdqdkmyrdtKAIFDELDIDIDPRAKVA---------------TLSVSQMQMIEIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 151 MVLAQDTPLILLDEPTTYL---DINHqveLMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGR 215
Cdd:PRK10982 147 KAFSYNAKIVIMDEPTSSLtekEVNH---LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-196 |
1.06e-11 |
|
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: 61.40 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGA-QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEIlldEKPiagfsarqLARRLALL 81
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMP--------EGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQHHLSPEGiTVRELVSYgrsPWlslwgrlsaednERVnvamsqtrtrnladrrltqLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:cd03223 70 PQRPYLPLG-TLREQLIY---PW------------DDV-------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 556321685 162 LDEPTTYLDINHQVELMRLmveLKRQGKTVVTVLH 196
Cdd:cd03223 115 LDEATSALDEESEDRLYQL---LKELGITVISVGH 146
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-225 |
2.26e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA---RRLALL---PQHHLSPegi 91
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIfqdPYASLDP--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 92 tvRELVSYGRSPWLSLWGRLSAED-NERVNVAMSQTRTR-NLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYL 169
Cdd:PRK10261 417 --RQTVGDSIMEPLRVHGLLPGKAaAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 170 DINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAV 225
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-229 |
2.57e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.26 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQHHLSPEGiTVREL 96
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 97 VsygrSPWL-----SLWGRLSAED-NERVNVAMSQTRTRNLADRrlTQLSGGQRQRAFLA-MVLAQDTPLILLDEPTTYL 169
Cdd:PTZ00243 1404 V----DPFLeassaEVWAALELVGlRERVASESEGIDSRVLEGG--SNYSVGQRQLMCMArALLKKGSGFILMDEATANI 1477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 170 D--INHQVElmrLMVELKRQGKTVVTVLHDLNQASRYcDHLVVLASGRVMAQGAP-EAVMKPE 229
Cdd:PTZ00243 1478 DpaLDRQIQ---ATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPrELVMNRQ 1536
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-175 |
3.05e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 6 ENLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDsGEILLDEKPIAGFSARQLARRLALLPQ 83
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 HHLSPEGITVRELVSYGRSPWLSLWgRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLD 163
Cdd:TIGR01271 1300 KVFIFSGTFRKNLDPYEQWSDEEIW-KVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170
....*....|...
gi 556321685 164 EPTTYLD-INHQV 175
Cdd:TIGR01271 1379 EPSAHLDpVTLQI 1391
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-193 |
7.29e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIA-GFSARQLArRLALL 81
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATrGDRSRFMA-YLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 82 PQhhLSPEGITVREL----VSYGRSPwlslwgrlsaedNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDT 157
Cdd:PRK13543 91 PG--LKADLSTLENLhflcGLHGRRA------------KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPA 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 556321685 158 PLILLDEPTTYLDINHQVELMRLM-VELKRQGKTVVT 193
Cdd:PRK13543 157 PLWLLDEPYANLDLEGITLVNRMIsAHLRGGGAALVT 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-216 |
8.10e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 8.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 21 LSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ-LARRLALLP----QHHL---SPEGIT 92
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrqSSGLyldAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 93 VRELVsYGRSPWlslWGRLSAEDN--ERVNVAMSQTRtrNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLD 170
Cdd:PRK15439 362 VCALT-HNRRGF---WIKPARENAvlERYRRALNIKF--NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556321685 171 INHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-205 |
9.66e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 9.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPI-AGFSARQlaRRLALLPQHH 85
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQ--KQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 86 LSPEGITVRELVSYGRSpwlslwgrlSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEP 165
Cdd:PRK13540 84 GINPYLTLRENCLYDIH---------FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556321685 166 TTYLDINHQVELMRLMVELKRQGKTVVTVLHD---LNQA--SRYC 205
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQdlpLNKAdyEEYH 199
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-244 |
1.81e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLncfSRLLtpdsGEILLDEKPIAgfsarqLARRLALLP 82
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLL---SALL----AEMDKVEGHVH------MKGSVAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSpEGITVRELVSYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILL 162
Cdd:TIGR00957 706 QQAWI-QNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 163 DEPTTYLD-------INHQVELMRLMvelkrQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMK-----PEL 230
Cdd:TIGR00957 785 DDPLSAVDahvgkhiFEHVIGPEGVL-----KNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQrdgafAEF 858
|
250
....*....|....
