|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-228 |
7.57e-160 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 441.14 E-value: 7.57e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 1 MPAENILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEE 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 ARAALRAQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARA 160
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 161 FNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLREEA 228
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEEA 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-228 |
3.70e-131 |
|
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: 368.69 E-value: 3.70e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 2 PAENILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEA 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 82 RAALRAQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQgdARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAF 161
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARAR--ARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 162 NGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLREEA 228
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDT 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-227 |
6.45e-115 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 327.39 E-value: 6.45e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARA 83
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 ALRAQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNG 163
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496080956 164 RPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-224 |
9.64e-104 |
|
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: 298.63 E-value: 9.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALR 86
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-226 |
5.75e-81 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 241.10 E-value: 5.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RAQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLRE 226
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-226 |
2.06e-71 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 216.84 E-value: 2.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RaQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAARCDRR-LRLVDGQLRE 226
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRvLELEDGRLVR 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-227 |
1.39e-66 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 205.05 E-value: 1.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RAQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-206 |
2.36e-64 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 200.32 E-value: 2.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 2 PAENILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEa 81
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 82 raalraqhVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAF 161
Cdd:COG1116 82 --------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496080956 162 NGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-223 |
1.55e-61 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 191.69 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVA---ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RaQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTHDP-LLAARCDRRLRLVDGQ 223
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLsLVDRVAHRVIILDDGR 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-206 |
3.23e-61 |
|
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: 191.15 E-value: 3.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRmdeearaalR 86
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-224 |
7.47e-60 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 198.79 E-value: 7.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RAQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAF-NGR 164
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALmNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 165 PALLfADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:PRK10535 164 QVIL-ADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
6-225 |
4.35e-59 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 185.61 E-value: 4.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RaQHVGFVFQSFMLIPTLNALENVELPA-LLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGR 164
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 165 PALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLR 225
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-228 |
3.85e-57 |
|
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: 180.78 E-value: 3.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAaL 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RAQHVGFVFQSFM--LIPTLNALENVELPALLRGASDSESQGDARALLEQLGLG---KRLHHLPAQLSGGEQQRVALARA 160
Cdd:cd03257 80 RRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 161 FNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLREEA 228
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-224 |
7.88e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 180.64 E-value: 7.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RAQhVGFVFQSFMLIPTLNALENV---------ELPALLRGASDSESQGdARALLEQLGLGKRLHHLPAQLSGGEQQRVA 156
Cdd:COG3638 79 RRR-IGMIFQQFNLVPRLSVLTNVlagrlgrtsTWRSLLGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 157 LARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
25-219 |
3.66e-55 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 175.11 E-value: 3.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRAQHVGFVFQSFMLIPTLN 104
Cdd:TIGR03608 13 ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENET 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDK 184
Cdd:TIGR03608 93 VEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDE 172
|
170 180 190
....*....|....*....|....*....|....*
gi 496080956 185 IADLLFSLNREhGTTLILVTHDPLLAARCDRRLRL 219
Cdd:TIGR03608 173 VLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-228 |
5.40e-55 |
|
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: 176.15 E-value: 5.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMdeeARAALR 86
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR---RRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQhVGFVFQSFMLipTLNALENVE----LPALLRGASDSESQgdARALLEQLGLGKR-LHHLPAQLSGGEQQRVALARAF 161
Cdd:COG1124 79 RR-VQMVFQDPYA--SLHPRHTVDrilaEPLRIHGLPDREER--IAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 162 NGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLREEA 228
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-227 |
4.34e-54 |
|
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: 173.24 E-value: 4.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 2 PAENILEVHHLKKSvgQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEA 81
Cdd:COG1127 1 MSEPMIEVRNLTKS--FGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 82 RAALRaQHVGFVFQSFMLIPTLNALENVELPaLLRGASDSESQGDARAL--LEQLGLGKRLHHLPAQLSGGEQQRVALAR 159
Cdd:COG1127 77 LYELR-RRIGMLFQGGALFDSLTVFENVAFP-LREHTDLSEAEIRELVLekLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 160 AFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PLLAARCDRRLRLVDGQLREE 227
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIAE 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-206 |
6.05e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 172.87 E-value: 6.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHrMDEEARAAL 85
Cdd:COG1126 1 MIEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RaQHVGFVFQSFMLIPTLNALENVEL-PALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGR 164
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496080956 165 PALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD 206
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHE 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-224 |
1.15e-51 |
|
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: 166.54 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03259 73 --NIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-207 |
3.22e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 169.51 E-value: 3.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAR 82
Cdd:COG3842 2 AMPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 aalraqHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFN 162
Cdd:COG3842 78 ------NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496080956 163 GRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDP 207
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQ 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-228 |
3.75e-51 |
|
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: 173.17 E-value: 3.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKS-VGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEA 81
Cdd:COG1123 257 AEPLLEVRNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 82 RAALRaQHVGFVFQ--SFMLIPTLNALENVELPALLRG-ASDSESQGDARALLEQLGLGKR-LHHLPAQLSGGEQQRVAL 157
Cdd:COG1123 337 LRELR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 158 ARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLREEA 228
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-223 |
7.09e-51 |
|
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: 165.43 E-value: 7.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALR 86
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENV---------ELPALLRGASDSESQgDARALLEQLGLGKRLHHLPAQLSGGEQQRVAL 157
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVlsgrlgrrsTWRSLFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 158 ARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQ 223
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGR 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-227 |
1.02e-50 |
|
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: 164.68 E-value: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RaQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PLLAARCDRRLRLVDGQLREE 227
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEVVEE 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-227 |
2.24e-50 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 163.83 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGqgEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALR 86
Cdd:cd03261 1 IELRGLTKSFG--GRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENVELPALLRGA-SDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDpLLAAR--CDRRLRLVDGQLREE 227
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHD-LDTAFaiADRIAVLYDGKIVAE 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-206 |
7.11e-50 |
|
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: 161.93 E-value: 7.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRmDEEARAALR 86
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENVEL-PALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD 206
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHE 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-224 |
2.94e-49 |
|
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: 160.27 E-value: 2.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRaQHVGFVFQSFMLIPTLNA 105
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 LENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKI 185
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 186 ADLLFSLNREhGTTLILVTHDPLLAARCDRR-LRLVDGQL 224
Cdd:cd03292 176 MNLLKKINKA-GTTVVVATHAKELVDTTRHRvIALERGKL 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-224 |
4.66e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 159.60 E-value: 4.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraaLR 86
Cdd:COG4619 1 LELEGLSFRVGGKP----ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQhVGFVFQ-SFMLIPTLnaLENVELPALLRGASDSESqgDARALLEQLGLGKR-LHHLPAQLSGGEQQRVALARAFNGR 164
Cdd:COG4619 74 RQ-VAYVPQePALWGGTV--RDNLPFPFQLRERKFDRE--RALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 165 PALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-227 |
2.62e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.30 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAAR-CDRRLRLVDGQLREE 227
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERlCDRVAIIDKGRIVAD 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-223 |
7.07e-48 |
|
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: 156.47 E-value: 7.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 8 EVHHLKKSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHrmdeEARAALRA 87
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT----KLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 88 QHVGFVFQSF--MLIpTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:cd03225 75 RKVGLVFQNPddQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDP-LLAARCDRRLRLVDGQ 223
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
2.44e-47 |
|
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: 163.15 E-value: 2.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS---SGEVSMLGKPLHRMDEe 80
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 araALRAQHVGFVFQSFM--LIPtLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALA 158
Cdd:COG1123 79 ---ALRGRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 159 RAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLREEA 228
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDG 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-206 |
7.14e-47 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 157.93 E-value: 7.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RaQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE 200
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-215 |
3.70e-46 |
|
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: 155.60 E-value: 3.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDD---GSSGEVSMLGKPLHRMDEEAR 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AALRAQHVGFVFQSFM--LIPTLNALENVELPALL-RGASDSESQGDARALLEQLGL---GKRLHHLPAQLSGGEQQRVA 156
Cdd:COG0444 81 RKIRGREIQMIFQDPMtsLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 157 LARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PLLAARCDR 215
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlGVVAEIADR 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-223 |
4.57e-46 |
|
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: 150.80 E-value: 4.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalR 86
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQHVGFVFQSFMLIPTLNALENVELPallrgasdsesqgdaralleqlglgkrlhhlpaqLSGGEQQRVALARAFNGRPA 166
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQ 223
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-222 |
1.61e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 151.40 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkpLHRMDEEARAAL 85
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RAQHVGFVFQSFMLIPTLNALENVEL-PALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGR 164
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 165 PALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAARCDRRLRLVDG 222
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-207 |
4.52e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 153.30 E-value: 4.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHqlsiLTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:COG3839 4 LELENVSKSYGGVEA----LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:COG3839 76 --NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDP 207
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ 194
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-215 |
8.63e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 152.61 E-value: 8.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSmlgkpLHrmDEEARAALR 86
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIV-----LN--GRDLFTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQ--HVGFVFQSFMLIPTLNALENVE--LPAllRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFN 162
Cdd:COG1118 72 PRerRVGFVFQHYALFPHMTVAENIAfgLRV--RPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496080956 163 GRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDR 215
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADR 203
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
25-224 |
2.89e-44 |
|
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: 147.86 E-value: 2.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmDEEARAALRaQHVGFVFQS-----FMl 99
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELR-RKVGLVFQNpddqlFA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 100 iPTLnaLENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDR 179
Cdd:COG1122 91 -PTV--EEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496080956 180 QTGDKIADLLFSLNREhGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:COG1122 168 RGRRELLELLKRLNKE-GKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-224 |
1.40e-43 |
|
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: 146.67 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RaQHVGFVFQSFMLIPTLNALENVELPAL--------LRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVAL 157
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGRLgykptwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 158 ARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEI 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-224 |
1.63e-43 |
|
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: 147.40 E-value: 1.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 29 VELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRAQHVGFVFQSFMLIPTLNALEN 108
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 109 VELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADL 188
Cdd:cd03294 123 VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190
....*....|....*....|....*....|....*..
gi 496080956 189 LFSLNREHGTTLILVTHDPLLAARC-DRRLRLVDGQL 224
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRL 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-224 |
4.16e-43 |
|
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: 145.57 E-value: 4.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLkkSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMdeeaRAAL 85
Cdd:COG1120 1 MLEAENL--SVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL----SRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RAQHVGFVFQSFMLIPTLNALENVEL---PAllRGASDSESQGD---ARALLEQLGLGKRLHHLPAQLSGGEQQRVALAR 159
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRELVALgryPH--LGLFGRPSAEDreaVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 160 AFNGRPALLFADEPTGNLD--RQTgdKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDlaHQL--EVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRI 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
1.51e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.38 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 1 MPAENILEVHHLkkSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRmdee 80
Cdd:COG1121 1 MMMMPAIELENL--TVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 araalRAQHVGFVFQSFMLIPT--LNALENVELPA-----LLRGASDSESQgDARALLEQLGLGKRLHHLPAQLSGGEQQ 153
Cdd:COG1121 73 -----ARRRIGYVPQRAEVDWDfpITVRDVVLMGRygrrgLFRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496080956 154 RVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDP-LLAARCDRRLRLVDGQLRE 226
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLgAVREYFDRVLLLNRGLVAH 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-228 |
1.63e-41 |
|
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: 140.78 E-value: 1.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDG-----SSGEVSMLGKPLHRMDEEa 81
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 82 RAALRAQhVGFVFQSFMLIPtLNALENVELPALLRG-ASDSESQGDARALLEQLGL----GKRLHhlPAQLSGGEQQRVA 156
Cdd:cd03260 76 VLELRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALwdevKDRLH--ALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 157 LARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDPLLAARC-DRRLRLVDGQLREEA 228
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFG 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-219 |
3.66e-41 |
|
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: 139.15 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:COG4133 3 LEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESqgDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:COG4133 75 -RRLAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLfSLNREHGTTLILVTHDPLLAARCdRRLRL 219
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELI-AAHLARGGAVLLTTHQPLELAAA-RVLDL 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
5.39e-41 |
|
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: 146.83 E-value: 5.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 2 PAENILEVHHLkkSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEa 81
Cdd:COG4987 329 PGGPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 82 raALRaQHVGFVFQSFMLIP-TLnaLENvelpalLRGASDSESQGDARALLEQLGLGKRLHHLP-----------AQLSG 149
Cdd:COG4987 406 --DLR-RRIAVVPQRPHLFDtTL--REN------LRLARPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSG 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 150 GEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPLLAARCDRRLRLVDGQLRE 226
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-227 |
8.36e-41 |
|
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: 139.61 E-value: 8.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:COG4555 2 IEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:COG4555 74 -RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDP-LLAARCDRRLRLVDGQLREE 227
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMqEVEALCDRVVILHKGKVVAQ 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-206 |
8.63e-41 |
|
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: 139.29 E-value: 8.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGehqlSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03300 73 --PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHD 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-223 |
2.84e-40 |
|
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: 137.57 E-value: 2.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSV---GQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAG---LDDGS------SGEVSMLGKP 73
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylPDSGSilvrhdGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 74 LHRMdeearAALRAQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHL-PAQLSGGEQ 152
Cdd:COG4778 84 PREI-----LALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 153 QRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDP-LLAARCDRRLRLVDGQ 223
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEeVREAVADRVVDVTPFS 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-228 |
3.14e-40 |
|
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: 144.44 E-value: 3.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 1 MPAENILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKS-TLLAILAGLDDGS---SGEVSMLGKPLHR 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 77 MDEEARAALRAQHVGFVFQSFMlipT-LNALENV-----ELPALLRGASDSESQGDARALLEQLGL---GKRLHHLPAQL 147
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPM---TsLNPLHTIgkqiaEVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 148 SGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLRE 226
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
..
