|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
22-276 |
1.45e-99 |
|
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: 291.95 E-value: 1.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYL 101
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHTPADTAIDVRTVVALGRYAHHRRRDRfrssLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQA 181
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGR----PSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 182 KVMLFDEPTAALDIGFQLEILELLGELADE-GHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRIDAIYR 260
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYG 236
|
250
....*....|....*.
gi 896182242 261 ISSAVDTDPHTGSVRV 276
Cdd:COG1120 237 VEARVIEDPVTGRPLV 252
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-272 |
2.49e-75 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 230.39 E-value: 2.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYL 101
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHTPADTAIDVRTVVALGRYAHHRRRDRfrsslnstDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQ-- 179
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPHGSSAAQ--------DRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlw 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 180 -----QAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPR 254
Cdd:COG4559 153 epvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL 232
|
250
....*....|....*...
gi 896182242 255 IDAIYRISSAVDTDPHTG 272
Cdd:COG4559 233 LERVYGADLRVLAHPEGG 250
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-266 |
9.24e-75 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 228.43 E-value: 9.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 18 DSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAheratR 97
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR-----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 LAYLPQHTPADTA--IDVRTVVALGRYAHHRRRDRFRSSlnstDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAK 175
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRA----DREAVDEALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 176 LLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIhNGGLEVTGSAEEVLTPPRI 255
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENL 231
|
250
....*....|.
gi 896182242 256 DAIYRISSAVD 266
Cdd:COG1121 232 SRAYGGPVALL 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-272 |
3.83e-74 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 227.35 E-value: 3.83e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAY 100
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQHTPADTAIDVRTVVALGRYAHHRRRDRfrsslnstDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQ- 179
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAE--------DDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 180 -----QAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGV--VLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTP 252
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHE-RGLAVivVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
250 260
....*....|....*....|
gi 896182242 253 PRIDAIYRISSAVDTDPHTG 272
Cdd:PRK13548 232 ETLRRVYGADVLVQPHPETG 251
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-272 |
3.55e-66 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 207.17 E-value: 3.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLP 102
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPADTAIDVRTVVALGRYAHHRRRDRfrssLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLSLWGR----LSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 183 VMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRIDAIYRIS 262
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVE 238
|
250
....*....|
gi 896182242 263 SAVDTDPHTG 272
Cdd:PRK11231 239 AEIHPEPVSG 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
24-231 |
5.01e-66 |
|
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: 205.07 E-value: 5.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 24 RATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAheratRLAYLPQ 103
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 104 HTPADTA--IDVRTVVALGRYAHHRrrdrFRSSLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQA 181
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKG----LFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 896182242 182 KVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHR 231
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR 201
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
24-240 |
1.48e-64 |
|
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: 200.35 E-value: 1.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 24 RATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQ 103
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 104 htpadtaidvrtvvalgryahhrrrdrfrsslnstdhdivayALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKV 183
Cdd:cd03214 81 ------------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 184 MLFDEPTAALDIGFQLEILELLGELADE-GHGIGVVLHDLNLAARSCHRLSVIHNGGL 240
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
26-285 |
1.23e-62 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 202.76 E-value: 1.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 26 TDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHT 105
Cdd:PRK09536 7 SDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 PADTAIDVRTVVALGRYAHhrrRDRFrSSLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVML 185
Cdd:PRK09536 87 SLSFEFDVRQVVEMGRTPH---RSRF-DTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 186 FDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRIDAIYRISSAV 265
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAV 242
|
250 260
....*....|....*....|
gi 896182242 266 DTDPHTGSVRVTALARARPA 285
Cdd:PRK09536 243 GTDPATGAPTVTPLPDPDRT 262
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
23-274 |
1.47e-56 |
|
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: 182.71 E-value: 1.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLP 102
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPADTAIDVRTVVALGRYAHhrrRDRFRSSlNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIPH---RSLWAGD-SPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 183 VMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRIDAIYRIS 262
Cdd:TIGR03873 158 LLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGVD 237
|
250
....*....|..
gi 896182242 263 SAVDTDPHTGSV 274
Cdd:TIGR03873 238 ATVLTHPDTGRP 249
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
26-259 |
6.72e-53 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 172.96 E-value: 6.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 26 TDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHT 105
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 PADTAIDVRTVVALGRYAHHRRRdrfrssLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVML 185
Cdd:COG4604 85 HINSRLTVRELVAFGRFPYSKGR------LTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 186 FDEPTAALDIGFQLEILELLGELADE-GHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRIDAIY 259
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIY 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-281 |
9.95e-52 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 170.55 E-value: 9.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 17 TDSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAT 96
Cdd:PRK10253 2 TESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 97 RLAYLPQH--TPADtaIDVRTVVALGRYAHHRRRDRFRSSlnstDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIA 174
Cdd:PRK10253 82 RIGLLAQNatTPGD--ITVQELVARGRYPHQPLFTRWRKE----DEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 175 KLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADE-GHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
250 260
....*....|....*....|....*...
gi 896182242 254 RIDAIYRISSAVDTDPHTGSVRVTALAR 281
Cdd:PRK10253 236 LIERIYGLRCMIIDDPVAGTPLVVPLGR 263
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-273 |
2.63e-49 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 164.19 E-value: 2.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 14 KPDTDSTALLRATDLSVGyrNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE 93
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVP--GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 94 RATRLAYLPQHTPADTAIDVRTVVALGRYAHHRRRDRFRsslnSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFI 173
Cdd:PRK10575 83 FARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFG----AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 174 AKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGV--VLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLT 251
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE-RGLTViaVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
250 260
....*....|....*....|..
gi 896182242 252 PPRIDAIYRISSAVDTDPHTGS 273
Cdd:PRK10575 238 GETLEQIYGIPMGILPHPAGAA 259
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
21-260 |
2.64e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 158.30 E-value: 2.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE-RATR- 97
Cdd:COG3638 1 PMLELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlRRLRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 -LAYLPQHTPADTAIDVRTVVALGRYAHHRRRDRFRSSLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKL 176
Cdd:COG3638 81 rIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 177 LAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVV--LHDLNLAARSCHRLSVIHNGGLEVTGSAEEvLTPPR 254
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIARE-DGITVVvnLHQVDLARRYADRIIGLRDGRVVFDGPPAE-LTDAV 238
|
....*.
gi 896182242 255 IDAIYR 260
Cdd:COG3638 239 LREIYG 244
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
23-251 |
5.07e-47 |
|
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: 157.11 E-value: 5.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYL 101
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHtpADTAIDVRTV---VALG----RYAHHRRRDRfrsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIA 174
Cdd:COG1122 81 FQN--PDDQLFAPTVeedVAFGpenlGLPREEIRER------------VEEALELVGLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182242 175 KLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLT 251
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
23-250 |
1.98e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.61 E-value: 1.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtRLAYLP 102
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPADTAIDVRTVVAL-GRYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQA 181
Cdd:COG1131 80 QEPALYPDLTVRENLRFfARLYGLPRKEA---------RERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896182242 182 KVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-254 |
1.08e-44 |
|
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: 151.05 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR-LAYL 101
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHTPADTAIDVRTVVALGRYAHHRRRDRFRSSLNStDHDIVAYA---LDRVGVTALADRPITALSGGQRQLVFIAKLLA 178
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARRE-EREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 179 QQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPR 254
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-254 |
2.54e-43 |
|
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: 154.29 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 10 DHVTKPDTDSTALLRATDLSVGYRNR-----TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGA 84
Cdd:COG1123 248 GRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGK 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 85 PLTKLRAHER---ATRLAYLPQHtpADTAID----VRTVVALGRYAHHRRRDRFRsslnstdHDIVAYALDRVGVTA-LA 156
Cdd:COG1123 328 DLTKLSRRSLrelRRRVQMVFQD--PYSSLNprmtVGDIIAEPLRLHGLLSRAER-------RERVAELLERVGLPPdLA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 157 DRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSV 234
Cdd:COG1123 399 DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRE-LGLTYLFisHDLAVVRYIADRVAV 477
|
250 260
....*....|....*....|
gi 896182242 235 IHNGGLEVTGSAEEVLTPPR 254
Cdd:COG1123 478 MYDGRIVEDGPTEEVFANPQ 497
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-254 |
3.03e-43 |
|
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: 148.03 E-value: 3.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGY----RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR 97
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 LAYLPQHtpADTAID----VRTVVALGRYAHHRRRDRFRsslnstdhdiVAYALDRVGVT-ALADRPITALSGGQRQLVF 172
Cdd:COG1124 81 VQMVFQD--PYASLHprhtVDRILAEPLRIHGLPDREER----------IAELLEQVGLPpSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 173 IAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREE-RGLTYLFvsHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
....
gi 896182242 251 TPPR 254
Cdd:COG1124 228 AGPK 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
31-232 |
3.33e-43 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 145.84 E-value: 3.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 31 GYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVellgapltklrAHERATRLAYLPQHTPADTA 110
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 111 --IDVRTVVALGRYAHHRRRDRfrssLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDE 188
Cdd:NF040873 70 lpLTVRDLVAMGRWARRGLWRR----LTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896182242 189 PTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRL 232
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-262 |
1.18e-42 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 146.52 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRnrtvVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIvTPSSGQVELLGAPLTKLRAHERATRLAYLP 102
Cdd:COG4138 1 LQLNDVAVAGR----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPADTAIDVRTVVALGRYAHHRRrdrfrsslnSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQ--- 179
Cdd:COG4138 76 QQQSPPFAMPVFQYLALHQPAGASS---------EAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 180 ----QAKVMLFDEPTAALDIGFQLEILELLGELADEghGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:COG4138 147 tinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQ--GITVVMssHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPE 224
|
....*....
gi 896182242 254 RIDAIYRIS 262
Cdd:COG4138 225 NLSEVFGVK 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
27-238 |
6.22e-42 |
|
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: 143.38 E-value: 6.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGY--RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQH 104
Cdd:cd03225 4 NLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 tPAD--TAIDVRTVVALGRYAHHRRRDrfrsslnsTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:cd03225 84 -PDDqfFGPTVEEEVAFGLENLGLPEE--------EIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 183 VMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
22-250 |
1.22e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 141.15 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtRLAYL 101
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQhtpadtaidvrtvvALGRYAHHRRRD--RFRSSLNSTDHDIVAYALDRV----GVTALADRPITALSGGQRQLVFIAK 175
Cdd:COG4555 80 PD--------------ERGLYDRLTVREniRYFAELYGLFDEELKKRIEELiellGLEEFLDRRVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 176 LLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-257 |
5.72e-40 |
|
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: 139.79 E-value: 5.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERA--- 95
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 96 -------TRLayLPQHTpadtaidVRTVVALGryAHHRRRDRFRSSLNSTD---------HDIVAYALDRVGVTALADRP 159
Cdd:COG0411 81 iartfqnPRL--FPELT-------VLENVLVA--AHARLGRGLLAALLRLPrarreereaRERAEELLERVGLADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 160 ITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHN 237
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDE-RGITILLieHDMDLVMGLADRIVVLDF 228
|
250 260
....*....|....*....|.
gi 896182242 238 GGLEVTGSAEEVLTPPR-IDA 257
Cdd:COG0411 229 GRVIAEGTPAEVRADPRvIEA 249
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
21-194 |
1.32e-39 |
|
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: 137.23 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtRLAY 100
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRR-RLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQHTPADTAIDVRTVVALGRYAHHRRRDRFRsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQ 180
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADREA----------IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170
....*....|....
gi 896182242 181 AKVMLFDEPTAALD 194
Cdd:COG4133 150 APLWLLDEPFTALD 163
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-278 |
3.94e-39 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 138.04 E-value: 3.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPS--------SGQVELLGAPLTKLRAHE 93
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 94 RATRLAYLPQHTPADTAIDVRTVVALGRYAHHRRrdrfRSSLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFI 173
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARR----AGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 174 AKLLAQ---------QAKVMLFDEPTAALDIGFQLEILELLGELADEGH-GIGVVLHDLNLAARSCHRLSVIHNGGLEVT 243
Cdd:PRK13547 157 ARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 896182242 244 GSAEEVLTPPRIDAIYRIS-SAVDTDPHTGSVRVTA 278
Cdd:PRK13547 237 GAPADVLTPAHIARCYGFAvRLVDAGDGVPPVIVPA 272
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
23-259 |
1.96e-38 |
|
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: 135.00 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE-RATR--L 98
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlRQLRrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQHTPADTAIDVRTVVALGRYAhhrRRDRFRSSLNS-TDHDIVA--YALDRVGVTALADRPITALSGGQRQLVFIAK 175
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLG---RRSTWRSLFGLfPKEEKQRalAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 176 LLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVV--LHDLNLAARSCHRLSVIHNGGLEVTGSAEEvLTPP 253
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINRE-EGITVIvsLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDE 235
|
....*.
gi 896182242 254 RIDAIY 259
Cdd:cd03256 236 VLDEIY 241
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
24-238 |
2.18e-38 |
|
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: 132.37 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 24 RATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQ 103
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 104 htpadtaidvrtvvalgryahhrrrdrfrsslnstdhdivayaldrvgvtaladrpitaLSGGQRQLVFIAKLLAQQAKV 183
Cdd:cd00267 81 -----------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 184 MLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
27-255 |
5.65e-38 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 133.78 E-value: 5.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHER---ATRLAYLPQ 103
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 104 HTPADTAIDVRTVVALGRYAHHRRRDRFRSslnstdhDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKV 183
Cdd:cd03261 85 SGALFDSLTVFENVAFPLREHTRLSEEEIR-------EIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 184 MLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVL--TPPRI 255
Cdd:cd03261 158 LLYDEPTAGLDpIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPLV 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
22-260 |
6.62e-38 |
|
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: 133.96 E-value: 6.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE----RAt 96
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 97 RLAYLPQHTPADTAIDVRTVVALGRYAHHrrrDRFRSSLN---STDHDIVAYALDRVGVTALADRPITALSGGQRQLVFI 173
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENVLHGRLGYK---PTWRSLLGrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 174 AKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVV--LHDLNLAARSCHRLSVIHNGGLEVTGSAEEvLT 251
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKE-DGITVIinLHQVDLAKKYADRIVGLKAGEIVFDGAPSE-LD 234
|
....*....
gi 896182242 252 PPRIDAIYR 260
Cdd:TIGR02315 235 DEVLRHIYG 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-254 |
9.56e-38 |
|
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: 139.27 E-value: 9.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 20 TALLRATDLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPS---SGQVELLGAPLTKLRAHER 94
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 95 ATRLAYLPQHtpADTAIDVRTV---VALGRYAHHRRRDRFRsslnstdhDIVAYALDRVGVTALADRPITALSGGQRQLV 171
Cdd:COG1123 82 GRRIGMVFQD--PMTQLNPVTVgdqIAEALENLGLSRAEAR--------ARVLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 172 FIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEV 249
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRE-RGTTVLLitHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
....*
gi 896182242 250 LTPPR 254
Cdd:COG1123 231 LAAPQ 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
23-240 |
1.08e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.25 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLP 102
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTP--ADTaidVRTVVALGRYAHHRRRDRfrsslnstdhDIVAYALDRVGVTA-LADRPITALSGGQRQLVFIAKLLAQ 179
Cdd:COG4619 81 QEPAlwGGT---VRDNLPFPFQLRERKFDR----------ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896182242 180 QAKVMLFDEPTAALDIG-FQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGL 240
Cdd:COG4619 148 QPDVLLLDEPTSALDPEnTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
38-191 |
8.49e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 128.15 E-value: 8.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHTPADTAIDVRTVV 117
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 118 ALGRYAHHRRRDRFRsslnstdhDIVAYALDRVGVTALADRPI----TALSGGQRQLVFIAKLLAQQAKVMLFDEPTA 191
Cdd:pfam00005 81 RLGLLLKGLSKREKD--------ARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
22-238 |
1.40e-36 |
|
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: 129.93 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNR----TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR 97
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 ---LAYLPQHtpADTAID----VRTVVALGRYAHHRRRDRFRSSLnstdhdIVAYALDRVG-VTALADRPITALSGGQRQ 169
Cdd:cd03257 81 rkeIQMVFQD--PMSSLNprmtIGEQIAEPLRIHGKLSKKEARKE------AVLLLLVGVGlPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 170 LVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNG 238
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEE-LGLTLLFitHDLGVVAKIADRVAVMYAG 222
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
43-269 |
2.39e-36 |
|
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: 129.20 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 43 LAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHeratrLAYLPQ-HTPA-DTAIDVRTVVALG 120
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRH-----IGYVPQrHEFAwDFPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 121 RYAH---HRRRDRfrsslnsTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGF 197
Cdd:TIGR03771 76 RTGHigwLRRPCV-------ADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896182242 198 QLEILELLGELADEGHGIGVVLHDLNLAARSCHRLsVIHNGGLEVTGSAEEVLTPPRIDAIYRISsavDTDP 269
Cdd:TIGR03771 149 QELLTELFIELAGAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDPAPWMTTFGVS---DSSP 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-250 |
1.92e-35 |
|
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: 126.78 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR-LAYL 101
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHTPADTAIDVRTVVALGRYAhhRRRDRFRSSLNStdhdivAYALdrvgVTALADR---PITALSGGQRQLVFIAKLLA 178
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYA--RRRAKRKARLER------VYEL----FPRLKERrkqLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896182242 179 QQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-257 |
1.68e-34 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 124.71 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 18 DSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERA-- 95
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 96 -TRLAYLPQHtpadTA-IDVRTV---VALGRYAHHRRRDRFRsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQL 170
Cdd:COG1127 81 rRRIGMLFQG----GAlFDSLTVfenVAFPLREHTDLSEAEI-------RELVLEKLELVGLPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALD-IGfqleilellgelAD----------EGHGIGVVL--HDLNLAARSCHRLSVIHN 237
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDpIT------------SAvidelirelrDELGLTSVVvtHDLDSAFAIADRVAVLAD 217
|
250 260
....*....|....*....|..
gi 896182242 238 GGLEVTGSAEEVL--TPPRIDA 257
Cdd:COG1127 218 GKIIAEGTPEELLasDDPWVRQ 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
23-240 |
2.66e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 122.51 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtRLAYLP 102
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHtpadtaidvrtvvalgryahhrrrDRFRSSLNSTDHdivayaLDrvgvtaladrpitaLSGGQRQLVFIAKLLAQQAK 182
Cdd:cd03230 80 EE------------------------PSLYENLTVREN------LK--------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 183 VMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGL 240
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-259 |
7.51e-34 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 123.50 E-value: 7.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRnrtvVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIvTPSSGQVELLGAPLTKLRAHERATRLAYLP 102
Cdd:PRK03695 1 MQLNDVAVSTR----LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPADTAIDVRTVVALGRYAHHRRRDrfrsslnstDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQ--- 179
Cdd:PRK03695 76 QQQTPPFAMPVFQYLTLHQPDKTRTEA---------VASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 180 ----QAKVMLFDEPTAALDIGFQLEILELLGELAdeGHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:PRK03695 147 dinpAGQLLLLDEPMNSLDVAQQAALDRLLSELC--QQGIAVVMssHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
....*.
gi 896182242 254 RIDAIY 259
Cdd:PRK03695 225 NLAQVF 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-259 |
1.22e-33 |
|
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: 122.40 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 20 TALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR-L 98
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQHtpadtaidvR------TV---VALGRYAHHRRRDRfrsslnstdHDIVAYALDRVGVtaLADR---PITALSGG 166
Cdd:COG0410 81 GYVPEG---------RrifpslTVeenLLLGAYARRDRAEV---------RADLERVYELFPR--LKERrrqRAGTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 167 QRQLVFIAKLLAQQAKVMLFDEPTAAL------DIGfqleilELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGL 240
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGLapliveEIF------EIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRI 214
|
250
....*....|....*....
gi 896182242 241 EVTGSAEEVLTPPRIDAIY 259
Cdd:COG0410 215 VLEGTAAELLADPEVREAY 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
23-244 |
7.62e-33 |
|
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: 119.93 E-value: 7.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERatRLAYLP 102
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR--NIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPADTAIDVRTVVALGRYAHHRRRDRFRsslnstdhDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIR--------ARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896182242 183 VMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTG 244
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRE-LGITTIYvtHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
17-194 |
1.45e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.19 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 17 TDSTALLRATDLSVGYRNR----TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAh 92
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 93 eratRLAYLPQHtpaDTAIDVRTV---VALG-RYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQR 168
Cdd:COG1116 81 ----DRGVVFQE---PALLPWLTVldnVALGlELRGVPKAER---------RERARELLELVGLAGFEDAYPHQLSGGMR 144
|
170 180
....*....|....*....|....*.
gi 896182242 169 QLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALD 170
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
20-241 |
2.22e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.99 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 20 TALLRATDLSVGYRN----RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKL----RA 91
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLsereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 92 HERATRLAYLPQHT---PADTAIDVrtvVALG-RYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQ 167
Cdd:COG1136 82 RLRRRHIGFVFQFFnllPELTALEN---VALPlLLAGVSRKER---------RERARELLERVGLGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 168 RQLVFIAKLLAQQAKVMLFDEPTAALDigfqleilellGELADE----------GHGIGVVL--HDLNLAARsCHRLSVI 235
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLD-----------SKTGEEvlellrelnrELGTTIVMvtHDPELAAR-ADRVIRL 217
|
....*.