gi 556321685 231 LKTVFSVEAEIHPE 244
Cdd:TIGR00957 859 LRTYAPDEQQGHLE 872
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-216 |
2.26e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.48 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 7 NLTVSY--GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDsGEILLDEKPIAGFSARQLARRLALLPQH 84
Cdd:cd03289 7 DLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 85 HLSPEGITVRELVSYGRSPWLSLWgrlsaEDNERVNVAMSQTRTRNLADRRLTQ----LSGGQRQRAFLAMVLAQDTPLI 160
Cdd:cd03289 86 VFIFSGTFRKNLDPYGKWSDEEIW-----KVAEEVGLKSVIEQFPGQLDFVLVDggcvLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 161 LLDEPTTYLD-INHQVelMRLMVELKRQGKTVVTVLHDLnQASRYCDHLVVLASGRV 216
Cdd:cd03289 161 LLDEPSAHLDpITYQV--IRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-197 |
2.51e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 58.39 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 30 ITALLGPNGCGKSTLLNCFSRLLTPDsgeilLDEKPIAGFSARQLARRLALLPQHHLSPEGITVRELVSYgRSPwlslwg 109
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKYALTGE-----LPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKYTIT-RSL------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 110 rlsaedNERVNVAM-SQTRTRNLADRRLTQLSGGQRQ------RAFLAMVLAQDTPLILLDEPTTYLDINH-QVELMRLM 181
Cdd:cd03240 92 ------AILENVIFcHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEII 165
|
170
....*....|....*..
gi 556321685 182 VELKRQG-KTVVTVLHD 197
Cdd:cd03240 166 EERKSQKnFQLIVITHD 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-240 |
2.82e-10 |
|
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: 59.82 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRL--LTPDSGEIL----LDEK------------ 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvaLCEKcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 65 --PIAGFS---------------ARQLARRLALLPQHHLSPEG-ITVRELVsygrspwLSLWGRLSAEDNERVNVAMSQT 126
Cdd:TIGR03269 81 pcPVCGGTlepeevdfwnlsdklRRRIRKRIAIMLQRTFALYGdDTVLDNV-------LEALEEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 127 RTRNLADRRL---TQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDiNHQVELMRLMVE--LKRQGKTVVTVLHDLNQA 201
Cdd:TIGR03269 154 EMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD-PQTAKLVHNALEeaVKASGISMVLTSHWPEVI 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 556321685 202 SRYCDHLVVLASGRVMAQGAPEAVMKpELLKTVFSVEAE 240
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEVVA-VFMEGVSEVEKE 270
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-220 |
3.07e-10 |
|
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: 58.04 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPD---SGEILLDEKPIAGFsARQLARRLALLPQHHLSPEGITVR 94
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEF-AEKYPGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 95 ELVSYgrspwlslwgRLSAEDNERVNVamsqtrtrnladrrltqLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQ 174
Cdd:cd03233 102 ETLDF----------ALRCKGNEFVRG-----------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556321685 175 VELMRLMVELKRQGKTVVTVlhDLNQAS----RYCDHLVVLASGRVMAQG 220
Cdd:cd03233 155 LEILKCIRTMADVLKTTTFV--SLYQASdeiyDLFDKVLVLYEGRQIYYG 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-204 |
4.13e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLA-LPAGKItALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEkpiaGFsarqlarRLALLPQH-HLSPEgITVR 94
Cdd:PRK11819 22 ILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP----GI-------KVGYLPQEpQLDPE-KTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 95 ELVSYGRSPWLSLWGRLsaedNErVNVAMS------------QTR------TRNL--ADRRL----------------TQ 138
Cdd:PRK11819 89 ENVEEGVAEVKAALDRF----NE-IYAAYAepdadfdalaaeQGElqeiidAADAwdLDSQLeiamdalrcppwdakvTK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556321685 139 LSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDI-------NHqvelmrlmveLKRQGKTVVTVLHDlnqasRY 204
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAesvawleQF----------LHDYPGTVVAVTHD-----RY 221
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
52-227 |
5.92e-10 |
|
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: 59.26 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 52 LTPDSGEILLDEKPIAGFSARQLARRLALLPQHHLSPEGITVRELVSygrspwlslwgrlsAEDNER----VNVAMSQTr 127
Cdd:TIGR00630 416 LKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVL--------------KEIRERlgflIDVGLDYL- 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 128 trNLaDRRLTQLSGGQRQRAFLAMVL-AQDTP-LILLDEPTTYLdinHQVELMRLMVELKR---QGKTVVTVLHDlNQAS 202
Cdd:TIGR00630 481 --SL-SRAAGTLSGGEAQRIRLATQIgSGLTGvLYVLDEPSIGL---HQRDNRRLINTLKRlrdLGNTLIVVEHD-EDTI 553
|
170 180 190
....*....|....*....|....*....|.
gi 556321685 203 RYCDHLVVLA------SGRVMAQGAPEAVMK 227
Cdd:TIGR00630 554 RAADYVIDIGpgagehGGEVVASGTPEEILA 584
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-240 |
1.36e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLncfsrlltpdsgEILLDEKPIAgfSARQLARR-LALLPQHHLSPEGiTVRE 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLL------------QSLLSQFEIS--EGRVWAERsIAYVPQQAWIMNA-TVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 96 LVSYgrspwlslwgrLSAEDNER----VNVAMSQTRTRNLADRRLTQ-------LSGGQRQRAFLAMVLAQDTPLILLDE 164
Cdd:PTZ00243 740 NILF-----------FDEEDAARladaVRVSQLEADLAQLGGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 165 PTTYLD------INHQVELMRLmvelkrQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMKPELLKTVFSVE 238
Cdd:PTZ00243 809 PLSALDahvgerVVEECFLGAL------AGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATLAAEL 881
|
..