gi 496080956 227 EA 228
Cdd:COG4172 238 QG 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-224 |
3.44e-40 |
|
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: 135.60 E-value: 3.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENVElpallrgasdsesqgdaralleqlglgkrlhhlpaqLSGGEQQRVALARAFNGRPA 166
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-174 |
8.00e-40 |
|
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: 133.93 E-value: 8.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraalRAQHVGFVFQSFMLIPTLNA 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS----LRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 106 LENVELPALLRGASDSESQGDARALLEQLGLG----KRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-206 |
9.41e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 134.54 E-value: 9.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPL---HRMDEEARA 83
Cdd:COG4598 9 LEVRDLHKSFGDLE----VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkPDRDGELVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 ALRAQ------HVGFVFQSFMLIPTLNALENV-ELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVA 156
Cdd:COG4598 85 ADRRQlqrirtRLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 157 LARAFNGRP-ALLFaDEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD 206
Cdd:COG4598 165 IARALAMEPeVMLF-DEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHE 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-215 |
3.08e-38 |
|
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: 133.24 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGqGehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAR 82
Cdd:COG0411 1 SDPLLEVRGLTKRFG-G---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AALraqhvGFV--FQSFMLIPTLNALENVELPALLRG---------------ASDSESQGDARALLEQLGLGKRLHHLPA 145
Cdd:COG0411 77 ARL-----GIArtFQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 146 QLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PLLAARCDR 215
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADR 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
25-223 |
3.24e-38 |
|
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: 130.58 E-value: 3.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeaRAALRaQHVGFVFQSFMLIP-TL 103
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR-KNIAYVPQDPFLFSgTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 naLENVelpallrgasdsesqgdaralleqlglgkrlhhlpaqLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGD 183
Cdd:cd03228 93 --RENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 184 KIADLLFSLnrEHGTTLILVTHDPLLAARCDRRLRLVDGQ 223
Cdd:cd03228 134 LILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
7-206 |
3.30e-38 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 135.55 E-value: 3.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:TIGR03265 5 LSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:TIGR03265 77 --DYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHD 194
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-227 |
4.30e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 134.93 E-value: 4.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 8 EVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRa 87
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 88 QHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPAL 167
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 168 LFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLREE 227
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQ 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-224 |
1.84e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 130.38 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRAQhVGFVFQSFMLIPTLNA 105
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 LENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKI 185
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 186 ADLLFSLNREhGTTLILVTHD-PLLAARCDRRLRLVDGQL 224
Cdd:PRK10908 177 LRLFEEFNRV-GVTVLMATHDiGLISRRSYRMLTLSDGHL 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-226 |
2.08e-37 |
|
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: 129.68 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03301 73 --DIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLA-ARCDRRLRLVDGQLRE 226
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQIQQ 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
25-227 |
3.45e-37 |
|
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: 137.27 E-value: 3.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeaRAALRaQHVGFVFQSFMLIP-TL 103
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR-RQIGVVLQDVFLFSgTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 naLENvelpalLRGASDSESQGDARALLEQLGLGKRLHHLP-----------AQLSGGEQQRVALARAFNGRPALLFADE 172
Cdd:COG2274 566 --REN------ITLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 173 PTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-206 |
3.64e-37 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 129.76 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsiLTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03299 72 --DISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
14-224 |
3.79e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 130.57 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 14 KSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalraqhvgFV 93
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---------LM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 94 FQSFMLIPTLNALENVELPalLRGasdsESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEP 173
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLG--LKG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496080956 174 TGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLA-ARCDRRLRLVDGQL 224
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-206 |
3.90e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 130.37 E-value: 3.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmdeEARAALR 86
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqhvGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
26-205 |
6.14e-37 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 132.12 E-value: 6.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraqhVGFVFQSFMLIPTLNA 105
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG------IAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 LENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKI 185
Cdd:NF040840 90 FENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180
....*....|....*....|
gi 496080956 186 ADLLFSLNREHGTTLILVTH 205
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTH 189
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-206 |
6.26e-37 |
|
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: 129.12 E-value: 6.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraqhvgfVFQSFMLIPTLNA 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 LENVELP--ALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGD 183
Cdd:TIGR01184 72 RENIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|...
gi 496080956 184 KIADLLFSLNREHGTTLILVTHD 206
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHD 174
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-224 |
9.13e-37 |
|
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: 127.17 E-value: 9.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 8 EVHHLkkSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeearAALRA 87
Cdd:cd03214 1 EVENL--SVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----PKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 88 QHVGFVFQSfmliptlnalenvelpallrgasdsesqgdaralLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPAL 167
Cdd:cd03214 73 RKIAYVPQA----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 168 LFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-224 |
2.01e-36 |
|
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: 126.99 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 18 QGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRAQHVGFvfQSF 97
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDY--QLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 98 MliptlnalENVELpALLRGASD-SESQGDARALLEQLGL-GKRLHHlPAQLSGGEQQRVALARAF-NGRPALLFaDEPT 174
Cdd:cd03226 86 T--------DSVRE-ELLLGLKElDAGNEQAETVLKDLDLyALKERH-PLSLSGGQKQRLAIAAALlSGKDLLIF-DEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-225 |
2.96e-36 |
|
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: 127.03 E-value: 2.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 35 PRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrMDEEARAALRAQ--HVGFVFQSFMLIPTLNALENVELP 112
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL--FDSRKKINLPPQqrKIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 113 alLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSL 192
Cdd:cd03297 100 --LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....
gi 496080956 193 NREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLR 225
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQ 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-206 |
5.44e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.17 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVgqgeHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSM------LGKPLHRMDEE 80
Cdd:PRK11264 4 IEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 ARAaLRaQHVGFVFQSFMLIPTLNALENV-ELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALAR 159
Cdd:PRK11264 80 IRQ-LR-QHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496080956 160 AFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHgTTLILVTHD 206
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHE 203
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-206 |
6.68e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 126.67 E-value: 6.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQgeHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPL---HRMDEEARA 83
Cdd:COG4161 3 IQLKNINCFYGS--HQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 ALRaQHVGFVFQSFMLIPTLNALEN-VELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFN 162
Cdd:COG4161 79 LLR-QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496080956 163 GRPALLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHD 206
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHE 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-225 |
1.70e-35 |
|
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: 124.92 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPLLAAR-CDRRLRLVDGQLR 225
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
25-228 |
1.73e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 131.80 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraalRAQHVGFVFQSFMLIP-TL 103
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS----WRRQIAWVPQNPYLFAgTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 naLENVELPAllRGASDSEsqgdARALLEQLGLGKRLHHLP-----------AQLSGGEQQRVALARAFNGRPALLFADE 172
Cdd:COG4988 428 --RENLRLGR--PDASDEE----LEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 173 PTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPLLAARCDRRLRLVDGQLREEA 228
Cdd:COG4988 500 PTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIVEQG 553
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-215 |
3.85e-35 |
|
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: 123.80 E-value: 3.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 8 EVHHLkkSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEearaalra 87
Cdd:cd03235 1 EVEDL--TVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 88 qHVGFVFQSFMLIPT--LNALENVELPA-----LLRGASDSESQgDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARA 160
Cdd:cd03235 69 -RIGYVPQRRSIDRDfpISVRDVVLMGLyghkgLFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 161 FNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDP-LLAARCDR 215
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLgLVLEYFDR 201
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-206 |
4.24e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 127.51 E-value: 4.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEearaalR 86
Cdd:PRK10851 3 IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQHVGFVFQSFMLIPTLNALENVE-----LPALLRGASDSESQgDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAF 161
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAfgltvLPRRERPNAAAIKA-KVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496080956 162 NGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHD 196
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-206 |
9.99e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.59 E-value: 9.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 19 GEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPL---HRMDEEARAALRaQHVGFVFQ 95
Cdd:PRK11124 13 GAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 96 SFMLIPTLNALEN-VELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:PRK11124 90 QYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190
....*....|....*....|....*....|..
gi 496080956 175 GNLDRQTGDKIADLLFSLnREHGTTLILVTHD 206
Cdd:PRK11124 170 AALDPEITAQIVSIIREL-AETGITQVIVTHE 200
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-224 |
1.21e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 123.73 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALR 86
Cdd:PRK13548 3 LEARNLSVRLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 A---QH--VGFVFqsfmliptlNALENVELPALLRGASDSESQGDARALLEQ---LGLGKRLHHlpaQLSGGEQQRVALA 158
Cdd:PRK13548 79 AvlpQHssLSFPF---------TVEEVVAMGRAPHGLSRAEDDALVAAALAQvdlAHLAGRDYP---QLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 159 RAF------NGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:PRK13548 147 RVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-224 |
1.46e-34 |
|
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: 122.93 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALR 86
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqhVGFVFQSFMLIPTLNALENVELPALLRG----------ASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVA 156
Cdd:cd03219 77 ---IGRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 157 LARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-PLLAARCDRRLRLVDGQL 224
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-223 |
1.47e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 122.94 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 31 LVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraqhVGFVFQSFMLIPTLNALENVE 110
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP------VSMLFQENNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 111 L---PALLRGASDsesQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAF-NGRPALLFaDEPTGNLD---RQtgd 183
Cdd:COG3840 94 LglrPGLKLTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLvRKRPILLL-DEPFSALDpalRQ--- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496080956 184 KIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQ 223
Cdd:COG3840 167 EMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGR 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-227 |
1.83e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.48 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 5 NILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGL-----DDGSSGEVSMLGKPLHRMDe 79
Cdd:PRK14247 2 NKIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 80 earAALRAQHVGFVFQSFMLIPTLNALENVEL-PALLRGA-SDSESQGDARALLEQLGL----GKRLHHLPAQLSGGEQQ 153
Cdd:PRK14247 77 ---VIELRRRVQMVFQIPNPIPNLSIFENVALgLKLNRLVkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 154 RVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDPLLAARC-DRRLRLVDGQLREE 227
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARIsDYVAFLYKGQIVEW 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-206 |
3.40e-34 |
|
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: 124.53 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 41 LIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalraqHVGFVFQSFMLIPTLNALENVELPALLRGASD 120
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR------HINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 121 SESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTL 200
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
....*.
gi 496080956 201 ILVTHD 206
Cdd:TIGR01187 155 VFVTHD 160
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-206 |
3.42e-34 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 122.22 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeearaaLR 86
Cdd:TIGR00968 1 IEIANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------AR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHD 190
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-223 |
4.62e-34 |
|
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: 119.27 E-value: 4.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 8 EVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalra 87
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 88 QHVGFVFQsfmliptlnalenvelpallrgasdsesqgdaralleqlglgkrlhhlpaqLSGGEQQRVALARAFNGRPAL 167
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 168 LFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPLLAAR-CDRRLRLVDGQ 223
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-228 |
1.71e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 121.33 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 5 NILEVHHLKKS------VGQGEHQlSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMD 78
Cdd:PRK10419 2 TLLNVSGLSHHyahgglSGKHQHQ-TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 79 EEARAALRaQHVGFVFQSfmLIPTLNALENV-----ELPALLRGASDSESQGDARALLEQLGLGKR-LHHLPAQLSGGEQ 152
Cdd:PRK10419 81 RAQRKAFR-RDIQMVFQD--SISAVNPRKTVreiirEPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 153 QRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLREEA 228
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQ 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-206 |
2.60e-33 |
|
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: 120.10 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHQLSILTgveLVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraaLR 86
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLN---LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGL--GKRLHHLPAQLSGGEQQRVALARAFNGR 164
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496080956 165 PALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD 195
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
9-227 |
4.83e-33 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 119.91 E-value: 4.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 9 VHHLKKSVGQGEHQ-LSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRa 87
Cdd:TIGR02769 9 THTYRTGGLFGAKQrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 88 QHVGFVFQSfmLIPTLNALENVE------LPALLRgASDSESQGDARALLEQLGL-GKRLHHLPAQLSGGEQQRVALARA 160
Cdd:TIGR02769 88 RDVQLVFQD--SPSAVNPRMTVRqiigepLRHLTS-LDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 161 FNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLREE 227
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-206 |
6.08e-33 |
|
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: 118.98 E-value: 6.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeearaaLR 86
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQHVGFVFQSFMLIPTLNALENV----ELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFN 162
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVafglRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496080956 163 GRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHD 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-227 |
8.28e-33 |
|
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: 124.03 E-value: 8.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSV-------GQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTL-LAILaGLDDgSSGEVSMLGKPL 74
Cdd:COG4172 272 APPLLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLIP-SEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 75 HRMDEEARAALRaQHVGFVFQ----SfmLIPTLNALENVE--LPALLRGASDSESQGDARALLEQLGLGKR-LHHLPAQL 147
Cdd:COG4172 350 DGLSRRALRPLR-RRMQVVFQdpfgS--LSPRMTVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLDPAaRHRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 148 SGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDplLA---ARCDRRLRLVDGQL 224
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHD--LAvvrALAHRVMVMKDGKV 504
|
...