gi 896182242 236 HNGGLE 241
Cdd:COG1136 218 RDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
23-238 |
2.25e-32 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 118.75 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRN----RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKL----RAHER 94
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 95 ATRLAYLPQHTpadTAIDVRTV---VALG-RYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQL 170
Cdd:cd03255 81 RRHIGFVFQSF---NLLPDLTAlenVELPlLLAGVPKKER---------RERAEELLERVGLGDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALD---------IGFQleilellgELADEGHGIGVVLHDLNLAARsCHRLSVIHNG 238
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDsetgkevmeLLRE--------LNKEAGTTIVVVTHDPELAEY-ADRIIELRDG 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
23-240 |
5.10e-32 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 117.68 E-value: 5.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGeVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtRLAYLP 102
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRR-RIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QH---TPADTAID-VRTVVALGRYAHHRRRDRfrsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLA 178
Cdd:cd03264 79 QEfgvYPNFTVREfLDYIAWLKGIPSKEVKAR------------VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896182242 179 QQAKVMLFDEPTAALDIGfQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGL 240
Cdd:cd03264 147 GDPSILIVDEPTAGLDPE-ERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
19-194 |
9.41e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 120.20 E-value: 9.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERatRL 98
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR--NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQ------HTpadtaidvrTV---VALG-RYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQR 168
Cdd:COG3842 80 GMVFQdyalfpHL---------TVaenVAFGlRMRGVPKAEI---------RARVAELLELVGLEGLADRYPHQLSGGQQ 141
|
170 180
....*....|....*....|....*.
gi 896182242 169 QLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALD 167
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
23-194 |
1.43e-31 |
|
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: 116.80 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNR----TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHeratrL 98
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQHtpaDTAIDVRTV---VALG-RYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQLVFIA 174
Cdd:cd03293 76 GYVFQQ---DALLPWLTVldnVALGlELQGVPKAEA---------RERAEELLELVGLSGFENAYPHQLSGGMRQRVALA 143
|
170 180
....*....|....*....|
gi 896182242 175 KLLAQQAKVMLFDEPTAALD 194
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALD 163
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
22-254 |
2.69e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 116.25 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERA--TRLA 99
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPQ------HtpadtaidvRTV---VALG-RYAHHRRRDrfrsslnstdhDIVAYA---LDRVGVTALADRPITALSGG 166
Cdd:COG1126 81 MVFQqfnlfpH---------LTVlenVTLApIKVKKMSKA-----------EAEERAmelLERVGLADKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 167 QRQLVFIAKLLAQQAKVMLFDEPTAALD----------IgfqleilellGELADEGHGIGVVLHDLNLAARSCHRLSVIH 236
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDpelvgevldvM----------RDLAKEGMTMVVVTHEMGFAREVADRVVFMD 210
|
250
....*....|....*...
gi 896182242 237 NGGLEVTGSAEEVLTPPR 254
Cdd:COG1126 211 GGRIVEEGPPEEFFENPQ 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
25-195 |
3.45e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 121.33 E-value: 3.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 25 ATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELlgapltklrahERATRLAYLPQH 104
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----------PKGLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 TPADTAIDVRTVVALG---RYAHHRRRDRFRSSLNSTDHDIVAYA---------------------LDRVGVT-ALADRP 159
Cdd:COG0488 70 PPLDDDLTVLDTVLDGdaeLRALEAELEELEAKLAEPDEDLERLAelqeefealggweaearaeeiLSGLGFPeEDLDRP 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 896182242 160 ITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
23-259 |
3.57e-31 |
|
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: 116.10 E-value: 3.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR-LAYL 101
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHTPADTAIDVR-TVVALGRYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQ 180
Cdd:cd03218 81 PQEASIFRKLTVEeNILAVLEIRGLSKKER---------EEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 181 AKVMLFDEPTAALD-IGFQLEILELLGELAdegHGIGVVLHDLNlaARS----CHRLSVIHNGGLEVTGSAEEVLTPPRI 255
Cdd:cd03218 152 PKFLLLDEPFAGVDpIAVQDIQKIIKILKD---RGIGVLITDHN--VREtlsiTDRAYIIYEGKVLAEGTPEEIAANELV 226
|
....
gi 896182242 256 DAIY 259
Cdd:cd03218 227 RKVY 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
42-258 |
1.13e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.47 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 42 NLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtrLAYLPQ------HtpadtaIDVRT 115
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP--VSMLFQennlfpH------LTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 116 VVALGRyahhrrRDRFRssLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:COG3840 91 NIGLGL------RPGLK--LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 196 GFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRIDAI 258
Cdd:COG3840 163 ALRQEMLDLVDELCRE-RGLTVLMvtHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
21-250 |
2.72e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.97 E-value: 2.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR-LA 99
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPQH-------TPADtaiDVRTVVALGRYAHHRRRDRfrsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVF 172
Cdd:COG1137 82 YLPQEasifrklTVED---NILAVLELRKLSKKEREER------------LEELLEEFGITHLRKSKAYSLSGGERRRVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 173 IAKLLAQQAKVMLFDEPTAALD-IGfqleilellgeLAD--------EGHGIGVVLHDLNlaARS----CHRLSVIHNGG 239
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDpIA-----------VADiqkiirhlKERGIGVLITDHN--VREtlgiCDRAYIISEGK 213
|
250
....*....|.
gi 896182242 240 LEVTGSAEEVL 250
Cdd:COG1137 214 VLAEGTPEEIL 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-250 |
4.29e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 118.71 E-value: 4.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 9 TDHVTKPDTDSTALlRATDLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLT 87
Cdd:COG4988 324 AGTAPLPAAGPPSI-ELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 88 KLRAHERATRLAYLPQHT--PADTaidVRTVVALGRyahhrrrdrfrssLNSTDHDIVAyALDRVGVTALADR------- 158
Cdd:COG4988 403 DLDPASWRRQIAWVPQNPylFAGT---IRENLRLGR-------------PDASDEELEA-ALEAAGLDEFVAAlpdgldt 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 159 PI----TALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELAdEGHGIGVVLHDLNLAARSCHRLsV 234
Cdd:COG4988 466 PLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRIL-V 543
|
250
....*....|....*.
gi 896182242 235 IHNGGLEVTGSAEEVL 250
Cdd:COG4988 544 LDDGRIVEQGTHEELL 559
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
24-238 |
4.94e-30 |
|
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: 112.35 E-value: 4.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 24 RATDLSVGY-RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLtklRAHERATRLAYLP 102
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTpaDTAIDVRTVvalgryahhRRRDRFRSSLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:cd03226 78 QDV--DYQLFTDSV---------REELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 183 VMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
23-265 |
2.37e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.70 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPL-TKLRAHERatRLAYL 101
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER--RVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQH-------TpadtaidVRTVVALGryAHHRRRDRfrsslnSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIA 174
Cdd:COG1118 81 FQHyalfphmT-------VAENIAFG--LRVRPPSK------AEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 175 KLLAQQAKVMLFDEPTAALDigfqleilellgelA--------------DEGHGIGV-VLHDLNLAARSCHRLSVIHNGG 239
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALD--------------AkvrkelrrwlrrlhDELGGTTVfVTHDQEEALELADRVVVMNQGR 211
|
250 260
....*....|....*....|....*.
gi 896182242 240 LEVTGSAEEVLTPPRIDAIYRISSAV 265
Cdd:COG1118 212 IEQVGTPDEVYDRPATPFVARFLGCV 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
36-253 |
4.43e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.57 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 36 TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLA--------YL-PQHTP 106
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEagmvfqqfYLfPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 107 ADTaidvrtvVALGRYahhrrrdRFRSSLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLF 186
Cdd:PRK09493 95 LEN-------VMFGPL-------RVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182242 187 DEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
31-254 |
6.46e-29 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 109.98 E-value: 6.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 31 GYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE-RATR--LAYLPQHTPA 107
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElRKARrrIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 108 DTAIDVRTVVALG-RYAHHRRRDRFRSslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLF 186
Cdd:cd03258 94 LSSRTVFENVALPlEIAGVPKAEIEER---------VLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 187 DEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPR 254
Cdd:cd03258 165 DEATSALDPETTQSILALLRDINRE-LGLTIVLitHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
23-194 |
2.67e-28 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 108.00 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR--LAY 100
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQHT---PADTAIDVrtvVALG-RYAHHRRRDRFRsslnstdhDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKL 176
Cdd:cd03262 81 VFQQFnlfPHLTVLEN---ITLApIKVKGMSKAEAE--------ERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170
....*....|....*...
gi 896182242 177 LAQQAKVMLFDEPTAALD 194
Cdd:cd03262 150 LAMNPKVMLFDEPTSALD 167
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
23-249 |
2.78e-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: 108.38 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR-LAYL 101
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHTPADTAIDVRTVVALGRYAHHRRrdrfrsslnstDHDIVAYALDRVGV-TALADRPITALSGGQRQLVFIAKLLAQQ 180
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRR-----------SRKIPDEIYELFPVlKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182242 181 AKVMLFDEPTAAL------DIGfqleilELLGELADEGhGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEV 249
Cdd:TIGR03410 150 PKLLLLDEPTEGIqpsiikDIG------RVIRRLRAEG-GMAILLveQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
23-238 |
2.84e-28 |
|
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: 107.75 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHeratRLAYLP 102
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHT---PADTAIDVrtVVALGRYAHHRRRDRFRSSLnstdhdivaYALDRVGVTALADRPITALSGGQRQLV-FIAKLLa 178
Cdd:cd03269 77 EERglyPKMKVIDQ--LVYLAQLKGLKKEEARRRID---------EWLERLELSEYANKRVEELSKGNQQKVqFIAAVI- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 179 QQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-255 |
5.41e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.03 E-value: 5.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHErATR- 97
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 --------LAYLPQhtpadtaidvRTV---VALGRYAHHRRRDRFRSSlnstdHDIVAYALDRVGVTALADRPITALSGG 166
Cdd:COG1129 80 giaiihqeLNLVPN----------LSVaenIFLGREPRRGGLIDWRAM-----RRRARELLARLGLDIDPDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 167 QRQLVFIAKLLAQQAKVMLFDEPTAALDigfqleilellgelADE------------GHGIGVVL--HDLNLAARSCHRL 232
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLT--------------EREverlfriirrlkAQGVAIIYisHRLDEVFEIADRV 210
|
250 260
....*....|....*....|...
gi 896182242 233 SVIHNGGLEVTGSAEEvLTPPRI 255
Cdd:COG1129 211 TVLRDGRLVGTGPVAE-LTEDEL 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-267 |
6.12e-28 |
|
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: 108.50 E-value: 6.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 18 DSTALLRATDLSVGYRNrtvvsgVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE-RAT 96
Cdd:cd03294 26 SKEEILKKTGQTVGVND------VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElREL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 97 R----------LAYLPQHTpadtaidVRTVVALG-RYAHHRRRDRFRSSLNstdhdivayALDRVGVTALADRPITALSG 165
Cdd:cd03294 100 RrkkismvfqsFALLPHRT-------VLENVAFGlEVQGVPRAEREERAAE---------ALELVGLEGWEHKYPDELSG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 166 GQRQLVFIAKLLAQQAKVMLFDEPTAALD----IGFQleiLELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLE 241
Cdd:cd03294 164 GMQQRVGLARALAVDPDILLMDEAFSALDplirREMQ---DELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|....*.
gi 896182242 242 VTGSAEEVLTPPRIDAIYRISSAVDT 267
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFFRGVDR 266
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
23-238 |
9.86e-28 |
|
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: 105.35 E-value: 9.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERA--TRLAY 100
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQHTPADTAIDVRTVVALGryahhrrrdrfrsslnstdhdivayaldrvgvtaladrpitaLSGGQRQLVFIAKLLAQQ 180
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 896182242 181 AKVMLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:cd03229 119 PDVLLLDEPTSALDpITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
27-259 |
1.64e-27 |
|
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: 106.65 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYlpQHTP 106
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF--QHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 107 ADTAIDVRTVVALGRYAHHRRRDRFRSSLNSTDHDIvayaLDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLF 186
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHEL----LKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896182242 187 DEPTAALDIGFQLEILELLGELADEGHGIGV-VLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRIDAIY 259
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVfVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVY 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
23-249 |
2.16e-27 |
|
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: 105.73 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIV-----TPSSGQVELLGAPLTKLRAH--ERA 95
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 96 TRLAYLPQH-TPADTAIdvRTVVALGRYAHHRRRDRFRsslnstdHDIVAYALDRVGVTALADRPITA--LSGGQRQLVF 172
Cdd:cd03260 81 RRVGMVFQKpNPFPGSI--YDNVAYGLRLHGIKLKEEL-------DERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182242 173 IAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEV 249
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-247 |
2.46e-27 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 106.89 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRaheRATR 97
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 LAYLPQHTPADTA--IDVRTVVALGRYAHHRRRDRFRSSlnstDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAK 175
Cdd:PRK15056 80 VAYVPQSEEVDWSfpVLVEDVVMMGRYGHMGWLRRAKKR----DRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182242 176 LLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCH-----RLSVIHNGGLEVTGSAE 247
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDytvmvKGTVLASGPTETTFTAE 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-194 |
5.06e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 105.71 E-value: 5.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGY----RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAhERAT 96
Cdd:COG4525 2 SMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 97 RL---AYLPQhtpadtaIDVRTVVALG-RYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQLVF 172
Cdd:COG4525 81 VFqkdALLPW-------LNVLDNVAFGlRLRGVPKAER---------RARAEELLALVGLADFARRRIWQLSGGMRQRVG 144
|
170 180
....*....|....*....|..
gi 896182242 173 IAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALD 166
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
27-250 |
7.20e-27 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 109.92 E-value: 7.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNRT--VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQH 104
Cdd:COG2274 478 NVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 TP--ADTaidVRTVVALGRyahhrrrdrfrssLNSTDHDIVAyALDRVGVTALA-------DRPI----TALSGGQRQLV 171
Cdd:COG2274 558 VFlfSGT---IRENITLGD-------------PDATDEEIIE-AARLAGLHDFIealpmgyDTVVgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 172 FIAKLLAQQAKVMLFDEPTAALDigfQLEILELLGELADEGHGIGVVL--HDLNLaARSCHRLSVIHNGGLEVTGSAEEV 249
Cdd:COG2274 621 AIARALLRNPRILILDEATSALD---AETEAIILENLRRLLKGRTVIIiaHRLST-IRLADRIIVLDKGRIVEDGTHEEL 696
|
.
gi 896182242 250 L 250
Cdd:COG2274 697 L 697
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-227 |
3.33e-26 |
|
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: 107.37 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRT-VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYL 101
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHtPADTAIDVRTVVALGRyahhrrrdrfrssLNSTDHDIVAyALDRVGV-TALADRPI----------TALSGGQRQL 170
Cdd:TIGR02857 402 PQH-PFLFAGTIAENIRLAR-------------PDASDAEIRE-ALERAGLdEFVAALPQgldtpigeggAGLSGGQAQR 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELAdEGHGIGVVLHDLNLAAR 227
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL 522
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
21-194 |
3.49e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.16 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERatRLAY 100
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR--NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQ------HTpadtaidvrTV---VALG-RYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQL 170
Cdd:COG3839 80 VFQsyalypHM---------TVyenIAFPlKLRKVPKAEI---------DRRVREAAELLGLEDLLDRKPKQLSGGQRQR 141
|
170 180
....*....|....*....|....
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
32-194 |
7.63e-26 |
|
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: 101.93 E-value: 7.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 32 YRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYlpQHTPADTAI 111
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVF--QNYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 112 DVRTVVALGRyahhRRRDRFRSSLNSTdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTA 191
Cdd:cd03300 88 TVFENIAFGL----RLKKLPKAEIKER----VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
...
gi 896182242 192 ALD 194
Cdd:cd03300 160 ALD 162
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-196 |
1.13e-25 |
|
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: 101.70 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 20 TALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQ-VELLGAPLTKLRAHERATRL 98
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AY----LPQHTPADTAidVRTVVALGRYAHHRRRDRFrsslNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIA 174
Cdd:COG1119 81 GLvspaLQLRFPRDET--VLDVVLSGFFDSIGLYREP----TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180
....*....|....*....|..
gi 896182242 175 KLLAQQAKVMLFDEPTAALDIG 196
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLG 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-254 |
3.22e-25 |
|
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: 104.38 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 15 PDTDSTALLRATDLSVGYR------NRTV-----VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVtPSSGQVELLG 83
Cdd:COG4172 268 VPPDAPPLLEARDLKVWFPikrglfRRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 84 APLTKLRAHE-RATR----------LAYL-PQHTpadtaidVRTVVALGRYAHHR------RRDRfrsslnstdhdiVAY 145
Cdd:COG4172 347 QDLDGLSRRAlRPLRrrmqvvfqdpFGSLsPRMT-------VGQIIAEGLRVHGPglsaaeRRAR------------VAE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 146 ALDRVGVT-ALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDL 222
Cdd:COG4172 408 ALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRE-HGLAYLFisHDL 486
|
250 260 270
....*....|....*....|....*....|....
gi 896182242 223 NLAARSCHRLSVIHNGglEV--TGSAEEVLTPPR 254
Cdd:COG4172 487 AVVRALAHRVMVMKDG--KVveQGPTEQVFDAPQ 518
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-194 |
3.30e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.93 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHTPADTAIDVr 114
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMGTAPSM- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 115 TV-----VALGRyahHRRRdRFRSSLNSTDHDIVAYALDRVGVtALADR---PITALSGGQRQLVfiAKLLA--QQAKVM 184
Cdd:COG1101 98 TIeenlaLAYRR---GKRR-GLRRGLTKKRRELFRELLATLGL-GLENRldtKVGLLSGGQRQAL--SLLMAtlTKPKLL 170
|
170
....*....|
gi 896182242 185 LFDEPTAALD 194
Cdd:COG1101 171 LLDEHTAALD 180
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-254 |
3.89e-25 |
|
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: 102.05 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGY--RNRTV--VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTP---SSGQVELLGAPLTKLRAHE- 93
Cdd:COG0444 1 LLEVRNLKVYFptRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 94 ---RATRLAYLPQHtpADTAID-VRTV---VALGRYAHHR--RRDRfrsslnstdHDIVAYALDRVGVTALADR----Pi 160
Cdd:COG0444 81 rkiRGREIQMIFQD--PMTSLNpVMTVgdqIAEPLRIHGGlsKAEA---------RERAIELLERVGLPDPERRldryP- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 161 TALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQleilellgelAD---------EGHGIGVVL--HDLNLAARSC 229
Cdd:COG0444 149 HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQ----------AQilnllkdlqRELGLAILFitHDLGVVAEIA 218
|
250 260
....*....|....*....|....*..
gi 896182242 230 HRLSVIHNGglEV--TGSAEEVLTPPR 254
Cdd:COG0444 219 DRVAVMYAG--RIveEGPVEELFENPR 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-195 |
4.77e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.99 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVElLGAPLtklraheratRLAYL 101
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHT----PADTAIDVrtvvaLGRYAHhrrrdrfrsslNSTDHDIVAYaLDRVGVT-ALADRPITALSGGQRQLVFIAKL 176
Cdd:COG0488 384 DQHQeeldPDKTVLDE-----LRDGAP-----------GGTEQEVRGY-LGRFLFSgDDAFKPVGVLSGGEKARLALAKL 446
|
170
....*....|....*....
gi 896182242 177 LAQQAKVMLFDEPTAALDI 195
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDI 465
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
27-196 |
5.03e-25 |
|
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: 104.56 E-value: 5.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQh 104
Cdd:TIGR03375 468 NVSFAYPGqeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQ- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 tpaDTAI---DVRTVVALGRyahhrrrdrfrssLNSTDHDIVAyALDRVGVTALA-------DRPIT----ALSGGQRQL 170
Cdd:TIGR03375 547 ---DPRLfygTLRDNIALGA-------------PYADDEEILR-AAELAGVTEFVrrhpdglDMQIGergrSLSGGQRQA 609
|
170 180
....*....|....*....|....*.