gi 556321685 239 AE 240
Cdd:PTZ00243 882 KE 883
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-225 |
1.38e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQ----AVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEK----------PIAG 68
Cdd:PRK10261 13 LAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 69 FSARQLAR----RLALL---PQHHLSP-----EGI--TVRELVSYGRSPWLSLWGRLSaednERVNVAMSQTrtrnLADR 134
Cdd:PRK10261 93 QSAAQMRHvrgaDMAMIfqePMTSLNPvftvgEQIaeSIRLHQGASREEAMVEAKRML----DQVRIPEAQT----ILSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 135 RLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQ-GKTVVTVLHDLNQASRYCDHLVVLAS 213
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQ 244
|
250
....*....|..
gi 556321685 214 GRVMAQGAPEAV 225
Cdd:PRK10261 245 GEAVETGSVEQI 256
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-220 |
1.81e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.41 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNcfsrlltpdsgEILldekpiagfsARQLARRLALLPQhhlspegitvrelv 97
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGL----------YASGKARLISFLP-------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 98 SYGRSPWLSLwGRLSAedneRVNVAMSQTRTrnlaDRRLTQLSGGQRQRAFLAMVLAQDTP--LILLDEPTTYLdinHQV 175
Cdd:cd03238 56 KFSRNKLIFI-DQLQF----LIDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL---HQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556321685 176 ELMRLMVELKR---QGKTVVTVLHDLnQASRYCDHLVVLA------SGRVMAQG 220
Cdd:cd03238 124 DINQLLEVIKGlidLGNTVILIEHNL-DVLSSADWIIDFGpgsgksGGKVVFSG 176
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-216 |
2.64e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.94 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 16 AVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLA----RRLALLPQHHLSPEGI 91
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklraKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 92 TVRELVSYgrsPWLsLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDI 171
Cdd:PRK10584 104 NALENVEL---PAL-LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556321685 172 NHQVELMRLMVELKR-QGKTVVTVLHDLNQASRyCDHLVVLASGRV 216
Cdd:PRK10584 180 QTGDKIADLLFSLNReHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-225 |
3.00e-09 |
|
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: 56.95 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 136 LTQLSGGQRQRAFLAMVL-AQDT--PLILLDEPTTYL---DINHqveLMRLMVELKRQGKTVVTVLHDLN---QAsrycD 206
Cdd:TIGR00630 827 ATTLSGGEAQRIKLAKELsKRSTgrTLYILDEPTTGLhfdDIKK---LLEVLQRLVDKGNTVVVIEHNLDvikTA----D 899
|
90 100
....*....|....*....|....*
gi 556321685 207 HLVVL------ASGRVMAQGAPEAV 225
Cdd:TIGR00630 900 YIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-226 |
3.79e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.96 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 55 DSGEILLDEKPIAGFSARQLARRLALLPQHHLSpEGITVRELVSYGRSpwlslwgRLSAEDNERV-NVAMSQTRTRNLAD 133
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGKE-------DATREDVKRAcKFAAIDEFIESLPN 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 134 RRLTQ-------LSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELK-RQGKTVVTVLHDLNQASRyC 205
Cdd:PTZ00265 1347 KYDTNvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKR-S 1425
|
170 180
....*....|....*....|....*.
gi 556321685 206 DHLVVL-----ASGRVMAQGAPEAVM 226
Cdd:PTZ00265 1426 DKIVVFnnpdrTGSFVQAHGTHEELL 1451
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-220 |
4.49e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.26 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 15 QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALLPQHHLspegitvr 94
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF-------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 95 eLVSYGRSPWLSLwGRLSAEDNERVNVAmsqtRTRNLADR--RLTQ------------LSGGQRQRAFLAMVLAQDTPLI 160
Cdd:PRK10789 400 -LFSDTVANNIAL-GRPDATQQEIEHVA----RLASVHDDilRLPQgydtevgergvmLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 161 LLDEPTTYLD--INHQVelmrlMVELK--RQGKTVVTVLHDLNqASRYCDHLVVLASGRVMAQG 220
Cdd:PRK10789 474 ILDDALSAVDgrTEHQI-----LHNLRqwGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRG 531
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
136-222 |
6.23e-09 |
|
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: 54.93 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 136 LTQLSGGQRQRAFLAMVLAQDTP---LILLDEPTTYL---DINHQVELMRLMVElkrQGKTVVTVLHDLNQAsRYCDHLV 209
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLLEVLQRLVD---KGNTVVVIEHNLDVI-KCADWII 242
|
90
....*....|....*....