gi 496080956 225 REE 227
Cdd:COG4172 505 VEQ 507
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
28-206 |
4.65e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 118.27 E-value: 4.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 28 GVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraaLRaQHVGFVFQSFMLIPTLNALE 107
Cdd:COG1125 20 DLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LR-RRIGYVIQQIGLFPHMTVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 108 NVELPALLRGASDSESQGDARALLEQLGL--GKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKI 185
Cdd:COG1125 96 NIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQL 175
|
170 180
....*....|....*....|.
gi 496080956 186 ADLLFSLNREHGTTLILVTHD 206
Cdd:COG1125 176 QDELLRLQRELGKTIVFVTHD 196
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-213 |
1.32e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.89 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLkkSVGQGEHQLsiLTGVELVVKPRQTIALIGESGSGKSTLLAILAG-LDDG--SSGEVSMLGKPLHRMDEEARa 83
Cdd:COG4136 2 LSLENL--TITLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 alraqHVGFVFQSFMLIPTLNALENVELpALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNG 163
Cdd:COG4136 77 -----RIGILFQDDLLFPHLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496080956 164 RPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDP---LLAARC 213
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEedaPAAGRV 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-224 |
2.67e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 115.50 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVgqgeHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGL---DDGSSGEVSMLGKPLHRMDEE 80
Cdd:PRK09984 2 QTIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 ARAALRAQ-HVGFVFQSFMLIPTLNALENVELPAL---------LRGASDSESQGDARALlEQLGLGKRLHHLPAQLSGG 150
Cdd:PRK09984 78 ARDIRKSRaNTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQRALQAL-TRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 151 EQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-225 |
7.80e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.06 E-value: 7.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALR 86
Cdd:COG4559 2 LEAENLSVRLGGRT----LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 A---QH--VGFVFqsfmliptlNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAF 161
Cdd:COG4559 78 AvlpQHssLAFPF---------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 162 -------NGRPALLFADEPTGNLDrqtgdkIA------DLLFSLNREhGTTLILVTHDPLLAAR-CDRRLRLVDGQLR 225
Cdd:COG4559 149 aqlwepvDGGPRWLFLDEPTSALD------LAhqhavlRLARQLARR-GGGVVAVLHDLNLAAQyADRILLLHQGRLV 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-225 |
7.91e-31 |
|
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: 116.35 E-value: 7.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 29 VELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHrmDEEARAALRAQ--HVGFVFQSFMLIPTLNAL 106
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ--DSARGIFLPPHrrRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 107 ENVELPalLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIA 186
Cdd:COG4148 96 GNLLYG--RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 187 DLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLR 225
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRVV 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-206 |
8.09e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.03 E-value: 8.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmdeEARAALRaqhvGFVFQSFMLIPTLN 104
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAER----GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDK 184
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 496080956 185 IADLLFSLNREHGTTLILVTHD 206
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-227 |
9.93e-31 |
|
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: 112.91 E-value: 9.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLkkSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALr 86
Cdd:cd03224 1 LEVENL--NAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqHVGFVFQSFMLIPTLNALENVELPALLRGasdsesQGDARALLEQL-----GLGKRLHHLPAQLSGGEQQRVALARAF 161
Cdd:cd03224 76 --GIGYVPEGRRIFPELTVEENLLLGAYARR------RAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 162 NGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAAR-CDRRLRLVDGQLREE 227
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEiADRAYVLERGRVVLE 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-227 |
3.85e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 111.13 E-value: 3.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVkPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH---DplLAARCDRRLRLVDGQLREE 227
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHiveD--VESLCNQVAVLNKGKLVFE 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
37-221 |
6.32e-30 |
|
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: 110.28 E-value: 6.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 37 QTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraqhVGFVFQSFMLIPTLNALENVELPALLR 116
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 117 GASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAF-NGRPALLFaDEPTGNLDRQTGDKIADLLFSLNRE 195
Cdd:cd03298 99 LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLvRDKPVLLL-DEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180
....*....|....*....|....*.
gi 496080956 196 HGTTLILVTHDPLLAARCDRRLRLVD 221
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-219 |
7.66e-30 |
|
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: 115.85 E-value: 7.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmdEEARAALRAQHVGFVFQS-FMLIPTLn 104
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL----ADADADSWRDQIAWVPQHpFLFAGTI- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 aLENVELPAllRGASDSESQGDARA-----LLEQL--GLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNL 177
Cdd:TIGR02857 413 -AENIRLAR--PDASDAEIREALERagldeFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496080956 178 DRQTGDKIADLLFSLNRehGTTLILVTHDPLLAARCDRRLRL 219
Cdd:TIGR02857 490 DAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-224 |
1.07e-29 |
|
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: 108.84 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraQHVGFVFQSFMLIP-TL 103
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG----DHVGYLPQDDELFSgSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 NalENVelpallrgasdsesqgdaralleqlglgkrlhhlpaqLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGD 183
Cdd:cd03246 93 A--ENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496080956 184 KIADLLFSLnREHGTTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:cd03246 134 ALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-215 |
1.49e-29 |
|
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: 109.77 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkplHRMDEEARAALR 86
Cdd:cd03265 1 IEVENLVKKYGDFE----AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVREPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AqhVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03265 74 R--IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLA-ARCDR 215
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDR 201
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-224 |
2.00e-29 |
|
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: 110.62 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRaQHVGFVFQS-----FMli 100
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQFpehqlFE-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 101 ptlnalENVEL-----PALLrGASDSESQGDARALLEQLGLGKR-LHHLPAQLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:TIGR04521 98 ------ETVYKdiafgPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 175 GNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PLLAARCDRRLRLVDGQL 224
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKI 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-206 |
2.04e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 111.75 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 1 MPAENILEVHHLKKS--VGQG-----EHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKP 73
Cdd:COG4608 2 AMAEPLLEVRDLKKHfpVRGGlfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 74 LHRMDEEARAALRaQHVGFVFQ----SfmLIPTLNALENVELPALLRG-ASDSESQGDARALLEQLGLGKR-LHHLPAQL 147
Cdd:COG4608 82 ITGLSGRELRPLR-RRMQMVFQdpyaS--LNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPEhADRYPHEF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 148 SGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-205 |
2.46e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGqGEHQLSiltGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeAR 82
Cdd:COG1129 1 AEPLLEMRGISKSFG-GVKALD---GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS--PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AALRAQhVGFVFQSFMLIPTLNALENVELPALLRGA---SDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALAR 159
Cdd:COG1129 75 DAQAAG-IAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496080956 160 AFNGRPALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISH 198
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
6-228 |
3.88e-29 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 109.31 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDD-----GSSGEVSMLGKPLH--RMD 78
Cdd:TIGR00972 1 AIEIENLNLFYGEKE----ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYdkKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 79 EEAraaLRAqHVGFVFQSFMLIPtLNALENVELPALLRGASD-SESQGDARALLEQLGL----GKRLHHLPAQLSGGEQQ 153
Cdd:TIGR00972 77 VVE---LRR-RVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDkKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 154 RVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPLLAARC-DRRLRLVDGQLREEA 228
Cdd:TIGR00972 152 RLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARIsDRTAFFYDGELVEYG 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-212 |
6.24e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.16 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGL-----DDGSSGEVSMLGKPLHRMD 78
Cdd:PRK14267 2 KFAIETVNLRVYYGSNH----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 79 EEARAALRaqHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDAR--------ALLEQLGlgKRLHHLPAQLSGG 150
Cdd:PRK14267 78 VDPIEVRR--EVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERvewalkkaALWDEVK--DRLNDYPSNLSGG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 151 EQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPLLAAR 212
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAAR 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-224 |
1.67e-28 |
|
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: 106.10 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSV--GQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS--SGEVSMLGKPLHrmdeeaR 82
Cdd:cd03213 4 LSFRNLTVTVksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLD------K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AALRAQhVGFVFQSFMLIPTLNALENVELPALLRGasdsesqgdaralleqlglgkrlhhlpaqLSGGEQQRVALARAFN 162
Cdd:cd03213 78 RSFRKI-IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496080956 163 GRPALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDP--LLAARCDRRLRLVDGQL 224
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-206 |
2.26e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 107.62 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVG-----QGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMD 78
Cdd:COG4167 2 SALLEVRNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 79 eearAALRAQHVGFVFQ--SFMLIPTLNALENVELPalLRGASD-SESQGDAR--ALLEQLGL-GKRLHHLPAQLSGGEQ 152
Cdd:COG4167 82 ----YKYRCKHIRMIFQdpNTSLNPRLNIGQILEEP--LRLNTDlTAEEREERifATLRLVGLlPEHANFYPHMLSSGQK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496080956 153 QRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-206 |
2.69e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 111.34 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKS-TLLAILAGLDDGS----SGEVSMLGKPLHRMDEE 80
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 ARAALRAQHVGFVFQSFMLipTLNALENVE-----LPALLRGASDSESQGDARALLEQLGL---GKRLHHLPAQLSGGEQ 152
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMV--SLNPLHTLEkqlyeVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGER 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496080956 153 QRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHN 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-206 |
6.35e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 106.59 E-value: 6.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRM----- 77
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 78 -----DEEARAALRAQhVGFVFQSFMLIPTLNALENV-ELPALLRGASDSESQGDARALLEQLGLGKRLH-HLPAQLSGG 150
Cdd:PRK10619 78 qlkvaDKNQLRLLRTR-LTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 151 EQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD 206
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHE 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-206 |
6.68e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.50 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaal 85
Cdd:PRK09452 14 LVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 raqHVGFVFQSFMLIPTLNALENVELPalLRGASDSESQGDAR---AL----LEQLGLGKrlhhlPAQLSGGEQQRVALA 158
Cdd:PRK09452 87 ---HVNTVFQSYALFPHMTVFENVAFG--LRMQKTPAAEITPRvmeALrmvqLEEFAQRK-----PHQLSGGQQQRVAIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496080956 159 RAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-227 |
8.77e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.25 E-value: 8.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeaRAALRaQHVGFVFQSFMLIpTLN 104
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR-RQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVelpALLR-GASDSEsqgdARALLEQLGLGKRLHHLP-----------AQLSGGEQQRVALARAFNGRPALLFADE 172
Cdd:COG1132 430 IRENI---RYGRpDATDEE----VEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 173 PTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:COG1132 503 ATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-228 |
9.27e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 106.64 E-value: 9.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmDEEAR 82
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AALRAQhVGFVFQ---------------SFmliptlnALENvelpallRGASDSESQGDARALLEQLGLGKRLHHLPAQL 147
Cdd:PRK13635 77 WDVRRQ-VGMVFQnpdnqfvgatvqddvAF-------GLEN-------IGVPREEMVERVDQALRQVGMEDFLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 148 SGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
.
gi 496080956 228 A 228
Cdd:PRK13635 222 G 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-227 |
1.84e-27 |
|
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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 105.20 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkpLHRMDEEARAALR 86
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQ---------------SFmliptlnALENvelpallRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGE 151
Cdd:TIGR04520 77 -KKVGMVFQnpdnqfvgatveddvAF-------GLEN-------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 152 QQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-215 |
1.94e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.12 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 2 PAENILEVHHLkkSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDD---GS--SGEVSMLGKPLHR 76
Cdd:COG1117 7 TLEPKIEVRNL--NVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipGArvEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 77 MDEEArAALRAQhVGFVFQsfmlipTLNAL-----ENVELPALLRGASD-SESQGDARALLEQLGLGK----RLHHLPAQ 146
Cdd:COG1117 83 PDVDV-VELRRR-VGMVFQ------KPNPFpksiyDNVAYGLRLHGIKSkSELDEIVEESLRKAALWDevkdRLKKSALG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 147 LSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPLLAARC-DR 215
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVsDY 222
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
28-228 |
3.84e-27 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 103.60 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 28 GVELVVKPRQTIALIGESGSGKS-TLLAILAGLDDG---SSGEVSMLGKPLhrmdeeARAALRAQHVGFVFQSFM--LIP 101
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPPGltqTSGEILLDGRPL------LPLSIRGRHIATIMQNPRtaFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 TLNALENVELPALLRGASDSESQGDARALLEQLGL--GKRLHHL-PAQLSGGEQQRVALARAFNGRPALLFADEPTGNLD 178
Cdd:TIGR02770 78 LFTMGNHAIETLRSLGKLSKQARALILEALEAVGLpdPEEVLKKyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 179 RQTGDKIADLLFSLNREHGTTLILVTHDPLLAARC-DRRLRLVDGQLREEA 228
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLFGTGILLITHDLGVVARIaDEVAVMDDGRIVERG 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-225 |
4.05e-27 |
|
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: 103.13 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPlhrMDEEARaalr 86
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP---LDIAAR---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03269 70 -NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLR 225
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-203 |
4.14e-27 |
|
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: 103.52 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLkkSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARA 83
Cdd:COG0410 1 MPMLEVENL--HAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 ALraqHVGFVFQSFMLIPTLNALENVELPALLRGasdseSQGDARALLEQLG-----LGKRLHHLPAQLSGGEQQRVALA 158
Cdd:COG0410 77 RL---GIGYVPEGRRIFPSLTVEENLLLGAYARR-----DRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 159 RAFNGRPALLFADEPTgnldrqTG------DKIADLLFSLNREhGTTLILV 203
Cdd:COG0410 149 RALMSRPKLLLLDEPS------LGlaplivEEIFEIIRRLNRE-GVTILLV 192
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
15-225 |
8.69e-27 |
|
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: 105.19 E-value: 8.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 15 SVGQGEHQLSI---LTGVELVvkprqtiALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHrmDEEARAALRAQH-- 89
Cdd:TIGR02142 6 SKRLGDFSLDAdftLPGQGVT-------AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLPPEKrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 90 VGFVFQSFMLIPTLNALENVELPalLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLF 169
Cdd:TIGR02142 77 IGYVFQEARLFPHLSVRGNLRYG--MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 170 ADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLR 225
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVA 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-227 |
1.01e-26 |
|
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: 106.81 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDD--GSSGEV----------------S 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 69 MLGKP--------------LHRMDEEARAALRaQHVGFVFQ-SFMLIPTLNALENVeLPALLR-GASDSESQGDARALLE 132
Cdd:TIGR03269 77 KVGEPcpvcggtlepeevdFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNV-LEALEEiGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 133 QLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDP-LLAA 211
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPeVIED 234
|
250
....*....|....*.