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALDIG 196
Cdd:TIGR03375 610 VALARALLRDPPILLLDEPTSAMDNR 635
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
17-254 |
5.46e-25 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 100.26 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 17 TDSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLtKLRAHERAT 96
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPDRDGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 97 RlaylpqhTPADtaidvrtvvalgryahHRRRDRFRSSL-------NSTDH--------------------DIVAYA--- 146
Cdd:COG4598 82 L-------VPAD----------------RRQLQRIRTRLgmvfqsfNLWSHmtvlenvieapvhvlgrpkaEAIERAeal 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 147 LDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAA 226
Cdd:COG4598 139 LAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFAR 218
|
250 260
....*....|....*....|....*...
gi 896182242 227 RSCHRLSVIHNGGLEVTGSAEEVLTPPR 254
Cdd:COG4598 219 DVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
23-194 |
7.26e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.97 E-value: 7.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHEratrLAYL 101
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE----IPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHtpadtaIDV----------RTV---VALG-RYAHHRRRDRFRSslnstdhdiVAYALDRVGVTALADRPITALSGGQ 167
Cdd:COG2884 78 RRR------IGVvfqdfrllpdRTVyenVALPlRVTGKSRKEIRRR---------VREVLDLVGLSDKAKALPHELSGGE 142
|
170 180
....*....|....*....|....*..
gi 896182242 168 RQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLD 169
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
35-196 |
9.45e-25 |
|
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: 98.82 E-value: 9.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHtPADTAIDVR 114
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQD-VTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 115 TVVALGRyahhrrrdrfrssLNSTDHDIVAyALDRVGVTALA-------DRPI----TALSGGQRQLVFIAKLLAQQAKV 183
Cdd:cd03245 96 DNITLGA-------------PLADDERILR-AAELAGVTDFVnkhpnglDLQIgergRGLSGGQRQAVALARALLNDPPI 161
|
170
....*....|...
gi 896182242 184 MLFDEPTAALDIG 196
Cdd:cd03245 162 LLLDEPTSAMDMN 174
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
27-254 |
1.89e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.54 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNR----TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE-RATR--LA 99
Cdd:COG1135 6 NLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElRAARrkIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPQHtpaDTAIDVRTV---VALG-RYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAK 175
Cdd:COG1135 86 MIFQH---FNLLSSRTVaenVALPlEIAGVPKAEI---------RKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 176 LLAQQAKVMLFDEPTAALD-------------IgfqleilellgelADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGL 240
Cdd:COG1135 154 ALANNPKVLLCDEATSALDpettrsildllkdI-------------NRE-LGLTIVLitHEMDVVRRICDRVAVLENGRI 219
|
250
....*....|....
gi 896182242 241 EVTGSAEEVLTPPR 254
Cdd:COG1135 220 VEQGPVLDVFANPQ 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
23-245 |
3.53e-24 |
|
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: 97.19 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtRLAY 100
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQ-SLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQHTPADTAIDVRTVVALgrYAhhrrrdRFRSSLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQ 180
Cdd:cd03263 80 CPQFDALFDELTVREHLRF--YA------RLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182242 181 AKVMLFDEPTAALDIgfqLEILELLGELADEGHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGS 245
Cdd:cd03263 152 PSVLLLDEPTSGLDP---ASRRAIWDLILEVRKGRSIILttHSMDEAEALCDRIAIMSDGKLRCIGS 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-248 |
6.11e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 96.73 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 18 DSTALLRATDLSVGYRNR----TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKL---- 89
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 90 RAHERATRLAYLPQH---TPADTAID-VRTVVALGRYAHHRRRDRfrsslnstdhdivaYALDRVGVTALAD-RPITaLS 164
Cdd:COG4181 84 RARLRARHVGFVFQSfqlLPTLTALEnVMLPLELAGRRDARARAR--------------ALLERVGLGHRLDhYPAQ-LS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 165 GGQRQLVFIAKLLAQQAKVMLFDEPTAALDigfqleilellgelADEGHGI-----------GVVL----HDLNLAARsC 229
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLD--------------AATGEQIidllfelnrerGTTLvlvtHDPALAAR-C 213
|
250
....*....|....*....
gi 896182242 230 HRLSVIHNGGLEVTGSAEE 248
Cdd:COG4181 214 DRVLRLRAGRLVEDTAATA 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
23-194 |
6.71e-24 |
|
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: 95.14 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGY--RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAY 100
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQHTPadtaidvrtvvalgryahhrrrdRFRSSlnstdhdiVAYALdrvgvtaladrpitaLSGGQRQLVFIAKLLAQQ 180
Cdd:cd03228 81 VPQDPF-----------------------LFSGT--------IRENI---------------LSGGQRQRIAIARALLRD 114
|
170
....*....|....
gi 896182242 181 AKVMLFDEPTAALD 194
Cdd:cd03228 115 PPILILDEATSALD 128
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-254 |
1.04e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.96 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERA------- 95
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 96 ------TRLAYLPQH-------TPADTAIDVrTVVALGrYAHHRRRDRfrsslnstdhdIVAYaLDRVGVTALA-DRPIT 161
Cdd:PRK10619 86 qlrllrTRLTMVFQHfnlwshmTVLENVMEA-PIQVLG-LSKQEARER-----------AVKY-LAKVGIDERAqGKYPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 162 ALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLE 241
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
250
....*....|...
gi 896182242 242 VTGSAEEVLTPPR 254
Cdd:PRK10619 232 EEGAPEQLFGNPQ 244
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-194 |
1.51e-23 |
|
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: 99.84 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 4 QTQNLTDHVTKPDTDSTALLRATDLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEL 81
Cdd:COG4987 315 APPAVTEPAEPAPAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 82 LGAPLTKLRAHERATRLAYLPQHTP--ADTaidVRTVVALGRyahhrrrdrfrssLNSTDHDIVAyALDRVGVTALADRP 159
Cdd:COG4987 395 GGVDLRDLDEDDLRRRIAVVPQRPHlfDTT---LRENLRLAR-------------PDATDEELWA-ALERVGLGDWLAAL 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 896182242 160 I-----------TALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG4987 458 PdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLD 503
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
29-254 |
2.20e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 97.56 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 29 SVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE-RATR--LAYLPQHT 105
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElRKARrqIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 padTAIDVRTV---VALGRYAHHRRRDRFRSSlnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:PRK11153 92 ---NLLSSRTVfdnVALPLELAGTPKAEIKAR--------VTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 183 VMLFDEPTAALD-------------IgfqleilellgelaDEGHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAE 247
Cdd:PRK11153 161 VLLCDEATSALDpattrsilellkdI--------------NRELGLTIVLitHEMDVVKRICDRVAVIDAGRLVEQGTVS 226
|
....*..
gi 896182242 248 EVLTPPR 254
Cdd:PRK11153 227 EVFSHPK 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-238 |
2.66e-23 |
|
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: 93.26 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLtklraheratrlaylp 102
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 qhtpadtaidvrtvvalgryahhrrrdRFRSSLNSTDHDIvayaldrvgvtaladRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:cd03216 65 ---------------------------SFASPRDARRAGI---------------AMVYQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 183 VMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-238 |
2.69e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 14 KPDTDSTALLRATDLSVgyrnRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLtKLRAHE 93
Cdd:COG1129 248 RAAAPGEVVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 94 RATR--LAYLPQhtpaD---TAI----DVR---TVVALGRYAHHRRRDRfrsslnSTDHDIVAYALDRVGV-TALADRPI 160
Cdd:COG1129 323 DAIRagIAYVPE----DrkgEGLvldlSIReniTLASLDRLSRGGLLDR------RRERALAEEYIKRLRIkTPSPEQPV 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 161 TALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREG 470
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-266 |
4.51e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.20 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 16 DTDSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKL---RAH 92
Cdd:PRK15439 5 DTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpaKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 93 ERATRLayLPQHTPADTAIDVRTVVALGRYAHHRRRDRFR---SSLNST-DHDIVAYALDrvgvtaLADrpitalsggqR 168
Cdd:PRK15439 85 QLGIYL--VPQEPLLFPNLSVKENILFGLPKRQASMQKMKqllAALGCQlDLDSSAGSLE------VAD----------R 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 169 QLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEE 248
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
250
....*....|....*...
gi 896182242 249 VLTPPRIDAIYRISSAVD 266
Cdd:PRK15439 227 LSTDDIIQAITPAAREKS 244
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-238 |
4.67e-23 |
|
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: 93.27 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRnrtvVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR-LA 99
Cdd:cd03215 3 PVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPqhtpadtaidvrtvvalgryahhrrRDRFRSSLN---STDHDIVAYALdrvgvtaladrpitaLSGGQRQLVFIAKL 176
Cdd:cd03215 79 YVP-------------------------EDRKREGLVldlSVAENIALSSL---------------LSGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896182242 177 LAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-260 |
5.26e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.08 E-value: 5.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVT---PSSGQVELLGapltklRAHERATRL 98
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLG------RTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQHTPADTA--------IDVRTVV------ALGRYAHHRRRDRFRSSLNSTDhdiVAYALDRVGVTALADRPITALS 164
Cdd:PRK09984 78 ARDIRKSRANTGyifqqfnlVNRLSVLenvligALGSTPFWRTCFSWFTREQKQR---ALQALTRVGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 165 GGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGfQLEILELLGELADEGHGIGVV--LHDLNLAARSCHRLSVIHNGGLEV 242
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVvtLHQVDYALRYCERIVALRQGHVFY 233
|
250
....*....|....*...
gi 896182242 243 TGSAEEvLTPPRIDAIYR 260
Cdd:PRK09984 234 DGSSQQ-FDNERFDHLYR 250
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-240 |
6.04e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 92.66 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGY--RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAY 100
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQhtpadtaiDVRTvvalgryahhrrrdrFRSSLNstdhDIVayaldrvgvtaladrpitaLSGGQRQLVFIAKLLAQQ 180
Cdd:cd03246 81 LPQ--------DDEL---------------FSGSIA----ENI-------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 181 AKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAArSCHRLSVIHNGGL 240
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-238 |
6.60e-23 |
|
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: 93.59 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRT----VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtR 97
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 LAYLPQHTPADTAIDVRTVVALGRYAHHRRRDRFRSSLNSTdhdivayaLDRVGVTALADRPITALSGGQRQLVFIAKLL 177
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEEL--------ADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 178 AQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-259 |
8.42e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.19 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR-LA 99
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPQhtpaDTAIDVRTVValgrYAHHRRRDRFRSSLNSTDHDIVAYAL-DRVGVTALADRPITALSGGQRQLVFIAKLLA 178
Cdd:PRK10895 82 YLPQ----EASIFRRLSV----YDNLMAVLQIRDDLSAEQREDRANELmEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 179 QQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRIDAI 258
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
.
gi 896182242 259 Y 259
Cdd:PRK10895 234 Y 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-194 |
1.17e-22 |
|
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: 92.56 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAhERATRLAYLp 102
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPAdtaidVRTVVALgryahhRRRDRFRSSLNSTDHdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:cd03231 79 GHAPG-----IKTTLSV------LENLRFWHADHSDEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRP 145
|
170
....*....|..
gi 896182242 183 VMLFDEPTAALD 194
Cdd:cd03231 146 LWILDEPTTALD 157
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-249 |
2.38e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.02 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 32 YRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTklraHERATRLAYLPQHT---PAD 108
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGYLPEERglyPKM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 109 TAIDVrtVVALGRYAHHRRRDRFRSslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLV-FIAKLLAqQAKVMLFD 187
Cdd:COG4152 87 KVGEQ--LVYLARLKGLSKAEAKRR---------ADEWLERLGLGDRANKKVEELSKGNQQKVqLIAALLH-DPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896182242 188 EPTAALDIGFQLEILELLGELADEghGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEV 249
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAK--GTTVIFssHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-253 |
2.96e-22 |
|
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: 92.40 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNrTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERatRLAYLP 102
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR--DISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPADTAIDVRTVVALGryAHHRRRDRfrsslnSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:cd03299 78 QNYALFPHMTVYKNIAYG--LKKRKVDK------KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896182242 183 VMLFDEPTAALDIGFQLEILELLGELADEgHGIGV--VLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKE-FGVTVlhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-238 |
3.13e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.72 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKlRAHERATRL 98
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQHTPADTAIDVR-TVVALGRYahhrrrdrFRSSlNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLL 177
Cdd:PRK13537 83 GVVPQFDNLDPDFTVReNLLVFGRY--------FGLS-AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 178 AQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-250 |
3.27e-22 |
|
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: 95.97 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 20 TALLRATDLSVGY--RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR 97
Cdd:COG4618 328 KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 LAYLPQhtpadtaiDVR----TVvalgryahhrrRD---RFRsslNSTDHDIVAyALDRVGV------------TALADR 158
Cdd:COG4618 408 IGYLPQ--------DVElfdgTI-----------AEniaRFG---DADPEKVVA-AAKLAGVhemilrlpdgydTRIGEG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 159 PiTALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDigfqleilellgelaDEG-------------HGIGVVL--HDLN 223
Cdd:COG4618 465 G-ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD---------------DEGeaalaaairalkaRGATVVVitHRPS 528
|
250 260
....*....|....*....|....*..
gi 896182242 224 LAArSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:COG4618 529 LLA-AVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
47-194 |
4.01e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 91.59 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 47 PGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPL------TKLRAHERatRLAYLPQHTPADTAIDVRTVVALG 120
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQQR--KIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896182242 121 RYAHHRRRDRFRsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:cd03297 100 LKRKRNREDRIS----------VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-195 |
5.81e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.70 E-value: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLP 102
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPADTAIDVRTVVAlgryahhrrrdRFrssLNSTDHDIVAyALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:PRK13539 83 AMKPALTVAENLEFWA-----------AF---LGGEELDIAA-ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRP 147
|
170
....*....|...
gi 896182242 183 VMLFDEPTAALDI 195
Cdd:PRK13539 148 IWILDEPTAALDA 160
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-250 |
6.10e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 6.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRT-VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAY 100
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQHTPADTAIDVRTV---VALGRYAHHRRRDRFrsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLL 177
Cdd:PRK13636 85 GMVFQDPDNQLFSASVyqdVSFGAVNLKLPEDEV--------RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896182242 178 AQQAKVMLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
11-195 |
6.25e-22 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 95.26 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 11 HVTKPDTDSTALLRATDLSVGYRN--RTVVSGvnlAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEllgaplTK 88
Cdd:PRK13409 329 RPPRDESERETLVEYPDLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 89 LraheratRLAYLPQHTPADTAIdvrTVVALGRYAhhrrRDRFRSSLnsTDHDIVayalDRVGVTALADRPITALSGGQR 168
Cdd:PRK13409 400 L-------KISYKPQYIKPDYDG---TVEDLLRSI----TDDLGSSY--YKSEII----KPLQLERLLDKNVKDLSGGEL 459
|
170 180
....*....|....*....|....*..
gi 896182242 169 QLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-240 |
7.49e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.06 E-value: 7.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 20 TALLRATDLSVGYRN---------RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKL- 89
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 90 ----RAHERATRL-------AYLPQHTpadtaidVRTVVA-----LGRYAHHRRRDRFRSSLNSTDHDivayaldrvgvT 153
Cdd:PRK10419 81 raqrKAFRRDIQMvfqdsisAVNPRKT-------VREIIReplrhLLSLDKAERLARASEMLRAVDLD-----------D 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 154 ALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGhGIGVVL--HDLNLAARSCHR 231
Cdd:PRK10419 143 SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQF-GTACLFitHDLRLVERFCQR 221
|
....*....
gi 896182242 232 LSVIHNGGL 240
Cdd:PRK10419 222 VMVMDNGQI 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-194 |
1.68e-21 |
|
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: 89.34 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHeRATRLAYLp 102
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPAdtaidVRTVVALGRYAHHRRRDrfrssLNSTDHDIVAyALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:TIGR01189 79 GHLPG-----LKPELSALENLHFWAAI-----HGGAQRTIED-ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRP 147
|
170
....*....|..
gi 896182242 183 VMLFDEPTAALD 194
Cdd:TIGR01189 148 LWILDEPTTALD 159
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-194 |
1.97e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.46 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTP---SSGQVELLGAPLTKLRAHERatRLA 99
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQR--RIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPQHTPADTAIDVRTVVALGRYAHHRRRDRfrsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQ 179
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFALPPTIGRAQR---------RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170
....*....|....*
gi 896182242 180 QAKVMLFDEPTAALD 194
Cdd:COG4136 151 EPRALLLDEPFSKLD 165
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-249 |
2.67e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.84 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKlraheratrla 99
Cdd:PRK13635 5 IIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 ylpqhtpaDTAIDVRTVVALgryahhrrrdRFRSSLN----STDHDIVAY------------------ALDRVGVTALAD 157
Cdd:PRK13635 74 --------ETVWDVRRQVGM----------VFQNPDNqfvgATVQDDVAFglenigvpreemvervdqALRQVGMEDFLN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 158 RPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARScHRLSVIH 236
Cdd:PRK13635 136 REPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDpRGRREVLETVRQLKEQKGITVLSITHDLDEAAQA-DRVIVMN 214
|
250
....*....|...
gi 896182242 237 NGGLEVTGSAEEV 249
Cdd:PRK13635 215 KGEILEEGTPEEI 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
40-254 |
3.66e-21 |
|
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: 89.45 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 40 GVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKlRAHERAT---RLAYLPQHTpadtaidVRTV 116
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMVvfqNYSLLPWLT-------VREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 117 VALG--RYAHHRRRDRFRSslnstdhdIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:TIGR01184 75 IALAvdRVLPDLSKSERRA--------IVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896182242 195 IGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTP-PR 254
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEE-HRVTVLMvtHDVDEALLLSDRVVMLTNGPAANIGQILEVPFPrPR 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
35-253 |
3.69e-21 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 89.67 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHT---PADTAI 111
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIglfPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 112 D-VRTVVALGRYAHHRRRDRFRSSLnstdhdivayALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPT 190
Cdd:cd03295 94 EnIALVPKLLKWPKEKIRERADELL----------ALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896182242 191 AALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:cd03295 164 GALDpITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-255 |
4.11e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 90.14 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVV-SGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLT-KLRAHERATRLA 99
Cdd:PRK13639 1 ILETRDLKYSYPDGTEAlKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPQHTPADT--AIDVRTVVALGryahhrrrdrfrsSLN-STDHDIVAY----ALDRVGVTALADRPITALSGGQRQLVF 172
Cdd:PRK13639 81 GIVFQNPDDQlfAPTVEEDVAFG-------------PLNlGLSKEEVEKrvkeALKAVGMEGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 173 IAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTP 252
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
...
gi 896182242 253 PRI 255
Cdd:PRK13639 228 IET 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-255 |
4.16e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.66 E-value: 4.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtrl 98
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 aylpQHTPADTAIDVR-----TVVALGRYAHHRR-RDRFRSSLNSTDH---------DIVAYALDRVGVTALADRPITAL 163
Cdd:PRK11300 79 ----RMGVVRTFQHVRlfremTVIENLLVAQHQQlKTGLFSGLLKTPAfrraesealDRAATWLERVGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 164 SGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLE 241
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNE-HNVTVLLieHDMKLVMGISDRIYVVNQGTPL 233
|
250
....*....|....
gi 896182242 242 VTGSAEEVLTPPRI 255
Cdd:PRK11300 234 ANGTPEEIRNNPDV 247
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-253 |
1.08e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 90.66 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 8 LTDHVTKPDTDS----TALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLG 83
Cdd:PRK11607 1 MNDAIPRPQAKTrkalTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 84 APLTKLRAHERATRL-----AYLPQHTpadtaidVRTVVALGryahhRRRDRF-RSSLNSTdhdiVAYALDRVGVTALAD 157
Cdd:PRK11607 81 VDLSHVPPYQRPINMmfqsyALFPHMT-------VEQNIAFG-----LKQDKLpKAEIASR----VNEMLGLVHMQEFAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 158 RPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDigfQLEILELLGELADEGHGIGV----VLHDLNLAARSCHRLS 233
Cdd:PRK11607 145 RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD---KKLRDRMQLEVVDILERVGVtcvmVTHDQEEAMTMAGRIA 221
|
250 260
....*....|....*....|
gi 896182242 234 VIHNGGLEVTGSAEEVLTPP 253
Cdd:PRK11607 222 IMNRGKFVQIGEPEEIYEHP 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
45-195 |
1.24e-20 |
|
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: 91.38 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 45 IRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEllgaplTKLRaheratrLAYLPQHTPADTAIDVRTVvaLGRYAh 124
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD------EDLK-------ISYKPQYISPDYDGTVEEF--LRSAN- 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 125 hrrRDRFRSSLnsTDHDIVayalDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:COG1245 427 ---TDDFGSSY--YKTEII----KPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
25-248 |
1.32e-20 |
|
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: 87.43 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 25 ATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKlRAHERATRLAYLPQH 104
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 TPADTAIDVRTVVAL-GR---YAHHRRRDRfrsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQ 180
Cdd:cd03265 82 LSVDDELTGWENLYIhARlygVPGAERRER------------IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 181 AKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEE 248
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEE-FGMTILLttHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
43-244 |
1.50e-20 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 87.16 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 43 LAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYlpQHTPADTAIDVRTVVALGRY 122
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF--QENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 123 AHHRrrdrfrssLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGF-QLEI 201
Cdd:cd03298 97 PGLK--------LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALrAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 896182242 202 LELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTG 244
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-224 |
2.52e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.48 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 20 TALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEllgapltklraHERATRLA 99
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPQHTPADTAIDVrTVvalgryahhRRRDRFRSSLNSTDhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQ 179
Cdd:PRK09544 71 YVPQKLYLDTTLPL-TV---------NRFLRLRPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 896182242 180 QAKVMLFDEPTAALDIGFQLEILELLGELADE-GHGIGVVLHDLNL 224
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHL 183
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-194 |
2.55e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 90.61 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHT 105
Cdd:COG1132 344 NVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 P--ADTaidVRTVVALGRyahhrrrdrfrssLNSTDHDIVAyALDRVGV------------TALADRPITaLSGGQRQLV 171
Cdd:COG1132 424 FlfSGT---IRENIRYGR-------------PDATDEEVEE-AAKAAQAhefiealpdgydTVVGERGVN-LSGGQRQRI 485
|
170 180
....*....|....*....|...