gi 556321685 210 VL------ASGRVMAQGAP 222
Cdd:cd03271 243 DLgpeggdGGGQVVASGTP 261
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
137-227 |
7.08e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 55.80 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 137 TQLSGGQRQRAFLAMVLAQ-DTP--LILLDEPTTYL---DINHqveLMRLMVELKRQGKTVVTVLHDLN---QAsrycDH 207
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrSTGktLYILDEPTTGLhfhDIRK---LLEVLHRLVDKGNTVVVIEHNLDvikTA----DW 897
|
90 100
....*....|....*....|....*.
gi 556321685 208 LVVL------ASGRVMAQGAPEAVMK 227
Cdd:COG0178 898 IIDLgpeggdGGGEIVAEGTPEEVAK 923
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
3-251 |
7.16e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.19 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSY----GAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLlTPDSGEIL-----LDEKPIAGFSARQ 73
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrmrFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 74 ----LARRLALL---PQHHLSPEGITVRELV------SYGRSPWLSLWGRL--SAEDNERVNVAMSQTRTRNLAdrrlTQ 138
Cdd:PRK15093 83 rrklVGHNVSMIfqePQSCLDPSERVGRQLMqnipgwTYKGRWWQRFGWRKrrAIELLHRVGIKDHKDAMRSFP----YE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 139 LSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLHDLNQASRYCDHLVVLASGRVM 217
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 556321685 218 AQGAPEavmkpELLKTVFS--VEAEIHPEPVSGRPM 251
Cdd:PRK15093 239 ETAPSK-----ELVTTPHHpyTQALIRAIPDFGSAM 269
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-196 |
8.27e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLL--TPDSGEILLDEKPIagfsarqlarrlal 80
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF-------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 lpqhhlsPEGITVRELVSYGRSPWLSLwgrlsaednERVNVAmsqtrtrNLAD-----RRLTQLSGGQRQRAFLAMVLAQ 155
Cdd:COG2401 97 -------GREASLIDAIGRKGDFKDAV---------ELLNAV-------GLSDavlwlRRFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556321685 156 DTPLILLDEPTTYLDINHQVELMRLMVEL-KRQGKTVVTVLH 196
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-211 |
9.37e-09 |
|
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: 52.76 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 28 GKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLdekpiagfsarqlarrlallpqhhlspegitvrelvsygrspwlsl 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 108 wgrLSAEDNERVNvamSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMR------LM 181
Cdd:smart00382 36 ---IDGEDILEEV---LDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
|
170 180 190
....*....|....*....|....*....|....*.
gi 556321685 182 VELKRQGKTVV------TVLHDLNQASRYCDHLVVL 211
Cdd:smart00382 110 LLKSEKNLTVIlttndeKDLGPALLRRRFDRRIVLL 145
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
139-211 |
1.80e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.57 E-value: 1.80e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 139 LSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQG-KTVVTVLHDLNQASRYCDHLVVL 211
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-220 |
1.97e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCG--KSTLLncfSRLLTPDSGEilldeKP--IAGFSARQLARRL 78
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALP---AHV*GPDAGR-----RPwrF*TWCANRRALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 79 ALLPQHhlsPEGITVRELVSyGRSPwLSLWGR---LSAED-NERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLA 154
Cdd:NF000106 86 TIG*HR---PVR*GRRESFS-GREN-LYMIGR*ldLSRKDaRARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 155 QDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-171 |
3.43e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDE------------KPIAG-- 68
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEGtv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 69 --FSARQLARRLALLPQ-HHLSpegitvrELVsyGRSPWLSLWGRLSA--EDNERVNVAMSQTRTRNL-------ADRRL 136
Cdd:PRK11147 84 ydFVAEGIEEQAEYLKRyHDIS-------HLV--ETDPSEKNLNELAKlqEQLDHHNLWQLENRINEVlaqlgldPDAAL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 556321685 137 TQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDI 171
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-214 |
3.97e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.76 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEIlldekpiagfsarQLARRLALLPQHHLSPEGiTVREL 96
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 97 ----VSYGRSPWLSLWGRLSAEdnERVNVAMSQTRTRnLADRRLTqLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDIN 172
Cdd:TIGR01271 507 iifgLSYDEYRYTSVIKACQLE--EDIALFPEKDKTV-LGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556321685 173 HQVE-----LMRLMVElkrqgKTVVTVLHDLNQASRyCDHLVVLASG 214
Cdd:TIGR01271 583 TEKEifescLCKLMSN-----KTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-196 |
4.01e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.72 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTllncFSRLLT--PD----SGEILLDEKPIAGFSARQLAR 76
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKST----LSKVIAghPAykilEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 77 R-LALLPQHHLSPEGITVRELV---------SYGRS---PwLSLWGRLsaedNERVN-VAMSQT-RTRNLADrrltQLSG 141
Cdd:CHL00131 84 LgIFLAFQYPIEIPGVSNADFLrlaynskrkFQGLPeldP-LEFLEII----NEKLKlVGMDPSfLSRNVNE----GFSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 142 GQRQR-AFLAMVLAqDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLH 196
Cdd:CHL00131 155 GEKKRnEILQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-196 |
4.40e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.80 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 15 QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLD-------EKPIAGFSARQLARRLALlpqhhls 87
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKncninniAKPYCTYIGHNLGLKLEM------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 88 pegiTVRELvsygrspwLSLWGRLSaEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTT 167
Cdd:PRK13541 86 ----TVFEN--------LKFWSEIY-NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180
....*....|....*....|....*....