gi 496080956 212 RCDRRLRLVDGQLREE 227
Cdd:TIGR03269 235 LSDKAIWLENGEIKEE 250
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-223 |
1.56e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.82 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVsmlgkplhRMDEEARAALRAQhvgfvfQSFMLIPTLn 104
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGARVLFLPQ------RPYLPLGTL- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 aLENVELPALLRGASDSEsqgdARALLEQLGLGKRLHHL------PAQLSGGEQQRVALARAFNGRPALLFADEPTGNLD 178
Cdd:COG4178 443 -REALLYPATAEAFSDAE----LREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496080956 179 RQTGDKIADLLfsLNREHGTTLILVTHDPLLAARCDRRLRLVDGQ 223
Cdd:COG4178 518 EENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-228 |
1.73e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 101.52 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalr 86
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQgdarALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03268 73 --RIGALIEAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHdpLLA---ARCDRRLRLVDGQLREEA 228
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSH--LLSeiqKVADRIGIINKGKLIEEG 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
42-206 |
2.69e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.34 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 42 IGESGSGKSTLLAILAGLDDGSSGEVSMLGKplhRMDEEARAAlraQHVGFVFQSFMLIPTLNALENVELPALLRGASDS 121
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPAE---RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 122 ESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDR----QTGDKIADLLFSLNRehg 197
Cdd:PRK11000 109 EINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvQMRIEISRLHKRLGR--- 185
|
....*....
gi 496080956 198 tTLILVTHD 206
Cdd:PRK11000 186 -TMIYVTHD 193
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-206 |
3.06e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 9 VHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMlgkplhrmdeeaRAALRaq 88
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------------PKGLR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 89 hVGFVFQSFMLIPTLNALENV------------ELPALLRGASDSESQGD--------------------ARALLEQLGL 136
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVldgdaelraleaELEELEAKLAEPDEDLErlaelqeefealggweaearAEEILSGLGF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 137 GKRLHHLP-AQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-206 |
4.87e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.70 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQG---EHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAR 82
Cdd:COG1101 1 MLELKNLSKTFNPGtvnEKR--ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AAlraqHVGFVFQSFML--IPTLNALENVELpALLRGAS-------DSESQGDARALLEQLGLG--KRLHHLPAQLSGGE 151
Cdd:COG1101 79 AK----YIGRVFQDPMMgtAPSMTIEENLAL-AYRRGKRrglrrglTKKRRELFRELLATLGLGleNRLDTKVGLLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 152 QQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-226 |
1.21e-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: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSmLGKPLhrmdeearaal 85
Cdd:COG0488 315 VLELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 raqHVGFVFQSF-MLIPTLNALENvelpalLRGASDSESQGDARALLEQLGL-GKRLHHLPAQLSGGEQQRVALARAFNG 163
Cdd:COG0488 379 ---KIGYFDQHQeELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496080956 164 RPALLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDP-LLAARCDRRLRLVDGQLRE 226
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEAL----DDFPGTVLLVSHDRyFLDRVATRILEFEDGGVRE 509
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
25-223 |
1.25e-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: 100.16 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAG-LDDGSSGEVSMLGKPLHRMD-EEARaalraQHVGFVFQSFM--LI 100
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDvWELR-----KRIGLVSPALQlrFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 101 PTLNALEnvelpALLRGASDS---------ESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFAD 171
Cdd:COG1119 93 RDETVLD-----VVLSGFFDSiglyreptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496080956 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARC-DRRLRLVDGQ 223
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-206 |
2.10e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 101.72 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 1 MPAENILEVHHLKKSVGQGehqlSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkplhrmDEE 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG------EDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 ARAALRAQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQ---GDARALLEQLGLGKRLhhlPAQLSGGEQQRVAL 157
Cdd:PRK11432 71 THRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKqrvKEALELVDLAGFEDRY---VDQISGGQQQRVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496080956 158 ARAFNGRPALLFADEPTGNLD----RQTGDKIADLLFSLNrehgTTLILVTHD 206
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDanlrRSMREKIRELQQQFN----ITSLYVTHD 196
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-221 |
2.53e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.94 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkplhRMDEEARAALRAQhVGFVF-QSFMLIPTLN 104
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKFLRR-IGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDK 184
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190
....*....|....*....|....*....|....*..
gi 496080956 185 IADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVD 221
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-225 |
3.24e-25 |
|
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: 102.90 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraQHVGFVFQSFMLIP-TL 103
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG----RHIGYLPQDVELFDgTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 NalENVelpALLRGASDSESQGDARALleqlglgkRLH----HLP-----------AQLSGGEQQRVALARAFNGRPALL 168
Cdd:COG4618 423 A--ENI---ARFGDADPEKVVAAAKLA--------GVHemilRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 169 FADEPTGNLDRQtGDK-----IADLlfslnREHGTTLILVTHDPLLAARCDRRLRLVDGQLR 225
Cdd:COG4618 490 VLDEPNSNLDDE-GEAalaaaIRAL-----KARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-206 |
5.26e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.07 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVgQGEHQLSiltGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAal 85
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 raqhVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:PRK11607 93 ----INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHD 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-224 |
8.90e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 98.61 E-value: 8.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEhqlSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhRMDEEARAAL 85
Cdd:PRK13639 1 ILETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RaQHVGFVFQS---FMLIPTLnaLENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFN 162
Cdd:PRK13639 77 R-KTVGIVFQNpddQLFAPTV--EEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 163 GRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD-PLLAARCDRRLRLVDGQL 224
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDvDLVPVYADKVYVMSDGKI 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-227 |
9.70e-25 |
|
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: 101.74 E-value: 9.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeaRAALR 86
Cdd:TIGR01193 474 IVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aQHVGFVFQS-FMLIPTLnaLENvelpaLLRGASDSESQGDARALLE-----------QLGLGKRLHHLPAQLSGGEQQR 154
Cdd:TIGR01193 548 -QFINYLPQEpYIFSGSI--LEN-----LLLGAKENVSQDEIWAACEiaeikddienmPLGYQTELSEEGSSISGGQKQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 155 VALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhgtTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-226 |
1.04e-24 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 97.98 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHqlsiLTGVELVVKPRQTIALIGESGSGKSTLLAILAG---LDDGSSGEVSMLGKP--LHRMDEE 80
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrlaPDHGTATYIMRSGAEleLYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 ARAALRAQHVGFVFQSFM--LIPTLNALENVELPALLRGAsdsESQGDARAL----LEQLGLGK-RLHHLPAQLSGGEQQ 153
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQNPRdgLRMRVSAGANIGERLMAIGA---RHYGNIRATaqdwLEEVEIDPtRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 154 RVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDpLLAAR--CDRRLRLVDGQLRE 226
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHD-LGVARllAQRLLVMQQGRVVE 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-224 |
1.18e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 96.89 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 20 EHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeaRAALRaQHVGFVFQSFML 99
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 100 IP-TLNalENVELPALLrgASDSE-------------SQGDARALLEQLGLGKRlhhlpaQLSGGEQQRVALARAFNGRP 165
Cdd:cd03245 90 FYgTLR--DNITLGAPL--ADDERilraaelagvtdfVNKHPNGLDLQIGERGR------GLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-227 |
1.26e-24 |
|
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: 95.84 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEaraalR 86
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQHVGFVFQSFMLIPTlnalenvelpallrgasdsesqgdarALLEQLGlgkrlhhlpAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03247 74 SSLISVLNQRPYLFDT--------------------------TLRNNLG---------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
37-226 |
2.17e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.64 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 37 QTIALIGESGSGKSTLLAILAGL--DDGS-SGEVSMLGKPLHRMDEEARAALRAQHVGFVFQSFM--LIPTLNALENV-E 110
Cdd:PRK09473 43 ETLGIVGESGSGKSQTAFALMGLlaANGRiGGSATFNGREILNLPEKELNKLRAEQISMIFQDPMtsLNPYMRVGEQLmE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 111 LPALLRGASDSESQGDARALLEQLGLG---KRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIAD 187
Cdd:PRK09473 123 VLMLHKGMSKAEAFEESVRMLDAVKMPearKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 188 LLFSLNREHGTTLILVTHD-PLLAARCDRRLRLVDGQLRE 226
Cdd:PRK09473 203 LLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGRTME 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-204 |
2.43e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.17 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVGQ-----GEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMD 78
Cdd:PRK15112 2 ETLLEVRNLSKTFRYrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 79 eearAALRAQHVGFVFQ--SFMLIPTLNALENVELPALLRGASDSESQGDA-RALLEQLGL-GKRLHHLPAQLSGGEQQR 154
Cdd:PRK15112 82 ----YSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQiIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496080956 155 VALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVT 204
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-207 |
2.87e-24 |
|
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: 96.19 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS---SGEVSMLGKPLHRmdeearaALRAQHVGFVFQSFMLIP 101
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKP-------DQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 TLNALENVELPALLR-GASDSESQGDARA---LLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNL 177
Cdd:cd03234 95 GLTVRETLTYTAILRlPRKSSDAIRKKRVedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190
....*....|....*....|....*....|
gi 496080956 178 DRQTGDKIADLLFSLNREhGTTLILVTHDP 207
Cdd:cd03234 175 DSFTALNLVSTLSQLARR-NRIVILTIHQP 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
5.47e-24 |
|
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: 99.11 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKK---SVGQGehQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSM--------LGK 72
Cdd:TIGR03269 277 EPIIKVRNVSKryiSVDRG--VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 73 PlhRMDEEARAAlraQHVGFVFQSFMLIPTLNALEN------VELP---ALLRGASDSESQG----DARALLEQLglgkr 139
Cdd:TIGR03269 355 P--GPDGRGRAK---RYIGILHQEYDLYPHRTVLDNlteaigLELPdelARMKAVITLKMVGfdeeKAEEILDKY----- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 140 lhhlPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PLLAARCDRRLR 218
Cdd:TIGR03269 425 ----PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAAL 500
|
....*.
gi 496080956 219 LVDGQL 224
Cdd:TIGR03269 501 MRDGKI 506
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-227 |
6.26e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 94.74 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 raqhvGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:cd03266 81 -----GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLREE 227
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYE 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-226 |
6.76e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.13 E-value: 6.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 22 QLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEearAALRAQhVGFVFQSFMLIP 101
Cdd:PRK11160 352 PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALRQA-ISVVSQRVHLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 -TLNalENvelpalLRGASDSESQGDARALLEQLGLGKRL---HHLPA-------QLSGGEQQRVALARAFNGRPALLFA 170
Cdd:PRK11160 428 aTLR--DN------LLLAAPNASDEALIEVLQQVGLEKLLeddKGLNAwlgeggrQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 171 DEPTGNLDRQTGDKIADLLFslnrEH--GTTLILVTHDPLLAARCDRRLRLVDGQLRE 226
Cdd:PRK11160 500 DEPTEGLDAETERQILELLA----EHaqNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-207 |
7.31e-24 |
|
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: 98.97 E-value: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALraqhVGFVFQSFMLIPTlN 104
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPAllRGASDSEsqgdARALLEQLGLGKRLHHLP-----------AQLSGGEQQRVALARAFNGRPALLFADEP 173
Cdd:TIGR02868 425 VRENLRLAR--PDATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....