gi 896182242 172 FIAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG1132 486 AIARALLKDPPILILDEATSALD 508
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
35-251 |
3.21e-20 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 87.51 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLG---APLTKLRAHERATRLAYLPQHtP----- 106
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrdiTAKKKKKLKDLRKKVGLVFQF-Pehqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 107 ADTaidVRTVVALGRyahhrrrdrfrSSLNSTDHDI---VAYALDRVGVT-ALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:TIGR04521 97 EET---VYKDIAFGP-----------KNLGLSEEEAeerVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 183 VMLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLT 251
Cdd:TIGR04521 163 VLILDEPTAGLDpKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
32-240 |
3.25e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 87.00 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 32 YRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLG-APLTKLRAHER--------ATRLAY-L 101
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRKKFLRrigvvfgqKTQLWWdL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PqhtPADTAIDVRTVVALGRYAHHRRRDRFRSSLNstdhdivayaldrvgVTALADRPITALSGGQRQLVFIAKLLAQQA 181
Cdd:cd03267 111 P---VIDSFYLLAAIYDLPPARFKKRLDELSELLD---------------LEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 182 KVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGL 240
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRE-RGTTVLLtsHYMKDIEALARRVLVIDKGRL 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
17-194 |
5.45e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 87.86 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 17 TDSTALLRATDLSV------GYRNRTV-----VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAP 85
Cdd:COG4608 2 AMAEPLLEVRDLKKhfpvrgGLFGRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 86 LTKLRAHE-RATR----------LAYL-PQHTPADT---AIDVRTVVAlgryaHHRRRDRfrsslnstdhdiVAYALDRV 150
Cdd:COG4608 82 ITGLSGRElRPLRrrmqmvfqdpYASLnPRMTVGDIiaePLRIHGLAS-----KAERRER------------VAELLELV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 896182242 151 GV-TALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG4608 145 GLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-254 |
6.00e-20 |
|
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: 89.36 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 18 DSTALLRATDLSVGYRN----RTVVSGVNLAIRPGEVQGIIGSNGTGKS----SLLRAMAGIVTPSSGQV-----ELLGA 84
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIlfdgqDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 85 PLTKLRAHeRATRLAYL---------PQHTPADtaiDVRTVVALgryahHRRRDRFRSslnstdHDIVAYALDRVGVTAl 155
Cdd:COG4172 82 SERELRRI-RGNRIAMIfqepmtslnPLHTIGK---QIAEVLRL-----HRGLSGAAA------RARALELLERVGIPD- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 156 ADRPITA----LSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSC 229
Cdd:COG4172 146 PERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRE-LGMALLLitHDLGVVRRFA 224
|
250 260
....*....|....*....|....*
gi 896182242 230 HRLSVIHNGGLEVTGSAEEVLTPPR 254
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-194 |
6.84e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 86.24 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 13 TKPDTDSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGI--VTPS---SGQVELLGA--- 84
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEdiy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 85 ----PLTKLRAheratRLAYLPQH-TPADTAIdvRTVVALG-RYahHRRRDRfrSSLNstdhDIVAYALDRVgvtAL--- 155
Cdd:COG1117 82 dpdvDVVELRR-----RVGMVFQKpNPFPKSI--YDNVAYGlRL--HGIKSK--SELD----EIVEESLRKA---ALwde 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 896182242 156 -ADR---PITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG1117 144 vKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-194 |
7.30e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.29 E-value: 7.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAhERATRL--- 98
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ERGVVFqne 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQHtpadtaiDVRTVVALG-RYAHHRRRDRFRSSLNstdhdivayALDRVGVTALADRPITALSGGQRQLVFIAKLL 177
Cdd:PRK11248 80 GLLPWR-------NVQDNVAFGlQLAGVEKMQRLEIAHQ---------MLKKVGLEGAEKRYIWQLSGGQRQRVGIARAL 143
|
170
....*....|....*..
gi 896182242 178 AQQAKVMLFDEPTAALD 194
Cdd:PRK11248 144 AANPQLLLLDEPFGALD 160
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
32-253 |
8.63e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.83 E-value: 8.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 32 YRNRT-VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERatRLAYLPQHTPADTA 110
Cdd:PRK10851 11 SFGRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR--KVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 111 IDVRTVVALGRYAHHRRRDRFRSSLNSTdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPT 190
Cdd:PRK10851 89 MTVFDNIAFGLTVLPRRERPNAAAIKAK----VTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896182242 191 AALDIGFQLEILELLGELADEGHGIGV-VLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVfVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
32-254 |
9.51e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.96 E-value: 9.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 32 YRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEL------LGAPLTKLRAHERATR-------- 97
Cdd:PRK11264 13 FHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIRQLRqhvgfvfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 -LAYLPQHTPADTAIDVRTVVALGRYAHHRRRDRfrsslnstdhdivaYALDRVGVTALADRPITALSGGQRQLVFIAKL 176
Cdd:PRK11264 93 nFNLFPHRTVLENIIEGPVIVKGEPKEEATARAR--------------ELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 177 LAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPR 254
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-238 |
1.14e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKlRAHERATRL 98
Cdd:PRK13536 38 STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQHTPADTAIDVR-TVVALGRYahhrrrdrFRSSLNSTDhDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLL 177
Cdd:PRK13536 117 GVVPQFDNLDLEFTVReNLLVFGRY--------FGMSTREIE-AVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 178 AQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-238 |
1.44e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.16 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 14 KPDTDSTALLRATDLSV-GYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAH 92
Cdd:COG3845 249 APAEPGEVVLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 93 E-RATRLAYLP---QHTPADTAIDVRTVVALGRYahhrRRDRFRSS--LNStdHDIVAYALDRVG----VTALADRPITA 162
Cdd:COG3845 329 ErRRLGVAYIPedrLGRGLVPDMSVAENLILGRY----RRPPFSRGgfLDR--KAIRAFAEELIEefdvRTPGPDTPARS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 163 LSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDL----NLaarsCHRLSVIHNG 238
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLdeilAL----SDRIAVMYEG 478
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
32-194 |
1.63e-19 |
|
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: 84.61 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 32 YRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRL-----AYLPQHTP 106
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMvfqnyALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 107 ADTaidvrtvVALGRYAHHRRRDRFRSSLNStdhdiVAYALdrvGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLF 186
Cdd:cd03301 90 YDN-------IAFGLKLRKVPKDEIDERVRE-----VAELL---QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
....*...
gi 896182242 187 DEPTAALD 194
Cdd:cd03301 155 DEPLSNLD 162
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-194 |
1.65e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.09 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRaHERATRLAYL 101
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHT---PADTAIDvrtvvALgryahhrrrdRFRSSL-NSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLL 177
Cdd:PRK13538 80 GHQPgikTELTALE-----NL----------RFYQRLhGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLW 144
|
170
....*....|....*..
gi 896182242 178 AQQAKVMLFDEPTAALD 194
Cdd:PRK13538 145 LTRAPLWILDEPFTAID 161
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
23-195 |
3.56e-19 |
|
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: 81.73 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEllgapltklraHERATRLAYLP 102
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-----------WGSTVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QhtpadtaidvrtvvalgryahhrrrdrfrsslnstdhdivayaldrvgvtaladrpitaLSGGQRQLVFIAKLLAQQAK 182
Cdd:cd03221 70 Q-----------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170
....*....|...
gi 896182242 183 VMLFDEPTAALDI 195
Cdd:cd03221 91 LLLLDEPTNHLDL 103
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-195 |
4.60e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.96 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGI--VTPSSGQVELLGAPLTKLRAHERATR--- 97
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 LAYlpQHtPadTAIDVRTVVALGRYAHHRRRDRFRSSLnsTDHDIVAYALDRVGVTA-LADRPITA-LSGGQRQLVFIAK 175
Cdd:COG0396 81 LAF--QY-P--VEIPGVSVSNFLRTALNARRGEELSAR--EFLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQ 153
|
170 180
....*....|....*....|
gi 896182242 176 LLAQQAKVMLFDEPTAALDI 195
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDI 173
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-196 |
7.79e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.01 E-value: 7.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 3 QQTQNLTDHVTKPDTDSTALLRATDLSVG-YRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEL 81
Cdd:COG4178 343 EAADALPEAASRIETSEDGALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 82 lgaPltklraheRATRLAYLPQHT--PADTaidVRTVVAlgrYAHHRRrdrfrsslnSTDHDIVAYALDRVGVTALADRP 159
Cdd:COG4178 423 ---P--------AGARVLFLPQRPylPLGT---LREALL---YPATAE---------AFSDAELREALEAVGLGHLAERL 476
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 896182242 160 ITA------LSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIG 196
Cdd:COG4178 477 DEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-250 |
7.93e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.90 E-value: 7.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTK-----LRAHERAT 96
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrglLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 97 RLAYLPQHTPADTAIDVRTVVALgryahhrrrdrfrSSLNSTDHDI---VAYALDRVGVTALADRPITALSGGQRQLVFI 173
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAFSL-------------RNLGVPEAEItrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182242 174 AKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-222 |
9.05e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 85.88 E-value: 9.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGY-RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYL 101
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHtPADTAIDVRTVVALGRYahhrrrdrfrsslNSTDHDIVAyALDRVGVTALADRPI-----------TALSGGQRQL 170
Cdd:TIGR02868 415 AQD-AHLFDTTVRENLRLARP-------------DATDEELWA-ALERVGLADWLRALPdgldtvlgeggARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALDIGfQLEILELLGELADEGHGIGVVLHDL 222
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAE-TADELLEDLLAALSGRTVVLITHHL 530
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
31-250 |
1.16e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.82 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 31 GYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLG---APLtklraherATRLAYLPQHTPA 107
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsALL--------ELGAGFHPELTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 108 DtaidvrTVVALGRYAHHRRRD---RFRsslnstdhDIVAYAldrvGVTALADRPITALSGGQR-QLVF-IAklLAQQAK 182
Cdd:COG1134 107 E------NIYLNGRLLGLSRKEideKFD--------EIVEFA----ELGDFIDQPVKTYSSGMRaRLAFaVA--TAVDPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 183 VMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
22-253 |
1.49e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYR-NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHErATRLAY 100
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQHTPADTAID--VRTVVALG--------RYAHHRrrdrfrsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQL 170
Cdd:PRK13652 82 LVFQNPDDQIFSptVEQDIAFGpinlgldeETVAHR----------------VSSALHMLGLEELRDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEV 249
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDpQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
....
gi 896182242 250 LTPP 253
Cdd:PRK13652 226 FLQP 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
41-253 |
1.82e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 84.00 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPL------TKLRAHERatRLAYLPQhtpadtaiDVR 114
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRR--RIGYVFQ--------EAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 115 -----TVVALGRYAHHRRRDRFRSSLnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEP 189
Cdd:COG4148 88 lfphlSVRGNLLYGRKRAPRAERRIS-------FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 190 TAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDE-LDIPILYvsHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
27-255 |
4.73e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.71 E-value: 4.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNRT-VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQhT 105
Cdd:PRK13647 9 DLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ-D 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 PADT--AIDVRTVVALGRYAHHRRRDRFRSSLNStdhdivayALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKV 183
Cdd:PRK13647 88 PDDQvfSSTVWDDVAFGPVNMGLDKDEVERRVEE--------ALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896182242 184 MLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGsAEEVLTPPRI 255
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDI 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-254 |
6.06e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRN----RTVVSGVNLAIRPGEVQGIIGSNGTGKS----SLLRAMAG--IVTPS-----SGQvELLG 83
Cdd:PRK15134 2 TQPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVVYPSgdirfHGE-SLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 84 APLTKLRaHERATRLAYL---------PQHTPADTAIDVRTVvalgryahHR--RRDRFRSSLNStdhdivayALDRVGV 152
Cdd:PRK15134 81 ASEQTLR-GVRGNKIAMIfqepmvslnPLHTLEKQLYEVLSL--------HRgmRREAARGEILN--------CLDRVGI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 153 ----TALADRPiTALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADE-GHGIGVVLHDLNLAAR 227
Cdd:PRK15134 144 rqaaKRLTDYP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRK 222
|
250 260
....*....|....*....|....*..
gi 896182242 228 SCHRLSVIHNGGLEVTGSAEEVLTPPR 254
Cdd:PRK15134 223 LADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-227 |
6.64e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRN----RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKL----R 90
Cdd:PRK11629 2 NKILLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 91 AHERATRLAYLPQ--HTPAD-TAID-VRTVVALGRYAHHRRRDRFRSSLNStdhdivayaldrVGVTALADRPITALSGG 166
Cdd:PRK11629 82 AELRNQKLGFIYQfhHLLPDfTALEnVAMPLLIGKKKPAEINSRALEMLAA------------VGLEHRANHRPSELSGG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 167 QRQLVFIAKLLAQQAKVMLFDEPTAALDIG-----FQLEILELLGeladEGHGIGVVLHDLNLAAR 227
Cdd:PRK11629 150 ERQRVAIARALVNNPRLVLADEPTGNLDARnadsiFQLLGELNRL----QGTAFLVVTHDLQLAKR 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
53-253 |
7.25e-18 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 82.16 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 53 IIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRL-----AYLPQHTPADTaidvrtvVALGRyahhrr 127
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMvfqsyALFPHMTVEEN-------VAFGL------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 128 rdRFRSSLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGE 207
Cdd:TIGR01187 68 --KMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 896182242 208 LADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:TIGR01187 146 IQEQ-LGITFVFvtHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
40-247 |
7.49e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 7.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 40 GVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTkLR--AHERATRLAYLPQHTpadTAIDVRTV- 116
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRspRDAIALGIGMVHQHF---MLVPNLTVa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 117 --VALGRyahhRRRDRFRSSLNSTDHDIVAYAlDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAAL- 193
Cdd:COG3845 99 enIVLGL----EPTKGGRLDRKAARARIRELS-ERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLt 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 194 ----DIGFQleileLLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGglEVTGSAE 247
Cdd:COG3845 174 pqeaDELFE-----ILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG--KVVGTVD 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
45-195 |
1.07e-17 |
|
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: 80.14 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 45 IRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGapltklraheraTRLAYLPQHTPADTAIDVRTVValgryaH 124
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL------------DTVSYKPQYIKADYEGTVRDLL------S 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 125 HRRRDRFRSSLNSTDhdivayALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:cd03237 84 SITKDFYTHPYFKTE------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
32-243 |
1.49e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 32 YRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHeraTRLAY-----LPQHTP 106
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED---TRLMFqdarlLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 107 ADTaidvrtvVALGRYAHHRRRDRfrsslnstdhdivaYALDRVGvtaLADR----PiTALSGGQRQLVFIAKLLAQQAK 182
Cdd:PRK11247 99 IDN-------VGLGLKGQWRDAAL--------------QALAAVG---LADRanewP-AALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896182242 183 VMLFDEPTAALD----IGFQLEILELLGEladegHGIGVVL--HDLNLAARSCHRLSVIHNG--GLEVT 243
Cdd:PRK11247 154 LLLLDEPLGALDaltrIEMQDLIESLWQQ-----HGFTVLLvtHDVSEAVAMADRVLLIEEGkiGLDLT 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-194 |
1.57e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 20 TALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR-- 97
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNtv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 ---LAYLPQHTpadtaidVRTVVALG----RYAHHRRRDRfrsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQL 170
Cdd:PRK09452 92 fqsYALFPHMT-------VFENVAFGlrmqKTPAAEITPR------------VMEALRMVQLEEFAQRKPHQLSGGQQQR 152
|
170 180
....*....|....*....|....
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALD 176
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
42-244 |
1.65e-17 |
|
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: 79.13 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 42 NLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtrLAYLPQHTPADTAIDVRTVVALGR 121
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP--VSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 122 YAHHRrrdrfrssLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEI 201
Cdd:TIGR01277 96 HPGLK--------LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896182242 202 LELLGELADEGH-GIGVVLHDLNLAARSCHRLSVIHNGGLEVTG 244
Cdd:TIGR01277 168 LALVKQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-194 |
1.66e-17 |
|
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: 82.29 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGqvELLGAPLTKlraheratrLAYLPQHTPADTAIDV 113
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--EARPQPGIK---------VGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALGRYAHHRRRDRFRS-SLNSTD---------------HDIV----AYALDR---VGVTAL----ADRPITALSGG 166
Cdd:TIGR03719 86 RENVEEGVAEIKDALDRFNEiSAKYAEpdadfdklaaeqaelQEIIdaadAWDLDSqleIAMDALrcppWDADVTKLSGG 165
|
170 180
....*....|....*....|....*...
gi 896182242 167 QRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-195 |
1.67e-17 |
|
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: 79.07 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQh 104
Cdd:cd03244 7 NVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 tpaDTAIDVRTVvalgryahhrrrdrfRSSLN----STDHDIVAyALDRVG----VTALA---DRPITA----LSGGQRQ 169
Cdd:cd03244 86 ---DPVLFSGTI---------------RSNLDpfgeYSDEELWQ-ALERVGlkefVESLPgglDTVVEEggenLSVGQRQ 146
|
170 180
....*....|....*....|....*.
gi 896182242 170 LVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDP 172
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-194 |
1.82e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 17 TDSTALLRATDlsVGYR--NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHER 94
Cdd:PRK10247 2 QENSPLLQLQN--VGYLagDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 95 ATRLAYLPQhTPA---DTAIDVRTvvalgrYAHHRRRDRfrsslnsTDHDIVAYALDRVGV-TALADRPITALSGGQRQL 170
Cdd:PRK10247 80 RQQVSYCAQ-TPTlfgDTVYDNLI------FPWQIRNQQ-------PDPAIFLDDLERFALpDTILTKNIAELSGGEKQR 145
|
170 180
....*....|....*....|....
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALD 169
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
18-254 |
2.23e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.58 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 18 DSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQV----------ELLGAPLT 87
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqlrDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 88 KLRAHERaTRLAYLPQHtPAD------TA---IDVRtVVALGryAHHRRRDRfrsslnstdhDIVAYALDRVGVTA--LA 156
Cdd:PRK11701 82 ERRRLLR-TEWGFVHQH-PRDglrmqvSAggnIGER-LMAVG--ARHYGDIR----------ATAGDWLERVEIDAarID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 157 DRPiTALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEIL-ELLGELADEGHGIGVVLHDLNLAARSCHRLSVI 235
Cdd:PRK11701 147 DLP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLdLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
250
....*....|....*....
gi 896182242 236 HNGGLEVTGSAEEVLTPPR 254
Cdd:PRK11701 226 KQGRVVESGLTDQVLDDPQ 244
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
35-194 |
2.40e-17 |
|
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: 78.85 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPS---SGQVELLGAPLTKlraHERATRLAYLPQHtpaDTAI 111
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKP---DQFQKCVAYVRQD---DILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 112 DVRTVV-ALGRYAHHRRRDRFRSSLNSTDHDIVAyaLDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPT 190
Cdd:cd03234 94 PGLTVReTLTYTAILRLPRKSSDAIRKKRVEDVL--LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
....
gi 896182242 191 AALD 194
Cdd:cd03234 172 SGLD 175
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-193 |
2.68e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPL--TKLRAHERA- 95
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAALAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 96 -----TRLAYLPQHTPADTaidvrtvVALGRYAH-----HRRRDRFRSSLnstdhdivayALDRVGVTALADRPITALSG 165
Cdd:PRK11288 81 vaiiyQELHLVPEMTVAEN-------LYLGQLPHkggivNRRLLNYEARE----------QLEHLGVDIDPDTPLKYLSI 143
|
170 180
....*....|....*....|....*...