gi 556321685 168 YLDINHQVELMRLMVELKRQGKTVVTVLH 196
Cdd:PRK13541 153 NLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-208 |
6.03e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDekpiagfsarqLARRLALLP 82
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD-----------PNERLGKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 QHHLSPEGITVRELVSYGRSPwlsLWGRLSAEDNERVNVAMSQ---TRTRNL-----------ADRR------------- 135
Cdd:PRK15064 71 QDQFAFEEFTVLDTVIMGHTE---LWEVKQERDRIYALPEMSEedgMKVADLevkfaemdgytAEARagelllgvgipee 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 136 -----LTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINhqveLMR-LMVELKRQGKTVVTVLHD---LNQAsryCD 206
Cdd:PRK15064 148 qhyglMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIN----TIRwLEDVLNERNSTMIIISHDrhfLNSV---CT 220
|
..
gi 556321685 207 HL 208
Cdd:PRK15064 221 HM 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-190 |
6.15e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNcfsrLLTPD-----------------SGEILLDEK 64
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS----LITGDhpqgysndltlfgrrrgSGETIWDIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 65 PIAGFSARQLarrlallpqhHLSPE-GITVRELVSYG------------------RSPWLSLWGrLSAEdnervnvamsq 125
Cdd:PRK10938 336 KHIGYVSSSL----------HLDYRvSTSVRNVILSGffdsigiyqavsdrqqklAQQWLDILG-IDKR----------- 393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 126 trtrnLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLD-INHQveLMRLMVE-LKRQGKT 190
Cdd:PRK10938 394 -----TADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDpLNRQ--LVRRFVDvLISEGET 453
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-197 |
8.61e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 8 LTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILL----------DEKPIAGFSA------ 71
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgnwqlawvnQETPALPQPAleyvid 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 72 -----RQLARRLALLPQHHlspEGITVRELvsYGRSPWLSLWGRLSAEDNERVNVAMSQTRTrnlaDRRLTQLSGGQRQR 146
Cdd:PRK10636 87 gdreyRQLEAQLHDANERN---DGHAIATI--HGKLDAIDAWTIRSRAASLLHGLGFSNEQL----ERPVSDFSGGWRMR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556321685 147 AFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLmveLKRQGKTVVTVLHD 197
Cdd:PRK10636 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKW---LKSYQGTLILISHD 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-213 |
1.26e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 21 LSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILL-DEKPIAGFSARQLARRLALLPQ---------------- 83
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQdpllfsnsiknnikys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 84 -----------HHLSPEGITVRELVSYGRSPWLSLWGRLS--------------------AEDNERVNVAMS-------- 124
Cdd:PTZ00265 484 lyslkdlealsNYYNEDGNDSQENKNKRNSCRAKCAGDLNdmsnttdsneliemrknyqtIKDSEVVDVSKKvlihdfvs 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 125 --QTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELK-RQGKTVVTVLHDLNQA 201
Cdd:PTZ00265 564 alPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTI 643
|
250
....*....|..
gi 556321685 202 sRYCDHLVVLAS 213
Cdd:PTZ00265 644 -RYANTIFVLSN 654
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
28-196 |
1.59e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 51.54 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 28 GKITALLGPNGCGKSTLLNCFSRLLTPDSGEIL--------LDEKPIAG-----FSA--RQLARRLALLP---------- 82
Cdd:COG3593 23 DDLTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedfylgDDPDLPEIeieltFGSllSRLLRLLLKEEdkeeleeale 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 83 --QHHLSPEGITVRELVSygrspwlSLWGRLSaeDNERVNVAMSQTRTRNLA-----------DRRLTQLSGGQRQRAFL 149
Cdd:COG3593 103 elNEELKEALKALNELLS-------EYLKELL--DGLDLELELSLDELEDLLkslslriedgkELPLDRLGSGFQRLILL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556321685 150 AMVLA-------QDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLH 196
Cdd:COG3593 174 ALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-214 |
1.64e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.01 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 17 VLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEIlldekpiagfsarQLARRLALLPQHHLSPEGiTVREL 96
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 97 ----VSYGRSPWLSLwgrLSAEDNERVNVAMSQTRTRNLADRRLTqLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDIN 172
Cdd:cd03291 118 iifgVSYDEYRYKSV---VKACQLEEDITKFPEKDNTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556321685 173 HQVELMRLMVELKRQGKTVVTVLHDLNQASRyCDHLVVLASG 214
Cdd:cd03291 194 TEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
137-227 |
1.76e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 51.61 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 137 TQLSGGQRQRAFLAMVLA-QDT--PLILLDEPTTYL---DINHqveLMRLMVELKRQGKTVVTVLHDLNqASRYCDHLVV 210
Cdd:PRK00349 829 TTLSGGEAQRVKLAKELSkRSTgkTLYILDEPTTGLhfeDIRK---LLEVLHRLVDKGNTVVVIEHNLD-VIKTADWIID 904
|
90 100
....*....|....*....|...