gi 496080956 174 TGNLDRQTGDKIADLLFSLNRehGTTLILVTHDP 207
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-206 |
8.03e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 96.96 E-value: 8.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAR 82
Cdd:PRK11308 8 AIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AALRaQHVGFVFQSfmliP--TLNALENV----ELPALLRGA-SDSESQGDARALLEQLGLgkRLHH---LPAQLSGGEQ 152
Cdd:PRK11308 88 KLLR-QKIQIVFQN----PygSLNPRKKVgqilEEPLLINTSlSAAERREKALAMMAKVGL--RPEHydrYPHMFSGGQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496080956 153 QRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-206 |
8.97e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 12 LKKSVGQGehqlSILTGVELVVKPRQTIALIGESGSGKSTL-LAILAGLddGSSGEVSMLGKPLHRMDEEARAALRAQhV 90
Cdd:PRK15134 292 LKRTVDHN----VVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLNRRQLLPVRHR-I 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 91 GFVFQ--SFMLIPTLNALENVELPALLRGASDSESQGDAR--ALLEQLGLGKRLHH-LPAQLSGGEQQRVALARAFNGRP 165
Cdd:PRK15134 365 QVVFQdpNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQviAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-205 |
9.07e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 9.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 28 GVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeARAALRAqHVGFVFQSFMLIPTLNALE 107
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRS--PRDAIAL-GIGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 108 NVEL---PALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDK 184
Cdd:COG3845 100 NIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADE 179
|
170 180
....*....|....*....|.
gi 496080956 185 IADLLFSLnREHGTTLILVTH 205
Cdd:COG3845 180 LFEILRRL-AAEGKSIIFITH 199
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-212 |
1.01e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 95.38 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 1 MPAENILEVHHLKKSVGQGEHqlsiLTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGK-----PLH 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 76 RMDEEARAALRAQHVGFVFQSFM--LIPTLNALENVELPALLRGAsdsESQGDARAL----LEQLGLG-KRLHHLPAQLS 148
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGA---RHYGDIRATagdwLERVEIDaARIDDLPTTFS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 149 GGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD----PLLAAR 212
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDlavaRLLAHR 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-220 |
1.96e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.03 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 31 LVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRAQHVGFVFQSFMLIPTLNALENVE 110
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 111 LPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLF 190
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|
gi 496080956 191 SLNREHGTTLILVTHDPLLAARCDRRLRLV 220
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-224 |
2.57e-23 |
|
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: 93.39 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 30 ELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKplhrmdEEARAALRAQHVGFVFQSFMLIPTLNALENV 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ------SHTGLAPYQRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 110 EL---PALLRGAsdsESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIA 186
Cdd:TIGR01277 92 GLglhPGLKLNA---EQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 496080956 187 DLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-207 |
3.18e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 97.43 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 22 QLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS---SGEVSMLGKPLHRMDEEARAAlraqhvgFVFQSFM 98
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISA-------YVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 99 LIPTLNALENVELPALLR-GASDSESQGDAR--ALLEQLGLGKRLHHL---PAQ---LSGGEQQRVALARAFNGRPALLF 169
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRmPRRVTKKEKRERvdEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 496080956 170 ADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDP 207
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQP 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-226 |
3.43e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.96 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 24 SILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDD------GSSGEVSMLGKPLHRMDeearAALRAQHVGFVFQSF 97
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQID----AIKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 98 MLIPTLNALENVELPALLRGASDS-ESQGDARALLEQLGLGK----RLHHLPAQLSGGEQQRVALARAFNGRPALLFADE 172
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 173 PTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDPLLAAR-CDRRLRLVDGQLRE 226
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
5.67e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVGQGEHQLSiltGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmDEEARA 83
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALK---GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI---DYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 ALR-AQHVGFVFQSfmliP-----TLNALENVELPALLRGASDSESQGDARALLEQLGLgKRLHHLPAQ-LSGGEQQRVA 156
Cdd:PRK13636 77 LMKlRESVGMVFQD----PdnqlfSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 157 LARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PLLAARCDRRLRLVDGQ 223
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGR 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-215 |
1.21e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.25 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGqgEHQlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmDEEARaal 85
Cdd:COG4152 1 MLELKGLTKRFG--DKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDR--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 raQHVGFvfqsfM-----LIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARA 160
Cdd:COG4152 71 --RRIGY-----LpeergLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 161 FNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAAR-CDR 215
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEElCDR 198
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-227 |
2.69e-22 |
|
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: 91.14 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraaLRaQHVGFVFQSFMLIPTlN 104
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR-RAIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPALlrGASDSESQGDARALleqlGLGKRLHHLPAQ-----------LSGGEQQRVALARAFNGRPALLFADEP 173
Cdd:cd03253 91 IGYNIRYGRP--DATDEEVIEAAKAA----QIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496080956 174 TGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVER 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-206 |
3.50e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.46 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLK-----KSVGQGEHQ----LSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHR 76
Cdd:PRK15079 8 LLEVADLKvhfdiKDGKQWFWQppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 77 MDEEARAALRaQHVGFVFQSFM--LIPTLNALENVELPalLR----GASDSESQGDARALLEQLGLGKRL-HHLPAQLSG 149
Cdd:PRK15079 88 MKDDEWRAVR-SDIQMIFQDPLasLNPRMTIGEIIAEP--LRtyhpKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 150 GEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
25-227 |
5.33e-22 |
|
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: 89.90 E-value: 5.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPlhrmdeearAALRAQHVGFVfqsfmliPTLN 104
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---------SSLLGLGGGFN-------PELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPALLRGASDSESQGDARALLEQLGLGKRLhHLP-AQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGD 183
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-DLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496080956 184 KIADLLFSLnREHGTTLILVTHDP-LLAARCDRRLRLVDGQLREE 227
Cdd:cd03220 180 KCQRRLREL-LKQGKTVILVSHDPsSIKRLCDRALVLEKGKIRFD 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-205 |
6.27e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.23 E-value: 6.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVsMLGKplHRMDEEARA----ALRaQHVGFVFQsfmlIP 101
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-TIGE--RVITAGKKNkklkPLR-KKVGIVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 TlNAL--ENVE----LPALLRGASDSESQGDARALLEQLGLGKR-LHHLPAQLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:PRK13634 95 E-HQLfeETVEkdicFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190
....*....|....*....|....*....|.
gi 496080956 175 GNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-224 |
1.18e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 89.26 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 31 LVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraqhVGFVFQSFMLIPTLNALENVE 110
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP------VSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 111 L---PALlrgASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIAD 187
Cdd:PRK10771 94 LglnPGL---KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 496080956 188 LLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRI 208
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
37-227 |
1.24e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.96 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 37 QTIALIGESGSGKS-TLLAILaGLDDG----SSGEVSMLGKPLHRMDEEARAALRAQHVGFVFQSFMliPTLNALENV-- 109
Cdd:PRK11022 34 EVVGIVGESGSGKSvSSLAIM-GLIDYpgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPM--TSLNPCYTVgf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 110 ---ELPALLRGASDSESQGDARALLEQLGL---GKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGD 183
Cdd:PRK11022 111 qimEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496080956 184 KIADLLFSLNREHGTTLILVTHD-PLLAARCDRRLRLVDGQLREE 227
Cdd:PRK11022 191 QIIELLLELQQKENMALVLITHDlALVAEAAHKIIVMYAGQVVET 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-226 |
1.26e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.45 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDD-----GSSGEVSMLGKPLH--R 76
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYspR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 77 MDEearAALRaQHVGFVFQSFMLIPtLNALENVELPALLRGASDSESQGDA-RALLEQLGL----GKRLHHLPAQLSGGE 151
Cdd:PRK14239 79 TDT---VDLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAvEKSLKGASIwdevKDRLHDSALGLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 152 QQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPLLAAR-CDRRLRLVDGQLRE 226
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRiSDRTGFFLDGDLIE 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-227 |
1.36e-21 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 88.82 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 20 EHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeaRAALRaQHVGFVFQSFML 99
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLR-SMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 100 IPTlNALENVELpallrgASDSESQGDARALLEQLGLGKRLHHLP-----------AQLSGGEQQRVALARAFNGRPALL 168
Cdd:cd03254 89 FSG-TIMENIRL------GRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 169 FADEPTGNLDRQTGDKIADLLFSLNreHGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEE 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-219 |
1.88e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.94 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 19 GEHQLsiLTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALR--AQHVGfvfqs 96
Cdd:PRK13538 12 DERIL--FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylGHQPG----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 97 fmLIPTLNALENVELPALLRGASDSESQGDAralLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGN 176
Cdd:PRK13538 85 --IKTELTALENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496080956 177 LDRQTgdkIADL--LFSLNREHGTTLILVTHDPL-LAARCDRRLRL 219
Cdd:PRK13538 160 IDKQG---VARLeaLLAQHAEQGGMVILTTHQDLpVASDKVRKLRL 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-226 |
2.30e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 1 MPAENILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHR---- 76
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 77 ---MDEEARAAL---RAQHVGFVFQSFM--LIPTLNALENV-ELPALLRGASDSESQGDARALLEQLGLGKR---LHHLP 144
Cdd:PRK10261 87 vieLSEQSAAQMrhvRGADMAMIFQEPMtsLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 145 AQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PLLAARCDRRLRLVDGQ 223
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVLVMYQGE 246
|
...
gi 496080956 224 LRE 226
Cdd:PRK10261 247 AVE 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-224 |
3.38e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.09 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 2 PAENILEVHHLKKSVGQGEHqlSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGL---DDGSSGEVSMLGKPLhrmD 78
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKK--PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITL---T 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 79 EEARAALRaQHVGFVFQS----FMLIPTLN----ALENvelpallRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGG 150
Cdd:PRK13640 76 AKTVWDIR-EKVGIVFQNpdnqFVGATVGDdvafGLEN-------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496080956 151 EQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-224 |
5.12e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.97 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGsSGEVSMLGKPLHRMDEEARAALRA---QHV--GF---VFQSF 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAylsQQQspPFampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 98 MLiptlnalenvELPAllrGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAF-------NGRPALLFA 170
Cdd:COG4138 91 AL----------HQPA---GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 171 DEPTGNLDrqtgdkIA-----DLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:COG4138 158 DEPMNSLD------VAqqaalDRLLRELCQQGITVVMSSHDLNHTLRhADRVWLLKQGKL 211
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-224 |
1.12e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 89.71 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraQHVGFVFQSFMLIPTLN 104
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 AlENVelpALLRGASDSESQGDARALLeqlGLGKRLHHLP-----------AQLSGGEQQRVALARAFNGRPALLFADEP 173
Cdd:TIGR01842 409 A-ENI---ARFGENADPEKIIEAAKLA---GVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 174 TGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-224 |
1.70e-20 |
|
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: 84.40 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeARAALR 86
Cdd:cd03216 1 LELRGITKRFGGVK----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS--PRDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQhVGFVFqsfmliptlnalenvelpallrgasdsesqgdaralleqlglgkrlhhlpaQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03216 75 AG-IAMVY---------------------------------------------------QLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
39-206 |
2.15e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.81 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKplHRMDEEARAALRA--QHVGFVFQ---SFMLIPTLnaLENVELPA 113
Cdd:PRK13641 36 VALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY--HITPETGNKNLKKlrKKVSLVFQfpeAQLFENTV--LKDVEFGP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 114 LLRGASDSESQGDARALLEQLGLGKRL-HHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSL 192
Cdd:PRK13641 112 KNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY 191
|
170
....*....|....
gi 496080956 193 NREhGTTLILVTHD 206
Cdd:PRK13641 192 QKA-GHTVILVTHN 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-205 |
3.29e-20 |
|
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: 88.92 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 37 QTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmdEEARAALRaQHVGFVFQSFMLIPTLNALENVELPALLR 116
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVR-QSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 117 GASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLfsLNREH 196
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRS 1109
|
....*....
gi 496080956 197 GTTLILVTH 205
Cdd:TIGR01257 1110 GRTIIMSTH 1118
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-206 |
3.61e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGK-PLHRmdeeaRAALrAQHVGFVF-QSFMLIPTL 103
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKR-----RKEF-ARRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 NALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHlPA-QLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTG 182
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180
....*....|....*....|....
gi 496080956 183 DKIADLLFSLNREHGTTLILVTHD 206
Cdd:COG4586 191 EAIREFLKEYNRERGTTILLTSHD 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-211 |
3.71e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVGQGEHQLSiltGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHrmdEEARA 83
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALK---GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 ALRAQhVGFVFQSfmliP-----TLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALA 158
Cdd:PRK13647 76 WVRSK-VGLVFQD----PddqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496080956 159 RAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAA 211
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAA 202
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-206 |
3.72e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.68 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 22 QLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVS----------------------MLGKPLHRMDE 79
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvleklVIQKTRFKKIK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 80 EARAaLRAQhVGFVFQ--SFMLIPTlNALENVELPALLRGASDSESQGDARALLEQLGLGKR-LHHLPAQLSGGEQQRVA 156
Cdd:PRK13651 99 KIKE-IRRR-VGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496080956 157 LARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD 206
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHD 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-210 |
3.98e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.21 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 28 GVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraqhVGFVFQSFMLIPTLNALE 107
Cdd:PRK11650 22 GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD------IAMVFQNYALYPHMSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 108 NVELPALLRGASDSESQ---GDARALLEqlgLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDrqtgdk 184
Cdd:PRK11650 96 NMAYGLKIRGMPKAEIEervAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD------ 166
|
170 180 190
....*....|....*....|....*....|...