gi 896182242 166 GQRQLVFIAKLLAQQAKVMLFDEPTAAL 193
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-282 |
3.88e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 79.32 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 1 MSQQTQNLTdHVTKPDT--DSTALlratdlsvgyrnrtvvSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQ 78
Cdd:PRK13637 1 MSIKIENLT-HIYMEGTpfEKKAL----------------DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 79 VELLGAPLTKLRAHERATR------LAYlPQHTPADTAIDvrTVVALGRyahhrrrdrfrSSLNSTDHDI---VAYALDR 149
Cdd:PRK13637 64 IIIDGVDITDKKVKLSDIRkkvglvFQY-PEYQLFEETIE--KDIAFGP-----------INLGLSEEEIenrVKRAMNI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 150 VGVT--ALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADE-GHGIGVVLHDLNLAA 226
Cdd:PRK13637 130 VGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 227 RSCHRLSVIHNGGLEVTGSAEEVLTppRIDAIYRISSAVdtdPhtgsvRVTALARA 282
Cdd:PRK13637 210 KLADRIIVMNKGKCELQGTPREVFK--EVETLESIGLAV---P-----QVTYLVRK 255
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
36-249 |
5.45e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.60 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 36 TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLrAHERATRL--AYLPQHTPADTAIDV 113
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLAAQLgiGIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALGRyahHRRRDRFrsSLNSTDHD----IVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEP 189
Cdd:PRK09700 98 LENLYIGR---HLTKKVC--GVNIIDWRemrvRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 190 TAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEV 249
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-276 |
7.86e-17 |
|
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: 79.39 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTK------LRAHERatRLAYLPQHTPADTAIDVR 114
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKR--RIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 115 TVVALGRYahhrrrdRFRSSLNSTDHDIVayaLDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:TIGR02142 94 GNLRYGMK-------RARPSERRISFERV---IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 195 IGFQLEILELLGELADE-GHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP------RIDAIYRISSAVDT 267
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPdlpwlaREDQGSLIEGVVAE 243
|
250
....*....|
gi 896182242 268 -DPHTGSVRV 276
Cdd:TIGR02142 244 hDQHYGLTAL 253
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
34-251 |
1.06e-16 |
|
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: 79.70 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQhtpaDTAIDV 113
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQ----DVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVAlgryahhrRRDRFRSslNSTDHDIVAyALDRVGV------------TALADRPITaLSGGQRQLVFIAKLLAQQA 181
Cdd:TIGR01842 406 GTVAE--------NIARFGE--NADPEKIIE-AAKLAGVhelilrlpdgydTVIGPGGAT-LSGGQRQRIALARALYGDP 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896182242 182 KVMLFDEPTAALD-IGFQLEILELLGELAdegHGIGVVL--HDLNLAArSCHRLSVIHNGGLEVTGSAEEVLT 251
Cdd:TIGR01842 474 KLVVLDEPNSNLDeEGEQALANAIKALKA---RGITVVVitHRPSLLG-CVDKILVLQDGRIARFGERDEVLA 542
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
42-194 |
1.22e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.93 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 42 NLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAtrLAYLPQHTPADTAIDVRTVVALGR 121
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP--VSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896182242 122 YAHHRrrdrfrssLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK10771 97 NPGLK--------LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
46-222 |
1.23e-16 |
|
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: 77.41 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 46 RPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQV-----------ELLGAPL----TKLRahERATRLAYLPQHtpadta 110
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELqnyfTKLL--EGDVKVIVKPQY------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 111 IDVRTVVALGRyahhrrrdrFRSSLNSTDH-DIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEP 189
Cdd:cd03236 96 VDLIPKAVKGK---------VGELLKKKDErGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|...
gi 896182242 190 TAALDIGFQLEILELLGELADEGHGIGVVLHDL 222
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
35-240 |
1.31e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.84 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE-----RATRLAYLPQHTPADT 109
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 110 AI----DVRTVVALGRYAHHRRRdrfrsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVML 185
Cdd:PRK10908 95 TVydnvAIPLIIAGASGDDIRRR--------------VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 186 FDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGL 240
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
34-238 |
1.38e-16 |
|
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: 76.68 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHeratRLAYLPQHT-------- 105
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGR----AIPYLRRKIgvvfqdfr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 --PADTAIDvRTVVALGRYAHHRRRDRFRsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKV 183
Cdd:cd03292 89 llPDRNVYE-NVAFALEVTGVPPREIRKR----------VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 184 MLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-254 |
2.07e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.88 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIV-----TPSSGQVELLGAPLTKLRAHERA 95
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 96 TRLAYLPQHTPADTAIDVRTVVALG----RYAHHRRRDRFRsslnstdhdiVAYALDRVG----VTALADRPITALSGGQ 167
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGlklnRLVKSKKELQER----------VRWALEKAQlwdeVKDRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 168 RQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEgHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAE 247
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTR 230
|
....*..
gi 896182242 248 EVLTPPR 254
Cdd:PRK14247 231 EVFTNPR 237
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-194 |
2.25e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 78.62 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELlgAPltklraherATRLAYLPQHTPADTAIDV 113
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--AP---------GIKVGYLPQEPQLDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALGRYAHHRRRDRF-----RSSLNSTDHDIV---------------AYALDR---VGVTAL----ADRPITALSGG 166
Cdd:PRK11819 88 RENVEEGVAEVKAALDRFneiyaAYAEPDADFDALaaeqgelqeiidaadAWDLDSqleIAMDALrcppWDAKVTKLSGG 167
|
170 180
....*....|....*....|....*...
gi 896182242 167 QRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-194 |
2.70e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.05 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRN------RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERA 95
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 96 TRLAYLPQHTPaDTAIdVRTVV----ALGRYAHHRRRDRFRSSlnstdhdiVAYALDRVGVTALADRPITALSGGQRQLV 171
Cdd:PRK13633 84 RNKAGMVFQNP-DNQI-VATIVeedvAFGPENLGIPPEEIRER--------VDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180
....*....|....*....|...
gi 896182242 172 FIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLD 176
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-238 |
6.07e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 20 TALLRATDLSVGYRNR----TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERA 95
Cdd:PRK10535 2 TALLELKDIRRSYPSGeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 96 T-----------RLAYLPqHTPADTAIDVRTVVA-LGRyahHRRRDRFRSslnstdhdivayALDRVGVTALADRPITAL 163
Cdd:PRK10535 82 QlrrehfgfifqRYHLLS-HLTAAQNVEVPAVYAgLER---KQRLLRAQE------------LLQRLGLEDRVEYQPSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 164 SGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARScHRLSVIHNG 238
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQA-ERVIEIRDG 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-263 |
9.59e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.03 E-value: 9.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 16 DTDSTALLRATDLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE 93
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 94 RATRLAYLPQHtPADTAIDVrTV---VALGryAHHRRRDRfrsslnSTDHDIVAYALDRVGVTALADRPITALSGGQRQL 170
Cdd:PRK13632 81 IRKKIGIIFQN-PDNQFIGA-TVeddIAFG--LENKKVPP------KKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNlAARSCHRLSVIHNGGLEVTGSAEEV 249
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDpKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFSEGKLIAQGKPKEI 229
|
250
....*....|....
gi 896182242 250 LTPPRIDAIYRISS 263
Cdd:PRK13632 230 LNNKEILEKAKIDS 243
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-222 |
9.91e-16 |
|
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: 76.75 E-value: 9.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 44 AIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVE---------------LLGAPLTKLRAHEraTRLAYLPQHtpad 108
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrfrgtELQDYFKKLANGE--IKVAHKPQY---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 109 taIDVrtvvaLGRYAHHRRRDrfrsSLNSTD-HDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFD 187
Cdd:COG1245 169 --VDL-----IPKVFKGTVRE----LLEKVDeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*
gi 896182242 188 EPTAALDIGFQLEILELLGELADEGHGIGVVLHDL 222
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
35-264 |
1.60e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.35 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGI----VTPSSGQVELLGAPL--TKLRAHERAT-----RLAYLPQ 103
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVapCALRGRKIATimqnpRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 104 HTPADTAIDvrTVVALGRYAhhrrrdrfrsslnstDHDIVAYALDRVGvtaLADRPITA------LSGGQRQLVFIAKLL 177
Cdd:PRK10418 96 HTMHTHARE--TCLALGKPA---------------DDATLTAALEAVG---LENAARVLklypfeMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 178 AQQAKVMLFDEPTAALDIGFQLEI-LELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRID 256
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARIlDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
....*...
gi 896182242 257 AIYRISSA 264
Cdd:PRK10418 236 VTRSLVSA 243
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-268 |
1.85e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.75 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 16 DTDSTA-LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSG-----QVELLGAPLTKL 89
Cdd:PRK14271 14 DVDAAApAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 90 R-AHERATRLAYLPQHtPADTAIDVRTVVALGRYAHH---RRRDRFRSSLNSTDHDIVAYALDRvgvtaLADRPITaLSG 165
Cdd:PRK14271 94 RdVLEFRRRVGMLFQR-PNPFPMSIMDNVLAGVRAHKlvpRKEFRGVAQARLTEVGLWDAVKDR-----LSDSPFR-LSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 166 GQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIgVVLHDLNLAARSCHRLSVIHNGGLEVTGS 245
Cdd:PRK14271 167 GQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVI-IVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
250 260
....*....|....*....|...
gi 896182242 246 AEEVLTPPRIDAIYRISSAVDTD 268
Cdd:PRK14271 246 TEQLFSSPKHAETARYVAGLSGD 268
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-194 |
1.90e-15 |
|
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: 73.62 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 20 TALLRATDLS-------VGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQ---------VELLG 83
Cdd:COG4778 2 TTLLEVENLSktftlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 84 AP---LTKLRAHEratrLAYLPQH---TPADTAIDV--RTVVALGrYAHHRRRDRFRSslnstdhdivayALDRVGV-TA 154
Cdd:COG4778 82 ASpreILALRRRT----IGYVSQFlrvIPRVSALDVvaEPLLERG-VDREEARARARE------------LLARLNLpER 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 896182242 155 LADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG4778 145 LWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-193 |
2.95e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 39 SGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLT--KLRAHERA------TRLAYLPQHTPADTa 110
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEAgigiihQELNLIPQLTIAEN- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 111 idvrtvVALGRyahhrrrdRFRSSLNSTDHDIVaYA-----LDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVML 185
Cdd:PRK10762 100 ------IFLGR--------EFVNRFGRIDWKKM-YAeadklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVII 164
|
....*...
gi 896182242 186 FDEPTAAL 193
Cdd:PRK10762 165 MDEPTDAL 172
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
36-235 |
3.15e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 36 TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKL----RAHERATRLAYLPQH---TPAD 108
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeaRAKLRAKHVGFVFQSfmlIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 109 TAIDVRTVVALGRYAHHRRrdrfrsslnstDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDE 188
Cdd:PRK10584 104 NALENVELPALLRGESSRQ-----------SRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 896182242 189 PTAALD--IGfQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVI 235
Cdd:PRK10584 173 PTGNLDrqTG-DKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLV 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
38-198 |
3.47e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 74.36 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE-RATR----------LAYL-PQHT 105
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwRAVRsdiqmifqdpLASLnPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 PAD-TAIDVRTvvalgrYAHHRRRDRFRsslnstdhDIVAYALDRVGVTA-LADRPITALSGGQRQLVFIAKLLAQQAKV 183
Cdd:PRK15079 117 IGEiIAEPLRT------YHPKLSRQEVK--------DRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKL 182
|
170
....*....|....*
gi 896182242 184 MLFDEPTAALDIGFQ 198
Cdd:PRK15079 183 IICDEPVSALDVSIQ 197
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
38-250 |
4.28e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.84 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVE-LLG---APLTKLRAHE--RATR-LAYLPQHtpadta 110
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGdewVDMTKPGPDGrgRAKRyIGILHQE------ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 111 idvrtvvaLGRYAHHRRRDRFRSSLNSTDHDIVA-----YALDRVGVT-----ALADRPITALSGGQRQLVFIAKLLAQQ 180
Cdd:TIGR03269 374 --------YDLYPHRTVLDNLTEAIGLELPDELArmkavITLKMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 181 AKVMLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:TIGR03269 446 PRIVILDEPTGTMDpITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-195 |
4.43e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.19 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 13 TKPDTDSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKlraH 92
Cdd:PRK13543 2 IEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 93 ERATRLAYLpQHTPA-----DTAIDVRTVVALgryaHHRRRDRFRSSlnstdhdivayALDRVGVTALADRPITALSGGQ 167
Cdd:PRK13543 79 DRSRFMAYL-GHLPGlkadlSTLENLHFLCGL----HGRRAKQMPGS-----------ALAIVGLAGYEDTLVRQLSAGQ 142
|
170 180
....*....|....*....|....*...
gi 896182242 168 RQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:PRK13543 143 KKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
32-194 |
4.88e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 72.74 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 32 YRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLT-KLRAHERATRL----------AY 100
Cdd:COG4161 12 YGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfSQKPSEKAIRLlrqkvgmvfqQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 --LPQHTPADTAID--VRtVVALGRYAHHRRRDRFrsslnstdhdivayaLDRVGVTALADRPITALSGGQRQLVFIAKL 176
Cdd:COG4161 92 nlWPHLTVMENLIEapCK-VLGLSKEQAREKAMKL---------------LARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170
....*....|....*...
gi 896182242 177 LAQQAKVMLFDEPTAALD 194
Cdd:COG4161 156 LMMEPQVLLFDEPTAALD 173
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
33-194 |
5.34e-15 |
|
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: 71.03 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 33 RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELlgapltklraHERAtRLAYLPQhtpadtaid 112
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM----------PEGE-DLLFLPQ--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 113 vRTVVALGryahhrrrdrfrsslnsTDHDIVAYALDRVgvtaladrpitaLSGGQRQLVFIAKLLAQQAKVMLFDEPTAA 192
Cdd:cd03223 72 -RPYLPLG-----------------TLREQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
..
gi 896182242 193 LD 194
Cdd:cd03223 122 LD 123
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
35-250 |
8.25e-15 |
|
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: 72.13 E-value: 8.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQhtpaDTAIDVR 114
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQ----ENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 115 TV---VALGRYAHHRRRDRFRSSLNSTdHDIVAYAldRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTA 191
Cdd:cd03252 91 SIrdnIALADPGMSMERVIEAAKLAGA-HDFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 896182242 192 ALDIGFQLEILELLGELADeGHGIGVVLHDLNlAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:cd03252 168 ALDYESEHAIMRNMHDICA-GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-194 |
8.37e-15 |
|
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: 73.98 E-value: 8.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 8 LTDHVTKPDTDSTALLRAT------DLSVGY--RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQV 79
Cdd:TIGR02203 310 LLDSPPEKDTGTRAIERARgdvefrNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 80 ELLGAPLTKLRAHERATRLAYLPQHTpadTAIDvRTVVALGRYAhhRRRDRFRSSLNSTDHDivAYALDRVGVTALA-DR 158
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDV---VLFN-DTIANNIAYG--RTEQADRAEIERALAA--AYAQDFVDKLPLGlDT 461
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 896182242 159 PI----TALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:TIGR02203 462 PIgengVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-253 |
8.80e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.22 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 13 TKPDTDSTALLRATDLSVGYR----NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSL------LRAMAGIVTPSS---GQv 79
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFStpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTafalmgLLAANGRIGGSAtfnGR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 80 ELLGAP---LTKLRAHERA-------TRLAylPQHTPADTAIDVrtvvaLGRYAHHRRRDRFRSSLNSTDHDIVAYALDR 149
Cdd:PRK09473 82 EILNLPekeLNKLRAEQISmifqdpmTSLN--PYMRVGEQLMEV-----LMLHKGMSKAEAFEESVRMLDAVKMPEARKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 150 VGVTAladrpiTALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADE-GHGIGVVLHDLNLAARS 228
Cdd:PRK09473 155 MKMYP------HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGI 228
|
250 260
....*....|....*....|....*
gi 896182242 229 CHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:PRK09473 229 CDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
33-240 |
8.95e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.81 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 33 RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGiVTP--SSGQVELLGAPLtKLRAHERATR--LAYLPQHTPAD 108
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPV-KIRNPQQAIAqgIAMVPEDRKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 109 ---TAIDVR---TVVALGRYAHHRRRDrfrsslNSTDHDIVAYALDRVGV-TALADRPITALSGGQRQLVFIAKLLAQQA 181
Cdd:PRK13549 351 givPVMGVGkniTLAALDRFTGGSRID------DAAELKTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 896182242 182 KVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGL 240
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-195 |
1.03e-14 |
|
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: 71.02 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGI--VTPSSGQVELLGAPLTKLRAHERATRLAY 100
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQHTPAdtAIDVRTVVALGRYahhrrrdrfrssLNstdhdivayaldrVGvtaladrpitaLSGGQRQLVFIAKLLAQQ 180
Cdd:cd03217 81 LAFQYPP--EIPGVKNADFLRY------------VN-------------EG-----------FSGGEKKRNEILQLLLLE 122
|
170
....*....|....*
gi 896182242 181 AKVMLFDEPTAALDI 195
Cdd:cd03217 123 PDLAILDEPDSGLDI 137
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
31-244 |
1.16e-14 |
|
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: 71.41 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 31 GYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLG--APLTKLRAheratrlAYLPQHTPAD 108
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLGG-------GFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 109 taiDVRTVVALgrYAHHRRRDRFRSslnstdHDIVAYAldrvGVTALADRPITALSGGQR-QLVF-IAklLAQQAKVMLF 186
Cdd:cd03220 104 ---NIYLNGRL--LGLSRKEIDEKI------DEIIEFS----ELGDFIDLPVKTYSSGMKaRLAFaIA--TALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 187 DEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTG 244
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-193 |
1.28e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.42 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGiVTPS---SGQVELLGAPLT--KLRAHERA------TRLAYLPQHTP 106
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQasNIRDTERAgiaiihQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 107 ADTaidvrtvVALGRYAHHRRRdrfrsslnsTDHDIVaYA-----LDRVGVTALADRPITALSGGQRQLVFIAKLLAQQA 181
Cdd:PRK13549 100 LEN-------IFLGNEITPGGI---------MDYDAM-YLraqklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170
....*....|..
gi 896182242 182 KVMLFDEPTAAL 193
Cdd:PRK13549 163 RLLILDEPTASL 174
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
36-271 |
1.29e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.32 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 36 TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSS--GQVELLGAPL--TKLRAHERATrLAYLPQHTPADTAI 111
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkaSNIRDTERAG-IVIIHQELTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 112 DVRTVVALGRYAHHRRRDRFRSSLNSTDHDIVA-YALDRVGVTaladRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPT 190
Cdd:TIGR02633 94 SVAENIFLGNEITLPGGRMAYNAMYLRAKNLLReLQLDADNVT----RPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 191 AALDigfQLEILELLGELAD-EGHGIGVVL--HDLNLAARSCHRLSVIHNGGlEVTGSAEEVLTPPRIDAIY---RISSA 264
Cdd:TIGR02633 170 SSLT---EKETEILLDIIRDlKAHGVACVYisHKLNEVKAVCDTICVIRDGQ-HVATKDMSTMSEDDIITMMvgrEITSL 245
|
....*..
gi 896182242 265 VDTDPHT 271
Cdd:TIGR02633 246 YPHEPHE 252
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
27-194 |
1.31e-14 |
|
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: 71.49 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYR-NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHT 105
Cdd:cd03253 5 NVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 PA--DTaidVRTVVALGRyahhrrrdrfrssLNSTDHDIVAYAL-----DRVGV------TALADRPiTALSGGQRQLVF 172
Cdd:cd03253 85 VLfnDT---IGYNIRYGR-------------PDATDEEVIEAAKaaqihDKIMRfpdgydTIVGERG-LKLSGGEKQRVA 147
|
170 180
....*....|....*....|..
gi 896182242 173 IAKLLAQQAKVMLFDEPTAALD 194
Cdd:cd03253 148 IARAILKNPPILLLDEATSALD 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
44-222 |
1.53e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 44 AIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVE---------------LLGAPLTKLRAHEraTRLAYLPQHtpad 108
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdevlkrfrgtELQNYFKKLYNGE--IKVVHKPQY---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 109 taIDVRTVVALGRyahhrrrdrFRSSLNSTD-HDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFD 187
Cdd:PRK13409 169 --VDLIPKVFKGK---------VRELLKKVDeRGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*
gi 896182242 188 EPTAALDIGfQLEILELLGELADEGHGIGVVLHDL 222
Cdd:PRK13409 238 EPTSYLDIR-QRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-195 |
1.57e-14 |
|
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: 73.43 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVElLGApltklraherATRLAYLp 102
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGE----------TVKLAYV- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 qhtpadtaidvrtvvalgryahhrrrDRFRSSL--NSTDHDIVAYALD--RVGVTALADR---------------PITAL 163
Cdd:TIGR03719 391 --------------------------DQSRDALdpNKTVWEEISGGLDiiKLGKREIPSRayvgrfnfkgsdqqkKVGQL 444
|
170 180 190
....*....|....*....|....*....|..
gi 896182242 164 SGGQRQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
41-249 |
1.81e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 71.71 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAP-----LTKLRAHeratrLAYLPQHtPADTAID--V 113
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnFEKLRKH-----IGIVFQN-PDNQFVGsiV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALGRYAHHRRRDRFrsslnstdHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAAL 193
Cdd:PRK13648 102 KYDVAFGLENHAVPYDEM--------HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 896182242 194 D-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHrLSVIHNGGLEVTGSAEEV 249
Cdd:PRK13648 174 DpDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-255 |
2.29e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.56 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRT-VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAY 100
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQHTPaDTAIDVRTV----------VALGRYAHHRRRDRfrsslnstdhdivayALDRVGVTALADRPITALSGGQRQL 170
Cdd:PRK13644 81 IVFQNP-ETQFVGRTVeedlafgpenLCLPPIEIRKRVDR---------------ALAEIGLEKYRHRSPKTLSGGQGQC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNlAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVL 223
|
....*
gi 896182242 251 TPPRI 255
Cdd:PRK13644 224 SDVSL 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-266 |
2.43e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.37 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGyrnrtvVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE----RATR 97
Cdd:PRK10070 34 ILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 LAYLPQH---TPADTAIDVRTV-VALGRYAHHRRRDRfrsSLNstdhdivayALDRVGVTALADRPITALSGGQRQLVFI 173
Cdd:PRK10070 108 IAMVFQSfalMPHMTVLDNTAFgMELAGINAEERREK---ALD---------ALRQVGLENYAHSYPDELSGGMRQRVGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 174 AKLLAQQAKVMLFDEPTAALDIGFQLEIL-ELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTP 252
Cdd:PRK10070 176 ARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
250
....*....|....