gi 556321685 211 L------ASGRVMAQGAPEAVMK 227
Cdd:PRK00349 905 LgpeggdGGGEIVATGTPEEVAK 927
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
133-220 |
4.86e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 133 DRRLTQLSGGQRQRAFLAMVLAQDTPLIL--LDEPTTYLdinHQVELMRLMVELKR---QGKTVVTVLHDLnQASRYCDH 207
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGL---HPRDNDRLIETLKRlrdLGNTVLVVEHDE-DTIRAADH 207
|
90
....*....|....*....
gi 556321685 208 LVVLA------SGRVMAQG 220
Cdd:cd03270 208 VIDIGpgagvhGGEIVAQG 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-231 |
6.45e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCfsrlltpdsgeiLLDEKPIAGFSARQLARRLALLPQHHLSPEGiTVRELV 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISA------------MLGELSHAETSSVVIRGSVAYVPQVSWIFNA-TVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 98 SYGRSPWLSLWGRLSAEDNERVNVAMSQTRTRNLADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLD--INHQV 175
Cdd:PLN03232 700 LFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDahVAHQV 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 176 ELMRLMVELkrQGKTVVTV---LHDLNQAsrycDHLVVLASGRVMAQGAPEAVMKPELL 231
Cdd:PLN03232 780 FDSCMKDEL--KGKTRVLVtnqLHFLPLM----DRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-216 |
1.45e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSyGaqavLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQ-LARRLAl 80
Cdd:PRK10762 257 RLKVDNLSGP-G----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIV- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 lpqhHLSPE--------GITVRELVSYGRSPWLS-LWGRLSAEDnERVNVA----MSQTRTRNLaDRRLTQLSGGQRQRA 147
Cdd:PRK10762 331 ----YISEDrkrdglvlGMSVKENMSLTALRYFSrAGGSLKHAD-EQQAVSdfirLFNIKTPSM-EQAIGLLSGGNQQKV 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 148 FLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
139-216 |
2.18e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 2.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556321685 139 LSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRV 216
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-223 |
2.41e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 134 RRLTQLSGGQRQRAFLAMVLAQDTP---LILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNqASRYCDHLVV 210
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMH-VVKVADYVLE 883
|
90
....*....|....*....
gi 556321685 211 LA------SGRVMAQGAPE 223
Cdd:PRK00635 884 LGpeggnlGGYLLASCSPE 902
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-196 |
2.51e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLT---PDSGEILLDEKPIAG--FSARQ---- 73
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIdgiPKNCQILHVEQEVVGddTTALQcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 74 --LARRLALLPQHHLSPEGITVRELVSYGRSPWLS---------------LWGRLSAED-----NERVNVAMSQTRTRNL 131
Cdd:PLN03073 258 tdIERTQLLEEEAQLVAQQRELEFETETGKGKGANkdgvdkdavsqrleeIYKRLELIDaytaeARAASILAGLSFTPEM 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556321685 132 ADRRLTQLSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDInHQVelMRLMVELKRQGKTVVTVLH 196
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAV--LWLETYLLKWPKTFIVVSH 399
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-220 |
5.65e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 3 LRTENLTVSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFS--RLLTPDSGEILLDEKPIAGFSARQLARRLAL 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 81 LP-QHHLSPEGIT--------VRELVSYGRSPWLSlwgRLSAED--NERVN-VAMSQ---TRTRNLAdrrltqLSGGQRQ 145
Cdd:PRK09580 82 MAfQYPVEIPGVSnqfflqtaLNAVRSYRGQEPLD---RFDFQDlmEEKIAlLKMPEdllTRSVNVG------FSGGEKK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 146 RAFLAMVLAQDTPLILLDEPTTYLDINhQVELMRLMVELKRQGKTVVTVLHDLNQASRYC--DHLVVLASGRVMAQG 220
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDID-ALKIVADGVNSLRDGKRSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSG 228
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-220 |
9.43e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEIlldekPIAGfSARQLArrlallpqhhlspegitvrelV 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKG-SAALIA---------------------I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 98 SYGrspwlsLWGRLSAEDN-ERVNVAMSQTRTR---------NLAD------RRLTQLSGGQRQRAFLAMVLAQDTPLIL 161
Cdd:PRK13545 93 SSG------LNGQLTGIENiELKGLMMGLTKEKikeiipeiiEFADigkfiyQPVKTYSSGMKSRLGFAISVHINPDILV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556321685 162 LDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQG 220
Cdd:PRK13545 167 IDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-240 |
1.58e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 133 DRRLTQLSGGQRQRAFLAMVLAQDTPLI--LLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDlNQASRYCDHLVV 210
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIID 549
|
90 100 110
....*....|....*....|....*....|....*.