gi 496080956 185 iADL-------LFSLNREHGTTLILVTHDPLLA 210
Cdd:PRK11650 167 -AKLrvqmrleIQRLHRRLKTTSLYVTHDQVEA 198
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-224 |
4.47e-20 |
|
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: 83.64 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLkkSVGQGehqlsiLTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeAR 82
Cdd:cd03215 1 GEPVLEVRGL--SVKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS--PR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AALRAqHVGFV---FQSFMLIPTLNALENVELPALLrgasdsesqgdaralleqlglgkrlhhlpaqlSGGEQQRVALAR 159
Cdd:cd03215 71 DAIRA-GIAYVpedRKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLAR 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 160 AFNGRPALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-PLLAARCDRRLRLVDGQL 224
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-208 |
5.39e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.95 E-value: 5.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLkkSVGQGEhqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEaraalR 86
Cdd:TIGR01189 1 LAARNL--ACSRGE--RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 AQHVGFVFQSFMLIPTLNALENVE-LPALLRGAsdsesQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSALENLHfWAAIHGGA-----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLfslnREH---GTTLILVTHDPL 208
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLL----RAHlarGGIVLLTTHQDL 188
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-228 |
1.19e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.76 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 24 SILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSG-----EVSMLGKPL--HRMDEEARaalraQHVGFVFQS 96
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnYRDVLEFR-----RRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 97 ---FMLIPTLNALENVELPALLrgaSDSESQGDARALLEQLGL----GKRLHHLPAQLSGGEQQRVALARAFNGRPALLF 169
Cdd:PRK14271 110 pnpFPMSIMDNVLAGVRAHKLV---PRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 170 ADEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDPLLAAR-CDRRLRLVDGQLREEA 228
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGRLVEEG 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-205 |
1.34e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.52 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGL-DDGS-SGEVSMLGKPLH----R 76
Cdd:PRK13549 2 MEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyPHGTyEGEIIFEGEELQasniR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 77 MDEEARAALraqhvgfVFQSFMLIPTLNALENVELPA-LLRGA--SDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQ 153
Cdd:PRK13549 78 DTERAGIAI-------IHQELALVKELSVLENIFLGNeITPGGimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496080956 154 RVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISH 201
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
42-215 |
1.69e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 86.72 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 42 IGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalraQHVGFVFQSFMLIPTLNALENVELPALLRGASDS 121
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR-----RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 122 ESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLI 201
Cdd:NF033858 373 EIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIF 452
|
170
....*....|....
gi 496080956 202 LVTHDPLLAARCDR 215
Cdd:NF033858 453 ISTHFMNEAERCDR 466
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-219 |
1.81e-19 |
|
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: 82.93 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 23 LSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRM-DEEARAALRAQHVGfvfqsfMLIP 101
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrDSIARGLLYLGHAP------GIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 TLNALENVELPALLRGASDSESQgdaralLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQT 181
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQVEEA------LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 496080956 182 GDKIADLLFSlNREHGTTLILVTHDPL-LAARCDRRLRL 219
Cdd:cd03231 161 VARFAEAMAG-HCARGGMVVLTTHQDLgLSEAGARELDL 198
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
28-206 |
1.84e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.89 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 28 GVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALraqhvGFV--FQSFMLIPTLNA 105
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-----GVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 LENVE-----------LPALLRGASDSESQGDA--RAL--LEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFA 170
Cdd:PRK11300 98 IENLLvaqhqqlktglFSGLLKTPAFRRAESEAldRAAtwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 496080956 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-219 |
2.64e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.90 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVsmlgkplhrmdeEARAALRaqhVGFVFQSFMLIPTLNA 105
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGAR---VAYVPQRSEVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 --LENVELPALLRGASDSESQGDARAL----LEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDR 179
Cdd:NF040873 73 tvRDLVAMGRWARRGLWRRLTRDDRAAvddaLERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 180 QTGDKIADLLFSLNREhGTTLILVTHDPLLAARCDRRLRL 219
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-206 |
3.18e-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: 80.57 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVsmlgkplhrmdeearaalr 86
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqhvgfvfqsfmliptlnalenvelpallrgasdsesqgdaralleQLGLGKRLHHLPaQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03221 58 ----------------------------------------------TWGSTVKIGYFE-QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHD 126
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-208 |
3.65e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.84 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPlhrmDEEARAALRAQHVGfvFQSFMLiPTLN 104
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAEACHYLG--HRNAMK-PALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPALLRGASDSesqgDARALLEQLGLGkRLHHLPAQ-LSGGEQQRVALAR-AFNGRPALLFaDEPTGNLDRQTG 182
Cdd:PRK13539 90 VAENLEFWAAFLGGEEL----DIAAALEAVGLA-PLAHLPFGyLSAGQKRRVALARlLVSNRPIWIL-DEPTAALDAAAV 163
|
170 180
....*....|....*....|....*.
gi 496080956 183 DKIADlLFSLNREHGTTLILVTHDPL 208
Cdd:PRK13539 164 ALFAE-LIRAHLAQGGIVIAATHIPL 188
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-205 |
4.19e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.56 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrMDEEARAALRAQHVGFVFQsfmlIPTLNA 105
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI--TDKKVKLSDIRKKVGLVFQ----YPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 LE-----NVELPALLRGASDSESQGDARALLEQLGLGKR--LHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLD 178
Cdd:PRK13637 97 FEetiekDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180
....*....|....*....|....*..
gi 496080956 179 RQTGDKIADLLFSLNREHGTTLILVTH 205
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSH 203
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
25-206 |
4.42e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.07 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraQHVGFVFQSfmliPTL- 103
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR----QQVSYCAQT----PTLf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 --NALENVELPALLRGASDSESQgdARALLEQLGLGKRLHHLP-AQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQ 180
Cdd:PRK10247 94 gdTVYDNLIFPWQIRNQQPDPAI--FLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180
....*....|....*....|....*.
gi 496080956 181 TGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-223 |
6.12e-19 |
|
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: 84.88 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGL-DDGS-SGEVSMLGKPL---HRMDEE 80
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyPHGTwDGEIYWSGSPLkasNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 ARAalraqhVGFVFQSFMLIPTLNALENVEL--PALLRGA--SDSESQGDARALLEQLGLGKRLHHLP-AQLSGGEQQRV 155
Cdd:TIGR02633 77 RAG------IVIIHQELTLVPELSVAENIFLgnEITLPGGrmAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 156 ALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTHD-PLLAARCDRRLRLVDGQ 223
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-221 |
7.62e-19 |
|
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: 80.28 E-value: 7.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLkkSVGQGEHQLsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPlhrmdeearaalr 86
Cdd:cd03223 1 IELENL--SLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 87 aqHVGFVFQsfmliptlnalenveLPALLRGAsdsesqgdaraLLEQLglgkrLHHLPAQLSGGEQQRVALARAFNGRPA 166
Cdd:cd03223 65 --DLLFLPQ---------------RPYLPLGT-----------LREQL-----IYPWDDVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDPLLAARCDRRLRLVD 221
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-224 |
7.76e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.47 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVGQGEHQLsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkplHRMDEEARA 83
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 ALRaQHVGFVFQS----FMLIPTLN----ALENvelpallRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRV 155
Cdd:PRK13650 78 DIR-HKIGMVFQNpdnqFVGATVEDdvafGLEN-------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 156 ALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
40-227 |
8.60e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRM--DEEARAaLRaQHVGFVFQsfmlIPTLNALE-NVELPALLR 116
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRP-VR-KRIGMVFQ----FPESQLFEdTVEREIIFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 117 ----GASDSESQGDARALLEQLGLGKRLHHL-PAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFS 191
Cdd:PRK13646 111 pknfKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKS 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 496080956 192 LNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQLREE 227
Cdd:PRK13646 191 LQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQ 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
28-228 |
9.90e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.05 E-value: 9.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 28 GVELVVKPRQTIALIGESGSGKS-TLLAILAGLDDG---SSGEVSMLGKPLhrmdeeARAALRAQHVGFVFQ----SFML 99
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAGvrqTAGRVLLDGKPV------APCALRGRKIATIMQnprsAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 100 IPTLNALENVELPALLRGASDSEsqgdARALLEQLGLGKR---LHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGN 176
Cdd:PRK10418 95 LHTMHTHARETCLALGKPADDAT----LTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496080956 177 LDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARC-DRRLRLVDGQLREEA 228
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-215 |
1.76e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.16 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGehqlSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaal 85
Cdd:PRK13537 7 PIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 raQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:PRK13537 80 --QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 166 ALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPLLAAR-CDR 215
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERlCDR 207
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-207 |
2.94e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.00 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 16 VGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLddgssgevsMLGKPLHRMDEearaalraqhvgfvfq 95
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA---------LKGTPVAGCVD---------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 96 sfmlIPTLNALENVelpALLRGASDSESQGDARALLEQLGLG-----KRLhhlPAQLSGGEQQRVALARAFNGRPALLFA 170
Cdd:COG2401 91 ----VPDNQFGREA---SLIDAIGRKGDFKDAVELLNAVGLSdavlwLRR---FKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 496080956 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDP 207
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-205 |
3.08e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.94 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRAQHVGFVFQ---SFMLIPT 102
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpeSQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 103 LnaLENVELPALLRGASDSESQGDARALLEQLGLGKRL-HHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQT 181
Cdd:PRK13649 103 V--LKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180
....*....|....*....|....
gi 496080956 182 GDKIADLLFSLNREhGTTLILVTH 205
Cdd:PRK13649 181 RKELMTLFKKLHQS-GMTIVLVTH 203
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
25-227 |
3.92e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPlhrmdeearAALRAQHVGFVfqsfmliPTLN 104
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV---------SALLELGAGFH-------PELT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPALLRGASDSEsqgdARALLEQL----GLGKRLhHLPAQ-LSGGEQQRVALARAFNGRPALLFADEPTGnldr 179
Cdd:COG1134 105 GRENIYLNGRLLGLSRKE----IDEKFDEIvefaELGDFI-DQPVKtYSSGMRARLAFAVATAVDPDILLVDEVLA---- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496080956 180 qTGD-----KIADLLFSLnREHGTTLILVTHDP-LLAARCDRRLRLVDGQLREE 227
Cdd:COG1134 176 -VGDaafqkKCLARIREL-RESGRTVIFVSHSMgAVRRLCDRAIWLEKGRLVMD 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
25-224 |
4.02e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.42 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMD-EEARaalraQHVGFVFQS----FML 99
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIR-----KKIGIIFQNpdnqFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 100 IpTLNA-----LENVELPAllrgasdSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:PRK13632 99 A-TVEDdiafgLENKKVPP-------KKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496080956 175 GNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-205 |
5.61e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.07 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMdeeARAALRaQHVGFVFQ-------SF 97
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL---SHSVLR-QGVAMVQQdpvvladTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 98 MLIPTL----------NALENVELPALLRGASDsesqgdaralleqlGLGKRLHHLPAQLSGGEQQRVALARAFNGRPAL 167
Cdd:PRK10790 432 LANVTLgrdiseeqvwQALETVQLAELARSLPD--------------GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190
....*....|....*....|....*....|....*...
gi 496080956 168 LFADEPTGNLDRQTGDKIADLLfSLNREHgTTLILVTH 205
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQAL-AAVREH-TTLVVIAH 533
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-206 |
5.61e-18 |
|
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: 81.91 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGQGEHqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGevsmlgkplhrmdeEAR 82
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------------EAR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AALRAQhVGFVFQSFMLIPTLNALENVE-----LPALLR-----GASDSESQGDARALLEQLG-------------LGKR 139
Cdd:TIGR03719 64 PQPGIK-VGYLPQEPQLDPTKTVRENVEegvaeIKDALDrfneiSAKYAEPDADFDKLAAEQAelqeiidaadawdLDSQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 140 LH------HLP------AQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTgdkIADLLFSLNREHGtTLILVTHD 206
Cdd:TIGR03719 143 LEiamdalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPG-TVVAVTHD 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-205 |
1.42e-17 |
|
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: 78.35 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraaLRaQHVGFVFQSFMLIPTlN 104
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW---LR-SQIGLVSQEPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELpallrGASDSESQGDARALleqlglGKRLHH-----LP-----------AQLSGGEQQRVALARAFNGRPALL 168
Cdd:cd03249 93 IAENIRY-----GKPDATDEEVEEAA------KKANIHdfimsLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 496080956 169 FADEPTGNLDRQTGDKIADllfSLNREH-GTTLILVTH 205
Cdd:cd03249 162 LLDEATSALDAESEKLVQE---ALDRAMkGRTTIVIAH 196
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
40-224 |
1.84e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraalRAQHVGFVFQSfmlIPTLNALENVELPALLR--- 116
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA----FARKVAYLPQQ---LPAAEGMTVRELVAIGRypw 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 117 -------GASDSESQGDARALleqLGLGKRLHHLPAQLSGGEQQR--VALARAFNGRPALLfaDEPTGNLDRQTGDKIAD 187
Cdd:PRK10575 114 hgalgrfGAADREKVEEAISL---VGLKPLAHRLVDSLSGGERQRawIAMLVAQDSRCLLL--DEPTSALDIAHQVDVLA 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 496080956 188 LLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:PRK10575 189 LVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEM 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
26-211 |
1.87e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.69 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMD-EEARaalraQHVGFVFQS---FMLIP 101
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVR-----KFVGLVFQNpddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 TLNalENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQT 181
Cdd:PRK13652 95 TVE--QDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190
....*....|....*....|....*....|
gi 496080956 182 GDKIADLLFSLNREHGTTLILVTHDPLLAA 211
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVP 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-222 |
1.98e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGqGEHQLSiltGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAR 82
Cdd:PRK09700 2 ATPYISMAGIGKSFG-PVHALK---SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AALraqHVGFVFQSFMLIPTLNALENVELPALLRG-------ASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRV 155
Cdd:PRK09700 78 AQL---GIGIIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 156 ALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD-PLLAARCDRRLRLVDG 222
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-206 |
2.78e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 78.27 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAR 82
Cdd:PRK11831 4 VANLVDMRGVSFTRGN----RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 83 AALRaQHVGFVFQSFMLIPTLNALENVELPalLRgasdSESQGDARAL-------LEQLGLGKRLHHLPAQLSGGEQQRV 155
Cdd:PRK11831 80 YTVR-KRMSMLFQSGALFTDMNVFDNVAYP--LR----EHTQLPAPLLhstvmmkLEAVGLRGAAKLMPSELSGGMARRA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 156 ALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-205 |
3.78e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRAQHVGFVFQ---SFMLIPT 102
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpeSQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 103 LnaLENVELPALLRGASDSESQGDARALLEQLGLGKRL-HHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQT 181
Cdd:PRK13643 102 V--LKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180
....*....|....*....|....