gi 896182242 253 PRIDAIYRISSAVD 266
Cdd:PRK10070 256 PANDYVRTFFRGVD 269
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
23-194 |
2.80e-14 |
|
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: 69.26 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGY--RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAhERATRLAY 100
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQhtpadtaidvrtvvalgryahhrRRDRFRSSLnstdhdivayaLDRVGvtaladrpiTALSGGQRQLVFIAKLLAQQ 180
Cdd:cd03247 80 LNQ-----------------------RPYLFDTTL-----------RNNLG---------RRFSGGERQRLALARILLQD 116
|
170
....*....|....
gi 896182242 181 AKVMLFDEPTAALD 194
Cdd:cd03247 117 APIVLLDEPTVGLD 130
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-250 |
2.83e-14 |
|
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: 72.85 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGY-RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYL 101
Cdd:TIGR01193 474 IVINDVSYSYgYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHtPADTAIDVRTVVALGRYAHHRRRDRFRS-SLNSTDHDIVAYALdrvGV-TALADRPiTALSGGQRQLVFIAKLLAQ 179
Cdd:TIGR01193 554 PQE-PYIFSGSILENLLLGAKENVSQDEIWAAcEIAEIKDDIENMPL---GYqTELSEEG-SSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 180 QAKVMLFDEPTAALDIGFQLEILELLGELADEghGIGVVLHDLNLAARScHRLSVIHNGGLEVTGSAEEVL 250
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELL 696
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
38-249 |
3.12e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.92 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHtpADTAIDVRTV- 116
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQN--PDNQFVGATVe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 117 --VALGR----YAHHRRRDRfrsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPT 190
Cdd:PRK13650 101 ddVAFGLenkgIPHEEMKER------------VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 191 AALDIGFQLEILELLGELADEgHGIGV--VLHDLNLAARScHRLSVIHNGGLEVTGSAEEV 249
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDD-YQMTVisITHDLDEVALS-DRVLVMKNGQVESTSTPREL 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-254 |
3.29e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 16 DTDSTALLRATDLSVGYRNR-----------TVVSGVNLAIRPGEVQGIIGSNGTGKSS----LLRAMAgivtpSSGQVE 80
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFPIRkgilkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 81 LLGAPLTKLRAHE-----RATRLAYLPQHTPADTAIDVRTVVALGRYAHHRrrdrfrsSLNSTDHDI-VAYALDRVGV-T 153
Cdd:PRK15134 344 FDGQPLHNLNRRQllpvrHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQP-------TLSAAQREQqVIAVMEEVGLdP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 154 ALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELaDEGHGIGVVL--HDLNLAARSCHR 231
Cdd:PRK15134 417 ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL-QQKHQLAYLFisHDLHVVRALCHQ 495
|
250 260
....*....|....*....|...
gi 896182242 232 LSVIHNGGLEVTGSAEEVLTPPR 254
Cdd:PRK15134 496 VIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
41-194 |
3.35e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLG-------APLTK-LRAHERATRLAY-----LPQHTPA 107
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSDKaIRELRRNVGMVFqqynlWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 108 DTAIDVRT-VVALGRYAHHRRRDRFrsslnstdhdivayaLDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLF 186
Cdd:PRK11124 101 QNLIEAPCrVLGLSKDQALARAEKL---------------LERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
....*...
gi 896182242 187 DEPTAALD 194
Cdd:PRK11124 166 DEPTAALD 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
34-194 |
3.37e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.67 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRL-----AYLPQHTPAD 108
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMvfqsyALFPHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 109 TaidvrtvVALGRYAHHRRRDRFRSSlnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDE 188
Cdd:PRK11432 98 N-------VGYGLKMLGVPKEERKQR--------VKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
....*.
gi 896182242 189 PTAALD 194
Cdd:PRK11432 163 PLSNLD 168
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
27-194 |
4.11e-14 |
|
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: 69.95 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQht 105
Cdd:cd03254 7 NVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 paDTAIDVRTVvalgryahhrrRDRFRSSLNSTDHDIVAYALDRVGV------------TALADRPiTALSGGQRQLVFI 173
Cdd:cd03254 85 --DTFLFSGTI-----------MENIRLGRPNATDEEVIEAAKEAGAhdfimklpngydTVLGENG-GNLSQGERQLLAI 150
|
170 180
....*....|....*....|.
gi 896182242 174 AKLLAQQAKVMLFDEPTAALD 194
Cdd:cd03254 151 ARAMLRDPKILILDEATSNID 171
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
41-253 |
4.32e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.82 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELlGAplTKLRAHERATRLAYLPQHtpadtaidvrtVVALG 120
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GE--RVITAGKKNKKLKPLRKK-----------VGIVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 121 RYAHHRRrdrFRSSLnstDHDI-----------------VAYALDRVGVT-ALADRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:PRK13634 92 QFPEHQL---FEETV---EKDIcfgpmnfgvseedakqkAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896182242 183 VMLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:PRK13634 166 VLVLDEPTAGLDpKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
29-240 |
4.59e-14 |
|
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: 69.12 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 29 SVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAG--IVTPSSGQVELLGAPLTKlraHERATRLAYLPQHtp 106
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 107 aDTAIDVRTVVALGRYAHHRRRdrfrsslnstdhdivayaldrvgvtaladrpitaLSGGQRQLVFIAKLLAQQAKVMLF 186
Cdd:cd03213 91 -DILHPTLTVRETLMFAAKLRG----------------------------------LSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 187 DEPTAALDIGFQLEILELLGELADEGHGIGVVLHDL-NLAARSCHRLSVIHNGGL 240
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
37-194 |
5.64e-14 |
|
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: 71.91 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 37 VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHTPADTAIDVRTV 116
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI 547
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 117 VALGRYAHHRRRDRFRssLNSTDHDIVAYALdrvGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:TIGR03797 548 AGGAPLTLDEAWEAAR--MAGLAEDIRAMPM---GMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-254 |
8.11e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.69 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIV------TPSSGQVELLGAPLTKLRAHERATRLAYLPQHTPA 107
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 108 DTAIDVRTVVALGRYAHHRRRDRfrsslnsTDHDIVAYALDRVGV-TALADR---PITALSGGQRQLVFIAKLLAQQAKV 183
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKR-------EIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 184 MLFDEPTAALDIGFQLEILELLGELADEgHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPR 254
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
37-194 |
9.25e-14 |
|
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: 68.26 E-value: 9.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 37 VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGapltklraheratRLAYLPQhTP---ADTaidV 113
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQ-EPwiqNGT---I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALGRYAHHRRRDRFrsslnstdhdIVAYALDR------------VGvtalaDRPITaLSGGQRQLVFIAKLLAQQA 181
Cdd:cd03250 83 RENILFGKPFDEERYEKV----------IKACALEPdleilpdgdlteIG-----EKGIN-LSGGQKQRISLARAVYSDA 146
|
170
....*....|...
gi 896182242 182 KVMLFDEPTAALD 194
Cdd:cd03250 147 DIYLLDDPLSAVD 159
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-194 |
1.02e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.42 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAM--AGIVTPS---SGQVELLGAPLTKLRAHE 93
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 94 RATRLA---YLPQHTPADTAIDVRTVVAL---GRYAHHRRRDRFRSSLNSTDhdIVAYALDRVGVTALAdrpitaLSGGQ 167
Cdd:PRK14239 82 VDLRKEigmVFQQPNPFPMSIYENVVYGLrlkGIKDKQVLDEAVEKSLKGAS--IWDEVKDRLHDSALG------LSGGQ 153
|
170 180
....*....|....*....|....*..
gi 896182242 168 RQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
10-250 |
1.22e-13 |
|
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: 70.93 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 10 DHVTKPDTDSTALLRATDLSVGYRNRT---------VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVE 80
Cdd:TIGR01846 436 NSPTEPRSAGLAALPELRGAITFENIRfryapdspeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVL 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 81 LLGAPLTKLRAHERATRLAYLPQHTPADTAiDVRTVVALGRYAHHRRRDRFRSSLNSTdHDIVAyALDRVGVTALADRPI 160
Cdd:TIGR01846 516 VDGVDLAIADPAWLRRQMGVVLQENVLFSR-SIRDNIALCNPGAPFEHVIHAAKLAGA-HDFIS-ELPQGYNTEVGEKGA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 161 tALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELAdEGHGIGVVLHDLNlAARSCHRLSVIHNGGL 240
Cdd:TIGR01846 593 -NLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLS-TVRACDRIIVLEKGQI 669
|
250
....*....|
gi 896182242 241 EVTGSAEEVL 250
Cdd:TIGR01846 670 AESGRHEELL 679
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-195 |
1.24e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 32 YRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGapltkLRAHERATRLAY----------- 100
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPFKRRKEFARrigvvfgqrsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 ----LPqhtPADTAIDVRTVVALGRYAHHRRRDRFRSSLnstdhdivayaldrvGVTALADRPITALSGGQRQLV-FIAK 175
Cdd:COG4586 107 lwwdLP---AIDSFRLLKAIYRIPDAEYKKRLDELVELL---------------DLGELLDTPVRQLSLGQRMRCeLAAA 168
|
170 180
....*....|....*....|
gi 896182242 176 LLaQQAKVMLFDEPTAALDI 195
Cdd:COG4586 169 LL-HRPKILFLDEPTIGLDV 187
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-253 |
1.49e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.52 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNRT---VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQ 103
Cdd:TIGR00958 483 DVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 104 HtPADTAIDVRTVVALGryahhrrrdrfrssLNSTDHDIVAYAldrvGVTALADRPITA---------------LSGGQR 168
Cdd:TIGR00958 563 E-PVLFSGSVRENIAYG--------------LTDTPDEEIMAA----AKAANAHDFIMEfpngydtevgekgsqLSGGQK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 169 QLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGEladEGHGIGVVLHDLNLaARSCHRLSVIHNGGLEVTGSAEE 248
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLST-VERADQILVLKKGSVVEMGTHKQ 699
|
....*
gi 896182242 249 VLTPP 253
Cdd:TIGR00958 700 LMEDQ 704
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
33-255 |
1.59e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 33 RNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATR-LAYLPQhTPADTAI 111
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYITE-SRRDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 112 ----DVRTVVALGRYAhhrRRDRFRSSLNSTDH-DIVAYALDRVGVTALA----DRPITALSGGQRQLVFIAKLLAQQAK 182
Cdd:PRK09700 353 fpnfSIAQNMAISRSL---KDGGYKGAMGLFHEvDEQRTAENQRELLALKchsvNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896182242 183 VMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRI 255
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEI 502
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-196 |
1.91e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 31 GYRNRTV---------VSG------VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLtKLRAHERA 95
Cdd:PRK11288 247 GYRPRPLgevrlrldgLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 96 TR--LAYLPQHTPADTAIDVRTV---VALGRYAHHRRrdrFRSSLNS------TDHDIVAYALDrvgvTALADRPITALS 164
Cdd:PRK11288 326 IRagIMLCPEDRKAEGIIPVHSVadnINISARRHHLR---AGCLINNrweaenADRFIRSLNIK----TPSREQLIMNLS 398
|
170 180 190
....*....|....*....|....*....|..
gi 896182242 165 GGQRQLVFIAKLLAQQAKVMLFDEPTAALDIG 196
Cdd:PRK11288 399 GGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-195 |
4.09e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.15 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVellgapltklRAHERAtRLAYLP 102
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENA-NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 QHTPADTAID-------------------VRTVvaLGRYahhrrrdrfrssLNSTDhDIvayaldrvgvtalaDRPITAL 163
Cdd:PRK15064 389 QDHAYDFENDltlfdwmsqwrqegddeqaVRGT--LGRL------------LFSQD-DI--------------KKSVKVL 439
|
170 180 190
....*....|....*....|....*....|..
gi 896182242 164 SGGQRQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM 471
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-241 |
4.12e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 69.04 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 14 KPDTDSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELlgapltklrahE 93
Cdd:PRK10636 304 APESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------A 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 94 RATRLAYLPQHTPADTAIDVRTVVALGRYAHHRRRDRFRSSLNStdhdivaYALDRVGVTALADRpitaLSGGQRQLVFI 173
Cdd:PRK10636 373 KGIKLGYFAQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGG-------FGFQGDKVTEETRR----FSGGEKARLVL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 174 AKLLAQQAKVMLFDEPTAALDIGFQLEILELLGelaDEGHGIGVVLHDLNLAARSCHRLSVIHNGGLE 241
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI---DFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-194 |
4.14e-13 |
|
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: 66.67 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNR--TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGA-----PLTKLRaheraTRLA 99
Cdd:cd03369 11 NLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLR-----SSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPQhtpaDTAIDVRTVvalgryahhrrrdrfRSSLNSTDH--DIVAYALDRVGVTALadrpitALSGGQRQLVFIAKLL 177
Cdd:cd03369 86 IIPQ----DPTLFSGTI---------------RSNLDPFDEysDEEIYGALRVSEGGL------NLSQGQRQLLCLARAL 140
|
170
....*....|....*..
gi 896182242 178 AQQAKVMLFDEPTAALD 194
Cdd:cd03369 141 LKRPRVLVLDEATASID 157
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-249 |
4.74e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.27 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 18 DSTALLRATDLSVGYRNRT--VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAP-LTKLRahER 94
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNIS--DV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 95 ATRLAYLPQHTPADTAIDVRTVVALgrYAhhrrrdRFRSSLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIA 174
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGREHLYL--YA------RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTA 2082
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 175 KLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEV 249
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-241 |
7.28e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.31 E-value: 7.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 13 TKPDTDSTALLRATDLS---VGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGiVTPS--SGQVELLGAPL- 86
Cdd:TIGR02633 248 HEPHEIGDVILEARNLTcwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKPVd 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 87 TKLRAHERATRLAYLPQHTPADTAIDVR------TVVALGRYAHHRRRDrfrsslNSTDHDIVAYALDRVGV-TALADRP 159
Cdd:TIGR02633 327 IRNPAQAIRAGIAMVPEDRKRHGIVPILgvgkniTLSVLKSFCFKMRID------AAAELQIIGSAIQRLKVkTASPFLP 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 160 ITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGG 239
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
..
gi 896182242 240 LE 241
Cdd:TIGR02633 481 LK 482
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-254 |
1.12e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.07 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRNRTV----VSGVNLAIRPGEVQGIIGSNGTGKS-SLLRAMAGIVTP---SSGQVELLGAPLTKLRAH 92
Cdd:PRK11022 2 ALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 93 ER----ATRLAYLPQH-----TPADTaIDVRTVVALGRYAHHRRRDRFRSSLNstdhdivayALDRVGVTALADR----P 159
Cdd:PRK11022 82 ERrnlvGAEVAMIFQDpmtslNPCYT-VGFQIMEAIKVHQGGNKKTRRQRAID---------LLNQVGIPDPASRldvyP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 160 iTALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLE-ILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:PRK11022 152 -HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQiIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG 230
|
250
....*....|....*.
gi 896182242 239 GLEVTGSAEEVLTPPR 254
Cdd:PRK11022 231 QVVETGKAHDIFRAPR 246
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
27-240 |
1.47e-12 |
|
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: 65.57 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNRT---VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRaHERATRLAYLPQ 103
Cdd:cd03248 16 NVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 104 HTPADTAIDVRTVVALGryahhrrrdrfrssLNSTDHDIVAYALDRVG----VTALADRPITA-------LSGGQRQLVF 172
Cdd:cd03248 95 QEPVLFARSLQDNIAYG--------------LQSCSFECVKEAAQKAHahsfISELASGYDTEvgekgsqLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 173 IAKLLAQQAKVMLFDEPTAALDIGFQlEILELLGELADEGHGIGVVLHDLNLAARScHRLSVIHNGGL 240
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESE-QQVQQALYDWPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-254 |
1.80e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.63 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPS-----SGQVELLG-----APLTKLRAH 92
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGrniysPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 93 ERATRLAYLPQHTPADTAIDVrtvVALGRyahhrRRDRFRSSLNSTDhDIVAYALDRVGV-----TALADRPiTALSGGQ 167
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDN---VAIGV-----KLNGLVKSKKELD-ERVEWALKKAALwdevkDRLNDYP-SNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 168 RQLVFIAKLLAQQAKVMLFDEPTAALD-IGFQLEILELLGELADegHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSA 246
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDpVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
....*...
gi 896182242 247 EEVLTPPR 254
Cdd:PRK14267 233 RKVFENPE 240
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-195 |
2.14e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 19 STALLRATDLSVGYRNR--TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERAT 96
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 97 RLAYLPQhTPADTAIDVRtvVALGRYAHHRRRDRFRSSLNSTDHDIVAYalDRVGVTALADRPITALSGGQRQLVFIAKL 176
Cdd:PLN03232 1311 VLSIIPQ-SPVLFSGTVR--FNIDPFSEHNDADLWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARA 1385
|
170
....*....|....*....
gi 896182242 177 LAQQAKVMLFDEPTAALDI 195
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDV 1404
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-261 |
2.27e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.58 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRT---------VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAH 92
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 93 ERATRLAYLPQHtpADTAIDVRTVVAlgryahhRRRD---RFRSSLNSTDHDIVAYA-LDRVGVtaLADRPIT---ALSG 165
Cdd:PRK15112 84 YRSQRIRMIFQD--PSTSLNPRQRIS-------QILDfplRLNTDLEPEQREKQIIEtLRQVGL--LPDHASYyphMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 166 GQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELaDEGHGIGV--VLHDLNLAARSCHRLSVIHNGGLEVT 243
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL-QEKQGISYiyVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250
....*....|....*...
gi 896182242 244 GSAEEVLTPPRIDAIYRI 261
Cdd:PRK15112 232 GSTADVLASPLHELTKRL 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-194 |
2.99e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIV--TPSSGQVELLGAPLTklrahERATRL 98
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG-----REASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQHTPADTAIDVRTVVALGryahhrrrdrfrsslnstdhDIVAYAldrvgvtaladRPITALSGGQRQLVFIAKLLA 178
Cdd:COG2401 104 DAIGRKGDFKDAVELLNAVGLS--------------------DAVLWL-----------RRFKELSTGQKFRFRLALLLA 152
|
170
....*....|....*.
gi 896182242 179 QQAKVMLFDEPTAALD 194
Cdd:COG2401 153 ERPKLLVIDEFCSHLD 168
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-253 |
3.24e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTP---SSGQVELLGAPLTKLRAHERATRLAYL 101
Cdd:PRK13640 10 HVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHtpADTAIDVRTV---VALGRYAHHRRRDRFRSslnstdhdIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLA 178
Cdd:PRK13640 90 FQN--PDNQFVGATVgddVAFGLENRAVPRPEMIK--------IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 179 QQAKVMLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLsVIHNGGLEVTGSAEEVLTPP 253
Cdd:PRK13640 160 VEPKIIILDESTSMLDpAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVL-VLDDGKLLAQGSPVEIFSKV 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-196 |
4.89e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.30 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 10 DHVTKPDTDSTALLRATDLSVGYRNR--TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLT 87
Cdd:PLN03130 1225 NNRPPPGWPSSGSIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 88 KLRAHERATRLAYLPQhTPADTAIDVRtvVALGRYAHHRRRDRFRSSLNSTDHDIVAYalDRVGVTALADRPITALSGGQ 167
Cdd:PLN03130 1305 KFGLMDLRKVLGIIPQ-APVLFSGTVR--FNLDPFNEHNDADLWESLERAHLKDVIRR--NSLGLDAEVSEAGENFSVGQ 1379
|
170 180
....*....|....*....|....*....
gi 896182242 168 RQLVFIAKLLAQQAKVMLFDEPTAALDIG 196
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-246 |
5.56e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLS-VGYRNrtvvsgVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHER-ATRLA 99
Cdd:PRK15439 268 VLTVEDLTgEGFRN------ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPQ-------HTPADTAIDVRTVVA------LGRYAHHRRRDRFRSSLNSTDHDivayaldrvgvtalADRPITALSGG 166
Cdd:PRK15439 342 YLPEdrqssglYLDAPLAWNVCALTHnrrgfwIKPARENAVLERYRRALNIKFNH--------------AEQAARTLSGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 167 QRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGL--EVTG 244
Cdd:PRK15439 408 NQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIsgALTG 487
|
..
gi 896182242 245 SA 246
Cdd:PRK15439 488 AA 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-195 |
1.07e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVElLGApltklraherATRLAYLp 102
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGE----------TVKLAYV- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 103 qhtpadtaidvrtvvalgryahhrrrDRFRSSLN---------STDHDIVayaldRVGVTALADR--------------- 158
Cdd:PRK11819 393 --------------------------DQSRDALDpnktvweeiSGGLDII-----KVGNREIPSRayvgrfnfkggdqqk 441
|
170 180 190
....*....|....*....|....*....|....*..