gi 556321685 211 LA------SGRVMAQGAPEavmkpELLKTVFSVEAE 240
Cdd:PRK00635 550 IGpgagifGGEVLFNGSPR-----EFLAKSDSLTAK 580
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
110-197 |
2.15e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 110 RLSAEDNE-RVNVAMsqtrtrNLADRRLTQLSGGQRQ------RAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMV 182
Cdd:PRK03918 765 RVKAEENKvKLFVVY------QGKERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIME 838
|
90
....*....|....*
gi 556321685 183 ELKRQGKTVVTVLHD 197
Cdd:PRK03918 839 RYLRKIPQVIIVSHD 853
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-227 |
2.27e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 18 LDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILL--DEKPIA----------------------GFSARQ 73
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRngEVSVIAisaglsgqltgieniefkmlcmGFKRKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 74 LARrlallpqhhLSPEGITVRELVSYGRSPwlslwgrlsaednervnvamsqtrtrnladrrLTQLSGGQRQRAFLAMVL 153
Cdd:PRK13546 120 IKA---------MTPKIIEFSELGEFIYQP--------------------------------VKKYSSGMRAKLGFSINI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556321685 154 AQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVMAQGAPEAVMK 227
Cdd:PRK13546 159 TVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLP 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-229 |
2.77e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 44.13 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTVSYGA--QAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLA 79
Cdd:cd03288 19 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 80 LLPQHHLSPEGITVRELVSYGRSPWLSLWgrlsaednERVNVAMSQTRTRNLA---DRRLTQ----LSGGQRQRAFLAMV 152
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLW--------EALEIAQLKNMVKSLPgglDAVVTEggenFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556321685 153 LAQDTPLILLDEPTTYLDINHQvELMRLMVELKRQGKTVVTVLHDLNQASRyCDHLVVLASGRVMAQGAPEAVMKPE 229
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-227 |
2.85e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 11 SYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLdekpIAGfsarqlarRLALLPQHHLSPEG 90
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV----IRG--------TVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 91 iTVRELVSYGrSPWlslwgrlsaeDNERVNVAMSQTRTRN----LADRRLTQ-------LSGGQRQRAFLAMVLAQDTPL 159
Cdd:PLN03130 694 -TVRDNILFG-SPF----------DPERYERAIDVTALQHdldlLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556321685 160 ILLDEPTTYLD--INHQVELMRLMVELKRQGKTVVT-VLHDLNQAsrycDHLVVLASGRVMAQGAPEAVMK 227
Cdd:PLN03130 762 YIFDDPLSALDahVGRQVFDKCIKDELRGKTRVLVTnQLHFLSQV----DRIILVHEGMIKEEGTYEELSN 828
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-56 |
6.69e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.89 E-value: 6.69e-05
10 20 30
....*....|....*....|....*....|....*...
gi 556321685 19 DGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDS 56
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-227 |
6.87e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 133 DRRLTQLSGGQRQRAFLAmvlaqdTPL------IL--LDEPTTYLdinHQVELMRL---MVELKRQGKTVVTVLHDLnQA 201
Cdd:COG0178 480 DRSAGTLSGGEAQRIRLA------TQIgsglvgVLyvLDEPSIGL---HQRDNDRLietLKRLRDLGNTVIVVEHDE-DT 549
|
90 100 110
....*....|....*....|....*....|..
gi 556321685 202 SRYCDHLVVL------ASGRVMAQGAPEAVMK 227
Cdd:COG0178 550 IRAADYIIDIgpgageHGGEVVAQGTPEEILK 581
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
29-59 |
1.29e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.29 E-value: 1.29e-04
10 20 30
....*....|....*....|....*....|.
gi 556321685 29 KITALLGPNGCGKSTLLNCFSRLLTPDSGEI 59
Cdd:COG3950 26 RLTVLVGENGSGKTTLLEAIALALSGLLSRL 56
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
133-227 |
2.22e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 133 DRRLTQLSGGQRQRAFLAM--------VLaqdtplILLDEPTTYLdinHQVELMRLMVELKR---QGKTVVTVLHDlNQA 201
Cdd:PRK00349 484 SRSAGTLSGGEAQRIRLATqigsgltgVL------YVLDEPSIGL---HQRDNDRLIETLKHlrdLGNTLIVVEHD-EDT 553
|
90 100 110
....*....|....*....|....*....|..