gi 496080956 182 GDKIADLLFSLNrEHGTTLILVTH 205
Cdd:PRK13643 180 RIEMMQLFESIH-QSGQTVVLVTH 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-207 |
4.41e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 24 SILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSsgevSMLGKPLHRMDEEARAALRaqHVGFVFQSFMLIPTL 103
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN----NFTGTILANNRKPTKQILK--RTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 NALENVELPALLR---GASDSESQGDARALLEQLGLGKRLHHLPAQ-----LSGGEQQRVALARAFNGRPALLFADEPTG 175
Cdd:PLN03211 156 TVRETLVFCSLLRlpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190
....*....|....*....|....*....|..
gi 496080956 176 NLDRQTGDKIADLLFSLNREhGTTLILVTHDP 207
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQK-GKTIVTSMHQP 266
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-215 |
5.18e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.33 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPlhrmdEEARAALRAQHVGFVFQSFMLIPTLN 104
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP-----VPARARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDK 184
Cdd:PRK13536 131 VRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190
....*....|....*....|....*....|..
gi 496080956 185 IADLLFSLnREHGTTLILVTHDPLLAAR-CDR 215
Cdd:PRK13536 211 IWERLRSL-LARGKTILLTTHFMEEAERlCDR 241
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-207 |
6.99e-17 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 75.74 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS--SGEVSMLGKPLhrmDEEARaalraQHVGFVFQSFMLIPT 102
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL---DKNFQ-----RSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 103 LNALENVELPALLRGasdsesqgdaralleqlglgkrlhhlpaqLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTG 182
Cdd:cd03232 94 LTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|....*
gi 496080956 183 DKIADLLFSLnREHGTTLILVTHDP 207
Cdd:cd03232 145 YNIVRFLKKL-ADSGQAILCTIHQP 168
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
24-225 |
7.40e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 7.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 24 SILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeARAAlrAQHVGFVFQSFMLIPTL 103
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS--ARAA--SRRVASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 NALENVEL---PALLR-GASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLD- 178
Cdd:PRK09536 93 DVRQVVEMgrtPHRSRfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDi 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 179 ---RQTGDKIADLLfslnrEHGTTLILVTHDPLLAAR-CDRRLRLVDGQLR 225
Cdd:PRK09536 173 nhqVRTLELVRRLV-----DDGKTAVAAIHDLDLAARyCDELVLLADGRVR 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-224 |
8.63e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.35 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 21 HQLSILTG-VELVVKPRQTIALIGESGSGKSTLLAILAGLDDgSSGEVSMLGKPLHRMDEEA-RaalraQHVGFVFQSFM 98
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESwR-----KHLSWVGQNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 99 LI-PTLnaLENVelpaLLRGASDSESQgdARALLEQLGLGKRLHHLP-----------AQLSGGEQQRVALARAFNGRPA 166
Cdd:PRK11174 434 LPhGTL--RDNV----LLGNPDASDEQ--LQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 167 LLFADEPTGNLDRQTGDKIadlLFSLNRE-HGTTLILVTH--DPLlaARCDRRLRLVDGQL 224
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLV---MQALNAAsRRQTTLMVTHqlEDL--AQWDQIWVMQDGQI 561
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-227 |
1.40e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.56 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkpLHRMDEEARAALRaQHVGFVFQS----FMLIP 101
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIR-KLVGIVFQNpetqFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 TLNAL----ENVELPAL-LRGASDsesqgdaRALLEqLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGN 176
Cdd:PRK13644 95 VEEDLafgpENLCLPPIeIRKRVD-------RALAE-IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 177 LDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
37-227 |
1.46e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 37 QTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMD-EEARaalraQHVGFVFQ--------SFMLIPTLNALE 107
Cdd:PRK13648 36 QWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLR-----KHIGIVFQnpdnqfvgSIVKYDVAFGLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 108 NVELPAllrgasdSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIAD 187
Cdd:PRK13648 111 NHAVPY-------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 188 LLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-227 |
1.96e-16 |
|
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: 75.34 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 15 SVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkplHRMDEEARAALRAQhVGFVF 94
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG---HDVRDYTLASLRRQ-IGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 95 QSFMLIPTlNALENVELPAllRGASDSESQGDARA-----LLEQL--GLGKRLHHLPAQLSGGEQQRVALARAFNGRPAL 167
Cdd:cd03251 83 QDVFLFND-TVAENIAYGR--PGATREEVEEAARAanaheFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 168 LFADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVER 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-227 |
2.05e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 29 VELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkpLHRMDEEARAALRaQHVGFVFQS--FMLIPTLnAL 106
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIR-NKAGMVFQNpdNQIVATI-VE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 107 ENVEL-PALLrGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKI 185
Cdd:PRK13633 105 EDVAFgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496080956 186 ADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:PRK13633 184 VNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-226 |
2.11e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.45 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraaLRaQHVGFVFQSFMLIpTLN 104
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY---LH-RQVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPalLRGASDSESQGDARAL--------LEQlGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGN 176
Cdd:TIGR00958 571 VRENIAYG--LTDTPDEEIMAAAKAAnahdfimeFPN-GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496080956 177 LDRQtgdkIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLRE 226
Cdd:TIGR00958 648 LDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-206 |
2.32e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 33 VKPRQTIALIGESGSGKSTLLAILAGLDDGSsGEVSMLGKPLhrmdEEARAALRAQHVGFVFQSFM---LIPTLNALEnV 109
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPL----EAWSAAELARHRAYLSQQQTppfAMPVFQYLT-L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 110 ELPAllrGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAF-------NGRPALLFADEPTGNLDrQTG 182
Cdd:PRK03695 93 HQPD---KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpdiNPAGQLLLLDEPMNSLD-VAQ 168
|
170 180
....*....|....*....|....
gi 496080956 183 DKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHD 192
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-227 |
2.75e-16 |
|
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: 74.83 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkplHRMDEEARAALRAQhVGFVFQSFMLIpTLN 104
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLRRQ-VGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVEL--PAL-LRGASDSESQGDARALLEQL--GLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDR 179
Cdd:cd03252 92 IRDNIALadPGMsMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496080956 180 QTGDKIADLLFSLNRehGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:cd03252 172 ESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-178 |
2.89e-16 |
|
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: 74.89 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHR--MDEEARAA 84
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 85 LraqhvGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGR 164
Cdd:cd03218 77 I-----GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170
....*....|....
gi 496080956 165 PALLFADEPTGNLD 178
Cdd:cd03218 152 PKFLLLDEPFAGVD 165
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-223 |
3.61e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLH----RMDEEAraalraqHVGFVFQSFMLIP 101
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQEA-------GIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 TLNALENVEL---PALLRGASD-SESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNL 177
Cdd:PRK10762 93 QLTIAENIFLgreFVNRFGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 178 -DRQTgdkiaDLLFSLNRE---HGTTLILVTHdpllaaR-------CDRRLRLVDGQ 223
Cdd:PRK10762 173 tDTET-----ESLFRVIRElksQGRGIVYISH------RlkeifeiCDDVTVFRDGQ 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-206 |
4.09e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.07 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSS-----GEVSMLGKPLHrmdeEARA---ALRAQhVGFVFQS 96
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIY----ERRVnlnRLRRQ-VSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 97 FMLIPtLNALENVELPALLRGASDS-------ESQGDARALLEQLGlgKRLHHLPAQLSGGEQQRVALARAFNGRPALLF 169
Cdd:PRK14258 97 PNLFP-MSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDEIK--HKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 496080956 170 ADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-217 |
4.38e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 35 PRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRaQHVGFVFQS--FMLIPTLNALENVELP 112
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLDPRQTVGDSIMEP 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 113 ALLRGASDSESQGDARA-LLEQLGLgkRLHH---LPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADL 188
Cdd:PRK10261 428 LRVHGLLPGKAAAARVAwLLERVGL--LPEHawrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINL 505
|
170 180
....*....|....*....|....*....
gi 496080956 189 LFSLNREHGTTLILVTHDPLLAARCDRRL 217
Cdd:PRK10261 506 LLDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-227 |
4.55e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.21 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 2 PAENILEVHHLkkSVGQGehqlsiLTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeA 81
Cdd:COG1129 252 PGEVVLEVEGL--SVGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS--P 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 82 RAALRAqhvGFVF-----QSFMLIPTLNALENVELPALLRGA-----SDSESQGDARALLEQLGL-GKRLHHLPAQLSGG 150
Cdd:COG1129 322 RDAIRA---GIAYvpedrKGEGLVLDLSIRENITLASLDRLSrggllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 151 EQQRVALARAFNGRPALLFADEPTGNLDrqTGDK--IADLLFSLNREhGTTLILVTHD-PLLAARCDRRLRLVDGQLREE 227
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGID--VGAKaeIYRLIRELAAE-GKAVIVISSElPELLGLSDRILVMREGRIVGE 475
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
25-226 |
5.96e-16 |
|
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: 73.68 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeaRAALRaQHVGFVFQsfmlIPTL- 103
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR-SRISIIPQ----DPVLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 --------------------NALENVELpallrgasdsesqgdaRALLEQL--GLGKRLHHLPAQLSGGEQQRVALARAF 161
Cdd:cd03244 91 sgtirsnldpfgeysdeelwQALERVGL----------------KEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 162 NGRPALLFADEPTGNLDRQTGDKIADLLfslnREH--GTTLILVTH--DPLLAarCDRRLRLVDGQLRE 226
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTI----REAfkDCTVLTIAHrlDTIID--SDRILVLDKGRVVE 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-178 |
6.92e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.30 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 19 GEHQLSILTGVelvvkPRQTI-ALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRAQHVGFVFQSF 97
Cdd:PRK11144 11 GDLCLTVNLTL-----PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 98 MLIPTLNALENvelpaLLRGASDSeSQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNL 177
Cdd:PRK11144 86 RLFPHYKVRGN-----LRYGMAKS-MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
.
gi 496080956 178 D 178
Cdd:PRK11144 160 D 160
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-224 |
8.22e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.89 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLkkSVGQGEHqlSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMdeEARAAl 85
Cdd:PRK11231 2 TLRTENL--TVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML--SSRQL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 rAQHVGFVFQSFMLIPTLNALENVEL---PAL-LRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAF 161
Cdd:PRK11231 75 -ARRLALLPQHHLTPEGITVRELVAYgrsPWLsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496080956 162 NGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRyCDHLVVLANGHV 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-206 |
9.96e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.54 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 1 MPAENILEVHHLKKSVGQGEHqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGevsmlgkplhrmdeE 80
Cdd:PRK11819 1 MMAQYIYTMNRVSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG--------------E 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 ARAALRAQhVGFVFQSFMLIPTLNALENVE-----LPALLR-----GASDSESQGDARALLEQLG-------------LG 137
Cdd:PRK11819 64 ARPAPGIK-VGYLPQEPQLDPEKTVRENVEegvaeVKAALDrfneiYAAYAEPDADFDALAAEQGelqeiidaadawdLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 138 KRLH------HLP------AQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTgdkIADLLFSLNREHGtTLILVTH 205
Cdd:PRK11819 143 SQLEiamdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPG-TVVAVTH 218
|
.
gi 496080956 206 D 206
Cdd:PRK11819 219 D 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-212 |
1.01e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.66 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDD-----GSSGEVSMLGKPLHRMDEEARAALRaqHVGFVFQSFMLI 100
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDPVEVRR--RIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 101 PTlNALENVELPALLRGAsdsesQGDARALLE----QLGL----GKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADE 172
Cdd:PRK14243 104 PK-SIYDNIAYGARINGY-----KGDMDELVErslrQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496080956 173 PTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPLLAAR 212
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAAR 215
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-205 |
1.14e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGL-DDGS-SGEVSMLGKPLHRMDeearaaLRA-QHVGFVF--QSFMLI 100
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyPHGSyEGEILFDGEVCRFKD------IRDsEALGIVIihQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 101 PTLNALENVEL---PAlLRGASD-SESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGN 176
Cdd:NF040905 91 PYLSIAENIFLgneRA-KRGVIDwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180
....*....|....*....|....*....