gi 896182242 159 PITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:PRK11819 442 KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-194 |
1.16e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.87 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 1 MSQQTQNLTDHVTKPDTDSTALLRATDLSVGYRNRTVVSG-VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVtPSSGQ- 78
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSl 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 79 ----VELLGAPLTKLRAHeratrLAYLPQ--HTPADTaidVRTVVALGRyaHHRRRDRFRSSLNSTD-HDIV---AYALD 148
Cdd:PRK11174 407 kingIELRELDPESWRKH-----LSWVGQnpQLPHGT---LRDNVLLGN--PDASDEQLQQALENAWvSEFLpllPQGLD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 896182242 149 rvgvTALADRPITaLSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK11174 477 ----TPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-194 |
1.35e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 24 RATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKlRAHERAT--RLAYL 101
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-ARHRRAVcpRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQhtpadtaidvrtvvALGR--Y-------------------AHHRRRdRFRSSLNSTdhdivayaldrvGVTALADRPI 160
Cdd:NF033858 82 PQ--------------GLGKnlYptlsvfenldffgrlfgqdAAERRR-RIDELLRAT------------GLAPFADRPA 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 896182242 161 TALSGGQRQlvfiaKL-----LAQQAKVMLFDEPTAALD 194
Cdd:NF033858 135 GKLSGGMKQ-----KLglccaLIHDPDLLILDEPTTGVD 168
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
34-194 |
1.67e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 64.35 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQhTP---ADTa 110
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ-TPflfSDT- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 111 idVRTVVALGRYAHHRRRDRFRSSLNSTDHDIVayALDRVGVTALADRPITaLSGGQRQLVFIAKLLAQQAKVMLFDEPT 190
Cdd:PRK10789 405 --VANNIALGRPDATQQEIEHVARLASVHDDIL--RLPQGYDTEVGERGVM-LSGGQKQRISIARALLLNAEILILDDAL 479
|
....
gi 896182242 191 AALD 194
Cdd:PRK10789 480 SAVD 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
39-193 |
2.04e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 39 SGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGiVTPS---SGQVELLGAPLT--KLRAHERA------TRLAYLPQHTPA 107
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRfkDIRDSEALgiviihQELALIPYLSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 108 DTaidvrtvVALGryahHRRRDRFRSSLNSTDHDIVAYaLDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFD 187
Cdd:NF040905 97 EN-------IFLG----NERAKRGVIDWNETNRRAREL-LAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
....*.
gi 896182242 188 EPTAAL 193
Cdd:NF040905 165 EPTAAL 170
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-194 |
2.44e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERaTRLAYL 101
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ-KQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PQHTPADTAIDVRTVVAlgrYAHHrrrdrFRSSLNSTDHDIVAYALDRvgvtaLADRPITALSGGQRQLVFIAKLLAQQA 181
Cdd:PRK13540 80 GHRSGINPYLTLRENCL---YDIH-----FSPGAVGITELCRLFSLEH-----LIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170
....*....|...
gi 896182242 182 KVMLFDEPTAALD 194
Cdd:PRK13540 147 KLWLLDEPLVALD 159
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-194 |
5.17e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSS-----GQVELLGAPLTKLRAH-ERAT 96
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 97 RLAYLPQHTPADTAIDVRTVVA-----LGRYAHHRRRDRFRSSLNSTD------HDIVAYALDrvgvtaladrpitaLSG 165
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAygvkiVGWRPKLEIDDIVESALKDADlwdeikHKIHKSALD--------------LSG 153
|
170 180
....*....|....*....|....*....
gi 896182242 166 GQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-194 |
5.31e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.53 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRNRT--VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRahERATRl 98
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS--EAALR- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 aylpqhtpadTAIdvrTVVAlgryahhRRRDRFRSSL---------NSTDHDIVAyALDRVGVTALAD------------ 157
Cdd:PRK11160 414 ----------QAI---SVVS-------QRVHLFSATLrdnlllaapNASDEALIE-VLQQVGLEKLLEddkglnawlgeg 472
|
170 180 190
....*....|....*....|....*....|....*...
gi 896182242 158 -RPitaLSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK11160 473 gRQ---LSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-194 |
8.87e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 26 TDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSS--GQVELLGAPLTKlrahERATRLAYLPQ 103
Cdd:PLN03211 72 SDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 104 HT---PADTAIDVRTVVALGRYAHHRRRDrfrSSLNSTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQ 180
Cdd:PLN03211 148 DDilyPHLTVRETLVFCSLLRLPKSLTKQ---EKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLIN 224
|
170
....*....|....
gi 896182242 181 AKVMLFDEPTAALD 194
Cdd:PLN03211 225 PSLLILDEPTSGLD 238
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-198 |
1.85e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 18 DSTALLRATDLSVGY--------RNRTV--VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQ-----VELL 82
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElyyqgQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 83 GAPLTKLRAHERATRLAYL-------PQHTPADT---AIDVRTvvALGRyahHRRRDRfrsslnstdhdiVAYALDRVGV 152
Cdd:PRK11308 81 KADPEAQKLLRQKIQIVFQnpygslnPRKKVGQIleePLLINT--SLSA---AERREK------------ALAMMAKVGL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 896182242 153 -TALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQ 198
Cdd:PRK11308 144 rPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-95 |
1.89e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 17 TDSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGivTPS----SGQVELLGAPLTKLRAH 92
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPE 79
|
...
gi 896182242 93 ERA 95
Cdd:CHL00131 80 ERA 82
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-195 |
2.10e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGI--VTPSSGQVELLGAPLTKLRAHERATRLA 99
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPQHTPAD-----TAIDVRTVV-ALGRYAHHRRRDRFrsslnstdhDIVAYALDRVGVTALADRPIT-----ALSGGQR 168
Cdd:PRK09580 81 FMAFQYPVEipgvsNQFFLQTALnAVRSYRGQEPLDRF---------DFQDLMEEKIALLKMPEDLLTrsvnvGFSGGEK 151
|
170 180
....*....|....*....|....*..
gi 896182242 169 QLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDI 178
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-194 |
2.12e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.43 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 29 SVGYRN------RTVVS-GVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVeLLGApltklraheraTRLAYL 101
Cdd:PRK11000 3 SVTLRNvtkaygDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGE-----------KRMNDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 102 PqhtPADTAID-VRTVVALgrYAHHRRRDR--FRSSLNSTDH-DI---VAYALDRVGVTALADRPITALSGGQRQLVFIA 174
Cdd:PRK11000 71 P---PAERGVGmVFQSYAL--YPHLSVAENmsFGLKLAGAKKeEInqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIG 145
|
170 180
....*....|....*....|
gi 896182242 175 KLLAQQAKVMLFDEPTAALD 194
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLD 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-195 |
2.73e-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: 61.11 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNRT--VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQh 104
Cdd:TIGR00957 1289 NYCLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ- 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 TPADTAIDVRtvVALGRYAHHRRRDRFRSSLNSTDHDIVAYALDrvGVTALADRPITALSGGQRQLVFIAKLLAQQAKVM 184
Cdd:TIGR00957 1368 DPVLFSGSLR--MNLDPFSQYSDEEVWWALELAHLKTFVSALPD--KLDHECAEGGENLSVGQRQLVCLARALLRKTKIL 1443
|
170
....*....|.
gi 896182242 185 LFDEPTAALDI 195
Cdd:TIGR00957 1444 VLDEATAAVDL 1454
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-195 |
2.98e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELlGaplTKLRaheratrLAYLPQH-- 104
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-G---TKLE-------VAYFDQHra 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 --TPADTAID-----VRTVVALGRYAHhrrrdrfrsslnstdhdIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLL 177
Cdd:PRK11147 393 elDPEKTVMDnlaegKQEVMVNGRPRH-----------------VLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLF 455
|
170
....*....|....*...
gi 896182242 178 AQQAKVMLFDEPTAALDI 195
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDV 473
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
40-194 |
4.68e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.99 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 40 GVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGaplTKLRAHERATRLAYLPQHTP-----ADTAIDVR 114
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDD---TLITSTSKNKDIKQIRKKVGlvfqfPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 115 TV---VALGRyahhrrrdrfrSSLNSTDHDIVAYALDR---VGVT-ALADRPITALSGGQRQLVFIAKLLAQQAKVMLFD 187
Cdd:PRK13649 102 TVlkdVAFGP-----------QNFGVSQEEAEALAREKlalVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
....*..
gi 896182242 188 EPTAALD 194
Cdd:PRK13649 171 EPTAGLD 177
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-196 |
4.75e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHER-ATRLAYLPQHTPADTAI---DV 113
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEDRKRDGLVlgmSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 R---TVVALGRYAHHRRRDRFRSSLNSTDHDIVAYALDrvgvTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPT 190
Cdd:PRK10762 348 KenmSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIK----TPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
....*.
gi 896182242 191 AALDIG 196
Cdd:PRK10762 424 RGVDVG 429
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-246 |
5.25e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 21 ALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAhERATR--L 98
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT-AKIMReaV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQHTPADTAIDVRTVVALGRYahHRRRDRFRSSLNSTdHDIVAYALDRvgvtaLADRPITaLSGGQRQLVFIAKLLA 178
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGF--FAERDQFQERIKWV-YELFPRLHER-----RIQRAGT-MSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 179 QQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGG--LEVTGSA 246
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHvvLEDTGDA 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
34-195 |
5.38e-10 |
|
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: 58.11 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHTPADTAIDV 113
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALGRYAHHRRRDRFRSSLNST----DHDIVAYAlDRvgvTALADRPITaLSGGQRQLVFIAKLLAQQAKVMLFDEP 189
Cdd:cd03290 93 ATVEENITFGSPFNKQRYKAVTDACslqpDIDLLPFG-DQ---TEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDP 167
|
....*.
gi 896182242 190 TAALDI 195
Cdd:cd03290 168 FSALDI 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
27-194 |
5.38e-10 |
|
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: 58.40 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQH 104
Cdd:cd03251 5 NVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 TP--ADTaidVRTVVALGRyahhrrrdrfrssLNSTDHDIV-----AYALDRV-----GV-TALADRPITaLSGGQRQLV 171
Cdd:cd03251 85 VFlfNDT---VAENIAYGR-------------PGATREEVEeaaraANAHEFImelpeGYdTVIGERGVK-LSGGQRQRI 147
|
170 180
....*....|....*....|...
gi 896182242 172 FIAKLLAQQAKVMLFDEPTAALD 194
Cdd:cd03251 148 AIARALLKDPPILILDEATSALD 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
41-193 |
6.21e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPL---TKLRAHERATRLAylpqHTPADTAIDvRTVV 117
Cdd:PRK10982 17 VNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMV----HQELNLVLQ-RSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 118 A---LGRYA-------HHRRRDRFRSSLNSTDHDIVAYalDRVGvtaladrpitALSGGQRQLVFIAKLLAQQAKVMLFD 187
Cdd:PRK10982 92 DnmwLGRYPtkgmfvdQDKMYRDTKAIFDELDIDIDPR--AKVA----------TLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
....*.
gi 896182242 188 EPTAAL 193
Cdd:PRK10982 160 EPTSSL 165
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
38-194 |
7.65e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.29 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVnlaIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPS---SGQVELLGAPLTKLRAHERAtrlAYLPQH---TPADTAI 111
Cdd:TIGR00955 44 VSGV---AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS---AYVQQDdlfIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 112 DVRTVVAlgryahHRRRDRFRSSlnSTDHDIVAYALDRVGVTALADRPITA------LSGGQRQLVFIAKLLAQQAKVML 185
Cdd:TIGR00955 118 EHLMFQA------HLRMPRRVTK--KEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLF 189
|
....*....
gi 896182242 186 FDEPTAALD 194
Cdd:TIGR00955 190 CDEPTSGLD 198
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-255 |
9.44e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 58.32 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSVGYRNRT-----VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEL--------------L 82
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 83 GAPLT-KLRAHERATRLAYL----PQHTPADTAIDVRTV---VALGRyahHRRRDRFRSslnstdhdivAYALDRVGV-T 153
Cdd:PRK13631 101 TNPYSkKIKNFKELRRRVSMvfqfPEYQLFKDTIEKDIMfgpVALGV---KKSEAKKLA----------KFYLNKMGLdD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 154 ALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLS 233
Cdd:PRK13631 168 SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVI 247
|
250 260
....*....|....*....|..
gi 896182242 234 VIHNGGLEVTGSAEEVLTPPRI 255
Cdd:PRK13631 248 VMDKGKILKTGTPYEIFTDQHI 269
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-194 |
1.27e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTP-SSGQVELLGapltklraheratRLAYLPQHTPADTAIdV 113
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRG-------------TVAYVPQVSWIFNAT-V 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALGRyahHRRRDRFRSSLNST--DHDIVayALDRVGVTALADRPITaLSGGQRQLVFIAKLLAQQAKVMLFDEPTA 191
Cdd:PLN03130 696 RDNILFGS---PFDPERYERAIDVTalQHDLD--LLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
...
gi 896182242 192 ALD 194
Cdd:PLN03130 770 ALD 772
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
38-238 |
1.28e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.80 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHtPADTAI--DVRT 115
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN-PDNQFVgaTVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 116 VVALGRYAHHRRRDRFRSSLNStdhdivayALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKRVDE--------ALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896182242 196 GFQLEILELLGELADEGH-GIGVVLHDLNLAARScHRLSVIHNG 238
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASS-DRILVMKAG 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
38-265 |
1.46e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGA-----PLTKLRAHERATRLAYL-------PQHT 105
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlSPGKLQALRRDIQFIFQdpyasldPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 PADTAIDVRTVVALGRYAHHRRRdrfrsslnstdhdiVAYALDRVGVTA-LADRPITALSGGQRQLVFIAKLLAQQAKVM 184
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAAR--------------VAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 185 LFDEPTAALDIGFQLEILELLGELADEgHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPPRIDAIYRIS 262
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRD-FGIAYLFisHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
...
gi 896182242 263 SAV 265
Cdd:PRK10261 565 AAV 567
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
36-250 |
1.69e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.40 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 36 TVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLgapltklRAHERATRLAYLPQHTPADTAIDVRT 115
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWI-------FKDEKNKKKTKEKEKVLEKLVIQKTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 116 VVALGRYAHHRRR----------DRFRSSLnstDHDIV----------AYALDR-------VGV-TALADRPITALSGGQ 167
Cdd:PRK13651 94 FKKIKKIKEIRRRvgvvfqfaeyQLFEQTI---EKDIIfgpvsmgvskEEAKKRaakyielVGLdESYLQRSPFELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 168 RQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAE 247
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTY 250
|
...
gi 896182242 248 EVL 250
Cdd:PRK13651 251 DIL 253
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-189 |
1.94e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.08 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 2 SQQTQNLTDhvtkpdtdstalLRATDLSVGyrNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEL 81
Cdd:PRK11831 1 EQSVANLVD------------MRGVSFTRG--NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 82 LG---APLTKLRAHERATRLAYLPQHTPADTAIDVRTVVALGRYAHHRRRDRFrssLNSTdhdiVAYALDRVGVTALADR 158
Cdd:PRK11831 67 DGeniPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPL---LHST----VMMKLEAVGLRGAAKL 139
|
170 180 190
....*....|....*....|....*....|.
gi 896182242 159 PITALSGGQRQLVFIAKLLAQQAKVMLFDEP 189
Cdd:PRK11831 140 MPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-194 |
1.96e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.89 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 23 LRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGI--VTPSSGQV----------------ELLGA 84
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 85 PLTKLRAHERATRLAYLPQHTPADTAIDVRTVVALGR----YAHHRRRDRFRSSLNSTDH---DIVAYALDRVGVTALAD 157
Cdd:TIGR03269 81 PCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRtfalYGDDTVLDNVLEALEEIGYegkEAVGRAVDLIEMVQLSH 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 896182242 158 RpIT----ALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:TIGR03269 161 R-IThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
27-196 |
2.16e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.81 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLrAHERATRLAYLPQHT 105
Cdd:PRK10790 345 NVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSVLRQGVAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 PADTAIDVRTVVALGRyahhrrrdrfrsslnSTDHDIVAYALDRVGVTALAdRPITA------------LSGGQRQLVFI 173
Cdd:PRK10790 424 PVVLADTFLANVTLGR---------------DISEEQVWQALETVQLAELA-RSLPDglytplgeqgnnLSVGQKQLLAL 487
|
170 180
....*....|....*....|...
gi 896182242 174 AKLLAQQAKVMLFDEPTAALDIG 196
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSG 510
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-195 |
2.85e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.19 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTK------LRAHERatRLAYLPQhtpadtaiDVR 114
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKR--RIGYVFQ--------DAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 115 TvvalgrYAHHRRRDRFRSSLNSTDHDIVAYALDRVGVTALADR-PITaLSGGQRQLVFIAKLLAQQAKVMLFDEPTAAL 193
Cdd:PRK11144 87 L------FPHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRyPGS-LSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
..
gi 896182242 194 DI 195
Cdd:PRK11144 160 DL 161
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
37-195 |
3.21e-09 |
|
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: 57.61 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 37 VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGapltklraheratRLAYLPQhTPADTAIDVRTV 116
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQ-TSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 117 VALG-RYAHHrrrdRFRSSLNST--DHDIVAYA-LDRvgvTALADRPITaLSGGQRQLVFIAKLLAQQAKVMLFDEPTAA 192
Cdd:TIGR01271 507 IIFGlSYDEY----RYTSVIKACqlEEDIALFPeKDK---TVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
...
gi 896182242 193 LDI 195
Cdd:TIGR01271 579 LDV 581
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
37-195 |
3.45e-09 |
|
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: 56.40 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 37 VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGapltklraheratRLAYLPQHT---PADTAIDV 113
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSwimPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALGRYahhrrrdRFRSSLNST--DHDIVAYAldRVGVTALADRPITaLSGGQRQLVFIAKLLAQQAKVMLFDEPTA 191
Cdd:cd03291 119 IFGVSYDEY-------RYKSVVKACqlEEDITKFP--EKDNTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFG 188
|
....
gi 896182242 192 ALDI 195
Cdd:cd03291 189 YLDV 192
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
41-250 |
3.59e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.28 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQV---ELLGAPLTKLRAHERATRLAYLPQHTPADTAID--VRT 115
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEetVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 116 VVALGRyahhrrrDRFRSSLNSTDhDIVAYALDRVGVTA-LADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK13643 105 DVAFGP-------QNFGIPKEKAE-KIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 195 IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVL 250
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-194 |
5.40e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPS----SGQVELLGAPLTKLRAHERAtRLAYLPQ---HTPA 107
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKKHYRG-DVVYNAEtdvHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 108 DTAIDVRTVVALGRYAHHR----RRDRFRSSLnsTDHDIVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKV 183
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQNRpdgvSREEYAKHI--ADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170
....*....|.
gi 896182242 184 MLFDEPTAALD 194
Cdd:TIGR00956 231 QCWDNATRGLD 241
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
34-194 |
6.62e-09 |
|
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: 55.24 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHtPADTAIDV 113
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE-PVLFDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALGRYahhrrrdrfrsslNSTDHDIVAYALDrvgvtALADRPI---------------TALSGGQRQLVFIAKLLA 178
Cdd:cd03249 94 AENIRYGKP-------------DATDEEVEEAAKK-----ANIHDFImslpdgydtlvgergSQLSGGQKQRIAIARALL 155
|
170
....*....|....*.
gi 896182242 179 QQAKVMLFDEPTAALD 194
Cdd:cd03249 156 RNPKILLLDEATSALD 171
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
32-194 |
8.56e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.62 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 32 YRNRT-VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHER---------------- 94
Cdd:PRK11650 13 YDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRdiamvfqnyalyphms 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 95 -ATRLAYlpqhtpadtAIDVRTVvalGRyAHHRRRdrfrsslnstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFI 173
Cdd:PRK11650 93 vRENMAY---------GLKIRGM---PK-AEIEER--------------VAEAARILELEPLLDRKPRELSGGQRQRVAM 145
|
170 180
....*....|....*....|.
gi 896182242 174 AKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLD 166
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
27-195 |
1.16e-08 |
|
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: 54.53 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQh 104
Cdd:cd03288 24 DLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 TPADTAIDVRTVVALGRYAHHrrrDRFRSSLNSTDHDIVAYALDRvGVTALADRPITALSGGQRQLVFIAKLLAQQAKVM 184
Cdd:cd03288 103 DPILFSGSIRFNLDPECKCTD---DRLWEALEIAQLKNMVKSLPG-GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170
....*....|.