gi 556321685 202 SRYCDHLVVLAS------GRVMAQGAPEAVMK 227
Cdd:PRK00349 554 IRAADYIVDIGPgagvhgGEVVASGTPEEIMK 585
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
30-53 |
4.90e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.17 E-value: 4.90e-04
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-236 |
5.69e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 153 LAQDTP-LILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLnQASRYCDHLVVLA------SGRVMAQGAPE-- 223
Cdd:PRK00635 1716 LPPKHPtLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQADYLIEMGpgsgktGGKILFSGPPKdi 1794
|
90
....*....|...
gi 556321685 224 AVMKPELLKTVFS 236
Cdd:PRK00635 1795 SASKDSLLKTYMC 1807
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
8-59 |
1.21e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 39.42 E-value: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 556321685 8 LTVSYGAQAVLDGLsLALPAGKITALLGPNGCGKSTLLNcfsrLLTPD----SGEI 59
Cdd:PRK00098 145 LELSAKEGEGLDEL-KPLLAGKVTVLAGQSGVGKSTLLN----ALAPDlelkTGEI 195
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-209 |
1.47e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 138 QLSGGQRqrAFLAMVL--------------AQDTPLILLDEPTTYLDINHQVELMRLMVELKRQG-KTVVTVLHD--LNQ 200
Cdd:PRK02224 781 QLSGGER--ALFNLSLrcaiyrllaegiegDAPLPPLILDEPTVFLDSGHVSQLVDLVESMRRLGvEQIVVVSHDdeLVG 858
|
....*....
gi 556321685 201 ASrycDHLV 209
Cdd:PRK02224 859 AA---DDLV 864
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
139-227 |
1.65e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 139 LSGGQRQRAFLAMVLAQDTPLILLDEPTTYLDINHQVELMRLMVELKRQGKTVVTVLHDLNQASRYCDHLVVLASGRVM- 217
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITg 484
|
90
....*....|....
gi 556321685 218 ----AQGAPEAVMK 227
Cdd:NF040905 485 elprEEASQERIMR 498
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
27-59 |
3.31e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.76 E-value: 3.31e-03
10 20 30
....*....|....*....|....*....|....*..
gi 556321685 27 AGKITALLGPNGCGKSTLLNcfsrLLTPDS----GEI 59
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLN----ALLPELvlatGEI 116
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
22-52 |
3.62e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.99 E-value: 3.62e-03
10 20 30
....*....|....*....|....*....|.
gi 556321685 22 SLALPAGKITALLGPNGCGKSTLLNCFsRLL 52
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDAL-RFL 44
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
27-55 |
3.67e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.14 E-value: 3.67e-03
10 20
....*....|....*....|....*....
gi 556321685 27 AGKITALLGPNGCGKSTLLNcfsrLLTPD 55
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLN----ALLPE 129
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
30-59 |
4.03e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 4.03e-03
10 20 30
....*....|....*....|....*....|
gi 556321685 30 ITALLGPNGCGKSTLLNCFSRLLTPDSGEI 59
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVI 30
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
11-184 |
4.20e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 36.90 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 11 SYGAQAVLDGLSlalpagKITALLGPNGCGKSTLLN--CFsrlltpdsgeilldekpiaGFSARQLA-RRLALLPQHHls 87
Cdd:cd03239 11 SYRDETVVGGSN------SFNAIVGPNGSGKSNIVDaiCF-------------------VLGGKAAKlRRGSLLFLAG-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 88 pegitvrelvSYGRSPWLSlwGRLSAEDNERVNVAMSQtrtrnladrRLTQ-LSGGQRQRAFLAMVLA----QDTPLILL 162
Cdd:cd03239 64 ----------GGVKAGINS--ASVEITFDKSYFLVLQG---------KVEQiLSGGEKSLSALALIFAlqeiKPSPFYVL 122
|
170 180
....*....|....*....|..
gi 556321685 163 DEPTTYLDINHQVELMRLMVEL 184
Cdd:cd03239 123 DEIDAALDPTNRRRVSDMIKEM 144
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-55 |
6.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.59 E-value: 6.35e-03
10 20 30
....*....|....*....|....*....|
gi 556321685 26 PAGKITALLGPNGCGKSTLLNCFSRLLTPD 55
Cdd:COG4913 22 FDGRGTLLTGDNGSGKSTLLDAIQTLLVPA 51
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2-108 |
7.05e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 37.33 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556321685 2 RLRTENLTvSYGAQAVLDGLSLALPAGKITALLGPNGCGKSTLLNCFSRLLTPDSGEILLDEKPIAGFSARQLARRLALL 81
Cdd:COG1106 4 SFSIENFR-SFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEPSE 82
|
90 100
....*....|....*....|....*..
gi 556321685 82 PQHHLSPEGITVRELVSYGRSPWLSLW 108
Cdd:COG1106 83 FEILFLLDGVRYEYGFELDKERIISEW 109
|
|
| |