gi 896182242 185 LFDEPTAALDI 195
Cdd:cd03288 179 IMDEATASIDM 189
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
41-253 |
1.41e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.84 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLT------KLRAHERATRLAY-LPQhtpadTAIDV 113
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFqFPE-----AQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVValgryahhrrRDRFRSSLN--STDHDIVAYALD---RVGV-TALADRPITALSGGQRQLVFIAKLLAQQAKVMLFD 187
Cdd:PRK13641 101 NTVL----------KDVEFGPKNfgFSEDEAKEKALKwlkKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 188 EPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-284 |
1.84e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 16 DTDSTALLRATDLSVGYRNRT----VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEllGAPLTKLRA 91
Cdd:PRK10261 6 ELDARDVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ--CDKMLLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 92 HERATRLAYLPQHT-----PADTAI-------DVRTVVALGRyahhRRRDRFRSSLNSTDHDIVAYA---LDRVGV---T 153
Cdd:PRK10261 84 SRQVIELSEQSAAQmrhvrGADMAMifqepmtSLNPVFTVGE----QIAESIRLHQGASREEAMVEAkrmLDQVRIpeaQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 154 ALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELADE-GHGIGVVLHDLNLAARSCHRL 232
Cdd:PRK10261 160 TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 896182242 233 SVIHNGGLEVTGSAEEVLTPPRIDAIYRISSAVdtdPHTGSVRVTALARARP 284
Cdd:PRK10261 240 LVMYQGEAVETGSVEQIFHAPQHPYTRALLAAV---PQLGAMKGLDYPRRFP 288
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-194 |
2.17e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.02 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 13 TKPDTDSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGI--VTPS---SGQVELLGAPLt 87
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 88 klraheratrlaYLPQHTPadtaIDVRTVVALgryaHHRRRDRFRSSLnstdHDIVAYA---------LDRVGVTALADR 158
Cdd:PRK14243 80 ------------YAPDVDP----VEVRRRIGM----VFQKPNPFPKSI----YDNIAYGaringykgdMDELVERSLRQA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 896182242 159 PI------------TALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK14243 136 ALwdevkdklkqsgLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
31-194 |
2.94e-08 |
|
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: 52.65 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 31 GYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIvTPSSGQVE--LLGAPLTKLRAHERATR-LAYLPQHtpa 107
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSVEgdIHYNGIPYKEFAEKYPGeIIYVSEE--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 108 DTAIDVRTVvalgryahhRRRDRFRSSLNstdhdivayaldrvgvtalADRPITALSGGQRQLVFIAKLLAQQAKVMLFD 187
Cdd:cd03233 92 DVHFPTLTV---------RETLDFALRCK-------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWD 143
|
....*..
gi 896182242 188 EPTAALD 194
Cdd:cd03233 144 NSTRGLD 150
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-194 |
3.20e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPS-SGQVELLGApltklraheratrLAYLPQhTPADTAIDVRTV 116
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGS-------------VAYVPQ-VSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 117 VALGRyahHRRRDRFRSSLNST--DHDIVAYA-LDRvgvTALADRPITaLSGGQRQLVFIAKLLAQQAKVMLFDEPTAAL 193
Cdd:PLN03232 699 ILFGS---DFESERYWRAIDVTalQHDLDLLPgRDL---TEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
.
gi 896182242 194 D 194
Cdd:PLN03232 772 D 772
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
41-100 |
3.74e-08 |
|
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: 54.03 E-value: 3.74e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTklraheRATRLAY 100
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT------ADNREAY 404
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-195 |
4.59e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 13 TKPDTDSTALLRATDLSVGYRNRTVV-SGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVellgapltkLRA 91
Cdd:PLN03073 499 TPDDRPGPPIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---------FRS 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 92 HEraTRLAYLPQHTPADTAIDVRTVVALGRYAHHRRRDRFRSSLNStdhdivayaldrVGVTA-LADRPITALSGGQRQL 170
Cdd:PLN03073 570 AK--VRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGS------------FGVTGnLALQPMYTLSGGQKSR 635
|
170 180
....*....|....*....|....*
gi 896182242 171 VFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDL 660
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
37-253 |
4.80e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 53.37 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 37 VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPS----SGQVELLGAPLTKLRAHER----ATRLAYLPQH---- 104
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERrkiiGREIAMIFQEpssc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 -TPADT-------AIDVRTvvaLGRYAHHRRRDRfrsslnstdHDIVAYALDRVGVTalADRPITA-----LSGGQRQLV 171
Cdd:COG4170 102 lDPSAKigdqlieAIPSWT---FKGKWWQRFKWR---------KKRAIELLHRVGIK--DHKDIMNsypheLTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 172 FIAKLLAQQAKVMLFDEPTAALDIGFQLEILELLGELaDEGHGIGVVL--HDLNLAARSCHRLSVIHNGGLEVTGSAEEV 249
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARL-NQLQGTSILLisHDLESISQWADTITVLYCGQTVESGPTEQI 246
|
....
gi 896182242 250 LTPP 253
Cdd:COG4170 247 LKSP 250
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
38-194 |
6.80e-08 |
|
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: 53.80 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGApltklraheratrLAYLPQHT--PADTaidVRT 115
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAwiQNDS---LRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 116 VVALGryaHHRRRDRFRSSLNS----TDHDIVAYAlDRvgvTALADRPITaLSGGQRQLVFIAKLLAQQAKVMLFDEPTA 191
Cdd:TIGR00957 718 NILFG---KALNEKYYQQVLEAcallPDLEILPSG-DR---TEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
...
gi 896182242 192 ALD 194
Cdd:TIGR00957 790 AVD 792
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-97 |
1.22e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 14 KPDTDSTALLRATDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTklrAHE 93
Cdd:NF033858 258 PADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGD 334
|
....
gi 896182242 94 RATR 97
Cdd:NF033858 335 IATR 338
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-245 |
1.49e-07 |
|
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: 52.71 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPL-TKLRAHERAtrLAYLPQHTPADTAIDV 113
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQS--LGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALgrYAHHRRRDRFRSSLNstdhdiVAYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAAL 193
Cdd:TIGR01257 1021 AEHILF--YAQLKGRSWEEAQLE------MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 896182242 194 DiGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGS 245
Cdd:TIGR01257 1093 D-PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-251 |
1.81e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.55 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNRT-----VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVEL----LGAPLTKLRAHERATR 97
Cdd:PRK13645 11 NVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaIPANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 98 ---LAY-LPQHTPADTAIDvrTVVALGRYahHRRRDRFRSslnstdHDIVAYALDRVGVTA-LADRPITALSGGQRQLVF 172
Cdd:PRK13645 91 eigLVFqFPEYQLFQETIE--KDIAFGPV--NLGENKQEA------YKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 173 IAKLLAQQAKVMLFDEPTAALD-IGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLT 251
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDpKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
43-195 |
2.98e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 43 LAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELlgapltklrahERATRLAYLPQHTPADTAIDVRTVVALG-- 120
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-----------EQDLIVARLQQDPPRNVEGTVYDFVAEGie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 121 -------RY---AHHRRRDRFRSSLNST-------DH-------DIVAYALDRVGVTAlaDRPITALSGGQRQLVFIAKL 176
Cdd:PRK11147 93 eqaeylkRYhdiSHLVETDPSEKNLNELaklqeqlDHhnlwqleNRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRA 170
|
170
....*....|....*....
gi 896182242 177 LAQQAKVMLFDEPTAALDI 195
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDI 189
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
26-251 |
4.24e-07 |
|
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: 50.24 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 26 TDLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTpSSGQVELLGAPLTKLRAHERATRLAYLPQ 103
Cdd:cd03289 6 KDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 104 htpadtaidvRTVVALGRyahhrrrdrFRSSLNS----TDHDIVAYAlDRVGVTALADR-PIT----------ALSGGQR 168
Cdd:cd03289 85 ----------KVFIFSGT---------FRKNLDPygkwSDEEIWKVA-EEVGLKSVIEQfPGQldfvlvdggcVLSHGHK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 169 QLVFIAKLLAQQAKVMLFDEPTAALD-IGFQLEILELLGELADeghgIGVVLHDLNLAAR-SCHRLSVIHNGGLEVTGSA 246
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDpITYQVIRKTLKQAFAD----CTVILSEHRIEAMlECQRFLVIEENKVRQYDSI 220
|
....*
gi 896182242 247 EEVLT 251
Cdd:cd03289 221 QKLLN 225
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
45-195 |
5.43e-07 |
|
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: 48.72 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 45 IRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGapltklraheraTRLAYLPQHtpadtaidvrtvvalgryah 124
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG------------ITPVYKPQY-------------------- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 125 hrrrdrfrsslnstdhdivayaldrvgvtaladrpiTALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:cd03222 70 ------------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-194 |
9.40e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLraheratrlaylpqHTPADTAIDV 113
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI--------------AKPYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALGRYAHHRRrdRFRSSLNSTDHDIVAyALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAAL 193
Cdd:PRK13541 78 NLGLKLEMTVFENL--KFWSEIYNSAETLYA-AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
.
gi 896182242 194 D 194
Cdd:PRK13541 155 S 155
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-198 |
1.11e-06 |
|
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: 49.91 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRN--RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTpSSGQVELLGAPLTKLRAHERATRLAYLPQh 104
Cdd:TIGR01271 1222 GLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQ- 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 105 tpadtaidvRTVVALGRyahhrrrdrFRSSLNS----TDHDIVAYAlDRVGVTALADR-PIT----------ALSGGQRQ 169
Cdd:TIGR01271 1300 ---------KVFIFSGT---------FRKNLDPyeqwSDEEIWKVA-EEVGLKSVIEQfPDKldfvlvdggyVLSNGHKQ 1360
|
170 180 190
....*....|....*....|....*....|
gi 896182242 170 LVFIAKLLAQQAKVMLFDEPTAALD-IGFQ 198
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
38-87 |
1.50e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.20 E-value: 1.50e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLT 87
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
52-195 |
2.99e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 52 GIIGSNGTGKSSLLRAMAGIVTPSSGQVELlgapltklrahERATRLAYLPQHTPADTAIDVRTVVALGR---YAHHRRR 128
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSL-----------DPNERLGKLRQDQFAFEEFTVLDTVIMGHtelWEVKQER 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 129 DRFRSSLNSTDHDI-------VAYA-LDrvGVTALAdR-----------------PITALSGGQRQLVFIAKLLAQQAKV 183
Cdd:PRK15064 100 DRIYALPEMSEEDGmkvadleVKFAeMD--GYTAEA-RagelllgvgipeeqhygLMSEVAPGWKLRVLLAQALFSNPDI 176
|
170
....*....|..
gi 896182242 184 MLFDEPTAALDI 195
Cdd:PRK15064 177 LLLDEPTNNLDI 188
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
34-238 |
3.89e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHE-------------RATRL-A 99
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalvteerRSTGIyA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 100 YLPqhtpadtaIDVRTVVA-LGRYahhrrRDRFRSSLNSTDHDIVAYALDRVGV-TALADRPITALSGGQRQLVFIAKLL 177
Cdd:PRK10982 340 YLD--------IGFNSLISnIRNY-----KNKVGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 178 AQQAKVMLFDEPTAALDIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNG 238
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
41-195 |
4.86e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 47.71 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 41 VNLAIRPGEVQGIIGSNGTGKSSllraMAGIVTP----SSGQVELLGA-----PLTKLRAHeratrLAYLPQ--HTPADT 109
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGHdlrdyTLASLRNQ-----VALVSQnvHLFNDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 110 aidVRTVVAlgrYAhhrRRDRFrsslnsTDHDI-----VAYALDRV-----GVTALADRPITALSGGQRQLVFIAKLLAQ 179
Cdd:PRK11176 433 ---IANNIA---YA---RTEQY------SREQIeeaarMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170
....*....|....*.
gi 896182242 180 QAKVMLFDEPTAALDI 195
Cdd:PRK11176 498 DSPILILDEATSALDT 513
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
27-194 |
8.54e-06 |
|
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: 46.74 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYR-NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTK-----LRAHeratrLAY 100
Cdd:COG5265 362 NVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvtqasLRAA-----IGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 101 LPQhtpaDTAI---DVRTVVALGRyahhrrrdrfrssLNSTDHDIVAYA----LD------------RVGVTALAdrpit 161
Cdd:COG5265 437 VPQ----DTVLfndTIAYNIAYGR-------------PDASEEEVEAAAraaqIHdfieslpdgydtRVGERGLK----- 494
|
170 180 190
....*....|....*....|....*....|...
gi 896182242 162 aLSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:COG5265 495 -LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-194 |
1.11e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 11 HVTKPDTDSTALLRatDLSVGYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLramaGIVT---PS--SGQVELLG-- 83
Cdd:PRK10938 251 RHALPANEPRIVLN--NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL----SLITgdhPQgySNDLTLFGrr 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 84 ----APLTKLRAHeratrLAYLPQ--HTPADTAIDVRTVV------ALGRYAHHRRRDRFrsslnstdhdIVAYALDRVG 151
Cdd:PRK10938 325 rgsgETIWDIKKH-----IGYVSSslHLDYRVSTSVRNVIlsgffdSIGIYQAVSDRQQK----------LAQQWLDILG 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896182242 152 VTA-LADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK10938 390 IDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
42-195 |
1.69e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 42 NLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQ--------VELLGAPLTKLRAHERATRLAYLPQHTPADTAIDV 113
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 114 RTVVALgryaHHRRRDRFRsslnstdhdivAYAlDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAAL 193
Cdd:PRK10938 103 AEIIQD----EVKDPARCE-----------QLA-QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
..
gi 896182242 194 DI 195
Cdd:PRK10938 167 DV 168
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-194 |
3.26e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 35 RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMA-----GIVTpsSGQVELLGAPLTKlrAHERatRLAYLPQHtpaDT 109
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervttGVIT--GGDRLVNGRPLDS--SFQR--SIGYVQQQ---DL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 110 AIDVRTVVALGRYAHHRRRDrfRSSLNSTDHDIVAYALDRVGVTALADR----PITALSGGQRQLVFIAKLLAQQAKVML 185
Cdd:TIGR00956 847 HLPTSTVRESLRFSAYLRQP--KSVSKSEKMEYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLL 924
|
170
....*....|
gi 896182242 186 F-DEPTAALD 194
Cdd:TIGR00956 925 FlDEPTSGLD 934
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
38-84 |
3.48e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 3.48e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGA 84
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS 86
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
38-240 |
4.07e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.39 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTklraheratrlaylpqHTPADTAI-DVRTV 116
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT----------------HKTKDKYIrPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 117 ValGRYAHHRRRDRFRSSL-----------NSTDHDIVAYALD---RVGVT--ALADRPITaLSGGQRQLVFIAKLLAQQ 180
Cdd:PRK13646 87 I--GMVFQFPESQLFEDTVereiifgpknfKMNLDEVKNYAHRllmDLGFSrdVMSQSPFQ-MSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896182242 181 AKVMLFDEPTAALDI-GFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGL 240
Cdd:PRK13646 164 PDIIVLDEPTAGLDPqSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
38-251 |
4.43e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 38 VSGVNLAIRPGEVQGIIGSNGtgkSSLLRAM--AGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHTPADTAIDVR- 114
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*G---AA**RGAlpAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRESFSGRe 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 115 TVVALGRYAHHRRRD-RFRSSlnstdhdivaYALDRVGVTALADRPITALSGGQRQLVFIAKLLAQQAKVMLFDEPTAAL 193
Cdd:NF000106 106 NLYMIGR*LDLSRKDaRARAD----------ELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 896182242 194 DIGFQLEILELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLT 251
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-196 |
6.85e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 22 LLRATDLSV---GYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLlrAMA--------GIvtpsSGQVELLGAPLTkLR 90
Cdd:NF040905 257 VFEVKNWTVyhpLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL--AMSvfgrsygrNI----SGTVFKDGKEVD-VS 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 91 AHERATR--LAY-----------LPQhtpadtaiDVR---TVVALGRYAHH---------RRRDRFRSSLNSTDHDIvay 145
Cdd:NF040905 330 TVSDAIDagLAYvtedrkgyglnLID--------DIKrniTLANLGKVSRRgvideneeiKVAEEYRKKMNIKTPSV--- 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 896182242 146 aLDRVGvtaladrpitALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDIG 196
Cdd:NF040905 399 -FQKVG----------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVG 438
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-194 |
8.27e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.80 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRN-RTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTK-----LRaHERATRL-- 98
Cdd:PRK13657 339 DVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvtrasLR-RNIAVVFqd 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 99 AYLPQHTPAD-------TAIDVRTVVALGRYAHhrrrdrfrsslnstdHDIVAYALDRVGvTALADRPiTALSGGQRQLV 171
Cdd:PRK13657 418 AGLFNRSIEDnirvgrpDATDEEMRAAAERAQA---------------HDFIERKPDGYD-TVVGERG-RQLSGGERQRL 480
|
170 180
....*....|....*....|...
gi 896182242 172 FIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALD 503
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-195 |
1.33e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 27 DLSVGYRNRTVVSGVNLAIrpGEVQGIIGSNGTGKSSLLRAMA-----GIvtPSSGQV-----ELLGAPLTKLRAH---- 92
Cdd:PLN03073 184 SISVGGRDLIVDASVTLAF--GRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQIlhveqEVVGDDTTALQCVlntd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 93 -ERATRLAYLPQHTPADTAIDVRTVVALGRYAHH---------RRRDRFRSSLNSTDhdivAYALDRVGVTALADRPITA 162
Cdd:PLN03073 260 iERTQLLEEEAQLVAQQRELEFETETGKGKGANKdgvdkdavsQRLEEIYKRLELID----AYTAEARAASILAGLSFTP 335
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 896182242 163 ---------LSGGQRQLVFIAKLLAQQAKVMLFDEPTAALDI 195
Cdd:PLN03073 336 emqvkatktFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
37-253 |
1.87e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 37 VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTP----SSGQVELLGAPLTKLRAHERATRLAY-------LPQHT 105
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGHnvsmifqEPQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 106 --PADTaIDVRTVVALGRYAHHRR-RDRFRSSLNSTDHdivayALDRVGVT----ALADRPITaLSGGQRQLVFIAKLLA 178
Cdd:PRK15093 102 ldPSER-VGRQLMQNIPGWTYKGRwWQRFGWRKRRAIE-----LLHRVGIKdhkdAMRSFPYE-LTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896182242 179 QQAKVMLFDEPTAALDIGFQLEI-LELLGELADEGHGIGVVLHDLNLAARSCHRLSVIHNGGLEVTGSAEEVLTPP 253
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIfRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-194 |
1.88e-04 |
|
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: 41.46 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 34 NRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPS--SGQVELLGAPLTKlrAHERATrlAYLPQhtpADTAI 111
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK--NFQRST--GYVEQ---QDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 112 DVRTVvalgryahhrrRDRFRSSlnstdhdivayALDRvgvtaladrpitALSGGQRQLVFIAKLLAQQAKVMLFDEPTA 191
Cdd:cd03232 92 PNLTV-----------REALRFS-----------ALLR------------GLSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
...
gi 896182242 192 ALD 194
Cdd:cd03232 138 GLD 140
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
47-126 |
4.92e-04 |
|
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: 39.66 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 47 PGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQHTPADTAIDVRTVVALGRYAHHR 126
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
162-194 |
5.07e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 5.07e-04
10 20 30
....*....|....*....|....*....|...
gi 896182242 162 ALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
31-83 |
6.84e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 6.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 31 GYRNRT--VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLG 83
Cdd:PRK13546 31 KHKNKTffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
31-82 |
1.26e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 39.64 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 896182242 31 GYRNRTVVSGVNLAIRPGEVQGIIGSNGTGKSSLLRA---MAGIVTPSSGQVELL 82
Cdd:COG1106 12 SFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEAlyfLRNLVLNSSQPGDKL 66
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
37-194 |
1.97e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 37 VVSGVNLAIRPGEVQGIIGSNGTGKSSLLRAMAGIVTPSSGQVELLGAPLTKLRAHERATRLAYLPQhTPADTAIDVRTV 116
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQ-DPVLFDGTVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 117 ValgryahhrrrDRFrssLNSTDHDIVAyALDRVGV---TALADRPITA--------LSGGQRQLVFIAK-LLAQQAKVM 184
Cdd:PTZ00243 1404 V-----------DPF---LEASSAEVWA-ALELVGLrerVASESEGIDSrvleggsnYSVGQRQLMCMARaLLKKGSGFI 1468
|
170
....*....|
gi 896182242 185 LFDEPTAALD 194
Cdd:PTZ00243 1469 LMDEATANID 1478
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
140-194 |
2.39e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 2.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 896182242 140 HDIVAYALDR----VGVTAladrpiTALSGGQRQLVFIAKLLAQQAKVMLFDEPTAALD 194
Cdd:PTZ00265 559 HDFVSALPDKyetlVGSNA------SKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
47-194 |
2.39e-03 |
|
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: 37.72 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 47 PGEVQGIIGSNGTGKSSLLRAMAgivtpssgqvellgapltklraheratrlaylpqhtpadtaidvrtVVALGRYAHHR 126
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG----------------------------------------------LALGGAQSATR 53
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896182242 127 RRDRFRSSLNSTDHDIVAYALdrvgvtaladrpITALSGGQRQLVFIAKLLAQQAK----VMLFDEPTAALD 194
Cdd:cd03227 54 RRSGVKAGCIVAAVSAELIFT------------RLQLSGGEKELSALALILALASLkprpLYILDEIDRGLD 113
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
152-194 |
2.42e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 2.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 896182242 152 VTALAD------RPITALSGGQRQLVFIAKLLAQQ----AKVMLFDEPTAALD 194
Cdd:cd03272 142 INSLTNmkqdeqQEMQQLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDAALD 194
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
53-194 |
3.34e-03 |
|
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: 37.97 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182242 53 IIGSNGTGKSSLLRAMAGIVTPSsgqvellGAPLTKLRAHER-----ATRLAYlpqhtpadtaIDVRTVVALGR-YAHHR 126
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALTGE-------LPPNSKGGAHDPklireGEVRAQ----------VKLAFENANGKkYTITR 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896182242 127 RRDRFRSSLNSTDHDIvayaldrvgvTALADRPITALSGGQRQLVFI------AKLLAQQAKVMLFDEPTAALD 194
Cdd:cd03240 90 SLAILENVIFCHQGES----------NWPLLDMRGRCSGGEKVLASLiirlalAETFGSNCGILALDEPTTNLD 153
|
|
| |