gi 496080956 177 LDRQTGDKIADLLFSLnREHGTTLILVTH 205
Cdd:NF040905 170 LNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-224 |
1.34e-15 |
|
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: 72.89 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraaLRAQhVGFVFQSfmliPTLN 104
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY---LHSK-VSLVGQE----PVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 A----------LENVELPALLRGASDSESQGDARALleQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:cd03248 101 ArslqdniaygLQSCSFECVKEAAQKAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496080956 175 GNLDRQTGDKIADLLFSLNREHgtTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:cd03248 179 SALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-205 |
2.09e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeeARAALRAQhVGFVFQSFMLIPTLNA 105
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS--TTAALAAG-VAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 LENV---ELPALLRGASDSESQGDARALLEQLGL----GKRLHHlpaqLSGGEQQRVALARAFnGRPALLFA-DEPTGNL 177
Cdd:PRK11288 97 AENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVdidpDTPLKY----LSIGQRQMVEIAKAL-ARNARVIAfDEPTSSL 171
|
170 180 190
....*....|....*....|....*....|..
gi 496080956 178 D-RQTgdkiaDLLFSLNRE---HGTTLILVTH 205
Cdd:PRK11288 172 SaREI-----EQLFRVIRElraEGRVILYVSH 198
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-221 |
2.10e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.50 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEvSMLGK-----PLHRMDEEARaaLRaQHVGFVFQsfmlI 100
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDyaipaNLKKIKEVKR--LR-KEIGLVFQ----F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 101 PTLNALE-----NVELPALLRGASDSESQGDARALLEQLGLGKR-LHHLPAQLSGGEQQRVALAR--AFNGRPALLfaDE 172
Cdd:PRK13645 99 PEYQLFQetiekDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGiiAMDGNTLVL--DE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496080956 173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDpllaarCDRRLRLVD 221
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHN------MDQVLRIAD 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
35-206 |
2.58e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 35 PRQTIA-LIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRmdeearaALRAQHVGFVFQSFML---IPTLnaLENVE 110
Cdd:PRK15056 31 PGGSIAaLVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQSEEVdwsFPVL--VEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 111 LPA------LLRGASdSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDK 184
Cdd:PRK15056 102 MMGryghmgWLRRAK-KRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180
....*....|....*....|..
gi 496080956 185 IADLLFSLnREHGTTLILVTHD 206
Cdd:PRK15056 181 IISLLREL-RDEGKTMLVSTHN 201
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-225 |
2.93e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 74.28 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 33 VKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARaalraQHVGFVFQSFMLIPTLNALENVELP 112
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVH-----QNMGYCPQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 113 ALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSL 192
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170 180 190
....*....|....*....|....*....|....
gi 496080956 193 NREhGTTLILVTHD-PLLAARCDRRLRLVDGQLR 225
Cdd:TIGR01257 2117 IRE-GRAVVLTSHSmEECEALCTRLAIMVKGAFQ 2149
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-177 |
4.98e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMdeearAAL 85
Cdd:PRK15439 11 LLCARSISKQYSGVE----VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-----TPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RAQHVG--FVFQSFMLIPTLNALENVelpaLLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNG 163
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170
....*....|....
gi 496080956 164 RPALLFADEPTGNL 177
Cdd:PRK15439 158 DSRILILDEPTASL 171
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-211 |
5.32e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 73.32 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMdeeARAALRAqHVGFVFQSFMLiptLN 104
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV---TQASLRA-AIGIVPQDTVL---FN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 A--LENVelpALLR-GASDSESQGDARAlleqlglgKRLH----HLPAQ-----------LSGGEQQRVALARAFNGRPA 166
Cdd:COG5265 446 DtiAYNI---AYGRpDASEEEVEAAARA--------AQIHdfieSLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 167 LLFADEPTGNLDRQTGDKIADLLFSLNREHgTTL--------------ILV----------THDPLLAA 211
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGR-TTLviahrlstivdadeILVleagrivergTHAELLAQ 582
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
6-224 |
5.50e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGehqlSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS--------SGEVSMLGKPLHRM 77
Cdd:PRK13547 1 MLTADHLHVARRHR----AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 78 DEEARAALRA-----QHVGFVFqsfmliptlNALENVEL---PALLRGASDSESQGD-ARALLEQLGLGKRLHHLPAQLS 148
Cdd:PRK13547 77 DAPRLARLRAvlpqaAQPAFAF---------SAREIVLLgryPHARRAGALTHRDGEiAWQALALAGATALVGRDVTTLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 149 GGEQQRVALARAF---------NGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLR 218
Cdd:PRK13547 148 GGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAM 227
|
....*.
gi 496080956 219 LVDGQL 224
Cdd:PRK13547 228 LADGAI 233
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-219 |
6.23e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 22 QLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVsmlgkplhrmdeEARAALRaqhVGFVFQSFMLIP 101
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR---IGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 TLNAleNVELPALLRGASDSesqGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQT 181
Cdd:PRK09544 81 TLPL--TVNRFLRLRPGTKK---EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 496080956 182 GDKIADLLFSLNREHGTTLILVTHD-PLLAARCDRRLRL 219
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDlHLVMAKTDEVLCL 194
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
40-228 |
7.01e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.25 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 40 ALIGESGSGKSTLL-AILAGLDDG---SSGEVSMLGKPLHRMDEEARAALRAQHVGFVFQ--SFMLIPTLNALENVE--L 111
Cdd:COG4170 37 GLVGESGSGKSLIAkAICGITKDNwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQepSSCLDPSAKIGDQLIeaI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 112 PA-LLRG-----ASDSESQgdARALLEQLGLGKRLHHL---PAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTG 182
Cdd:COG4170 117 PSwTFKGkwwqrFKWRKKR--AIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQ 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496080956 183 DKIADLLFSLNREHGTTLILVTHDPL-LAARCDRRLRLVDGQLREEA 228
Cdd:COG4170 195 AQIFRLLARLNQLQGTSILLISHDLEsISQWADTITVLYCGQTVESG 241
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-202 |
7.82e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 72.69 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMdeeARAALRaQHVGFVFQSFMLIPTLNA 105
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLR-RNIAVVFQDAGLFNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 lENVEL--PallrGASDSESQGDARA-------LLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGN 176
Cdd:PRK13657 427 -DNIRVgrP----DATDEEMRAAAERaqahdfiERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180
....*....|....*....|....*.
gi 496080956 177 LDRQTGDKIADLLFSLnREHGTTLIL 202
Cdd:PRK13657 502 LDVETEAKVKAALDEL-MKGRTTFII 526
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-178 |
1.18e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 2 PAENILEVHHLkkSVgQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDeea 81
Cdd:COG3845 253 PGEVVLEVENL--SV-RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS--- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 82 RAALRAQHVGFV---FQSFMLIPTLNALENVEL-----PALLRGA--SDSESQGDARALLEQLGLGKRLHHLPA-QLSGG 150
Cdd:COG3845 327 PRERRRLGVAYIpedRLGRGLVPDMSVAENLILgryrrPPFSRGGflDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGG 406
|
170 180
....*....|....*....|....*...
gi 496080956 151 EQQRVALARAFNGRPALLFADEPTGNLD 178
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-173 |
1.39e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.06 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGK-----PLHRmdee 80
Cdd:COG1137 3 TLEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPMHK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 araalRAQH-VGF------VFQSfmliptLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQ 153
Cdd:COG1137 75 -----RARLgIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERR 143
|
170 180
....*....|....*....|
gi 496080956 154 RVALARAFNGRPALLFADEP 173
Cdd:COG1137 144 RVEIARALATNPKFILLDEP 163
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-205 |
1.71e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.03 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQG-EHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLG-KPLHRMDEEARA 83
Cdd:PRK13631 21 ILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 ALRAQH-----------VGFVFQ--SFMLIPTLNALENVELPALLrGASDSESQGDARALLEQLGLGKR-LHHLPAQLSG 149
Cdd:PRK13631 101 TNPYSKkiknfkelrrrVSMVFQfpEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 150 GEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSlNREHGTTLILVTH 205
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITH 234
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-178 |
2.92e-14 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 69.23 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAAL 85
Cdd:TIGR04406 1 TLVAENLIKSYKKRK----VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 raqHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGD-ARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGR 164
Cdd:TIGR04406 77 ---GIGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREErLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATN 153
|
170
....*....|....
gi 496080956 165 PALLFADEPTGNLD 178
Cdd:TIGR04406 154 PKFILLDEPFAGVD 167
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-228 |
4.05e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 69.74 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVgQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKplhRMDEEARAAL 85
Cdd:PRK13642 4 ILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RaQHVGFVFQSfmliptlnaLENVELPALLRG--ASDSESQGDAR---------ALLEQLGLGKRLHHlPAQLSGGEQQR 154
Cdd:PRK13642 80 R-RKIGMVFQN---------PDNQFVGATVEDdvAFGMENQGIPReemikrvdeALLAVNMLDFKTRE-PARLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496080956 155 VALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLREEA 228
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-214 |
5.62e-14 |
|
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: 68.02 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 40 ALIGESGSGKSTLL-AILAGLddgsSGEVSMLGKPLHRMDEEARAALRAQHVGFVFQSFM-----LIPTLNALENVelpA 113
Cdd:cd03240 26 LIVGQNGAGKTTIIeALKYAL----TGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANgkkytITRSLAILENV---I 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 114 LLRgasdsesQGDARALLEQLglgkrlhhlPAQLSGGEQQ------RVALARAFNGRPALLFADEPTGNLDRQTGD-KIA 186
Cdd:cd03240 99 FCH-------QGESNWPLLDM---------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLA 162
|
170 180
....*....|....*....|....*...
gi 496080956 187 DLLFSLNREHGTTLILVTHDPLLAARCD 214
Cdd:cd03240 163 EIIEERKSQKNFQLIVITHDEELVDAAD 190
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-224 |
7.35e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.57 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 8 EVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEAraalRA 87
Cdd:COG4604 3 EIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE----LA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 88 QHVGFVFQSfmliPTLNALENV-ELPALLR--------GASDSESQGDAralLEQLGL----GKRLHhlpaQLSGGEQQR 154
Cdd:COG4604 75 KRLAILRQE----NHINSRLTVrELVAFGRfpyskgrlTAEDREIIDEA---IAYLDLedlaDRYLD----ELSGGQRQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 155 VALARAFNGRPALLFADEPTGNLD----RQtgdkIADLLFSLNREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDmkhsVQ----MMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRV 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-205 |
1.12e-13 |
|
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: 67.17 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDG--SSGEVSMLGKPLHRMDEEARAA 84
Cdd:cd03217 1 LEIKDLHVSVGGKE----ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 85 LraqHVGFVFQSFMLIPTLNALEnvelpaLLRGasdsesqgdaralleqLGLGkrlhhlpaqLSGGEQQRVALARAFNGR 164
Cdd:cd03217 77 L---GIFLAFQYPPEIPGVKNAD------FLRY----------------VNEG---------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496080956 165 PALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITH 162
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-201 |
1.60e-13 |
|
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: 66.90 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 17 GQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS---SGEVSMLGKPLHRMDEEARAalraqHVGFV 93
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG-----EIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 94 FQSFMLIPTLNALENVELPALLRGasDSESQGdaralleqlglgkrlhhlpaqLSGGEQQRVALARAFNGRPALLFADEP 173
Cdd:cd03233 89 SEEDVHFPTLTVRETLDFALRCKG--NEFVRG---------------------ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180
....*....|....*....|....*...
gi 496080956 174 TGNLDRQTGDKIADLLFSLNREHGTTLI 201
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-223 |
1.97e-13 |
|
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: 66.34 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHQLS-ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKplhrmdeearaal 85
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 raqhVGFVFQSFMLiptLNA--LENVelpalLRGAS-DSEsqgDARALLEQLGLGKRLHHLPAQ-----------LSGGE 151
Cdd:cd03250 68 ----IAYVSQEPWI---QNGtiRENI-----LFGKPfDEE---RYEKVIKACALEPDLEILPDGdlteigekginLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 152 QQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQ 223
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-222 |
3.20e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDG---SSGEVSMLGKPLhrmDEE 80
Cdd:TIGR00956 757 EDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL---DSS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 AraalrAQHVGFVFQSFMLIPTLNALENVELPALLR-GASDSESQGDARA-----LLEQLGLGKRLHHLPAQ-LSGGEQQ 153
Cdd:TIGR00956 834 F-----QRSIGYVQQQDLHLPTSTVRESLRFSAYLRqPKSVSKSEKMEYVeevikLLEMESYADAVVGVPGEgLNVEQRK 908
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 154 RVALARAFNGRPALL-FADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDP--LLAARCDRRLRLVDG 222
Cdd:TIGR00956 909 RLTIGVELVAKPKLLlFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPsaILFEEFDRLLLLQKG 979
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
33-178 |
3.79e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 33 VKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPlhrmdeeARAALRAQHVGFVFQSFMLIPTLNALENVELP 112
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-------ATRGDRSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 113 ALLRGASDSESQGDARALleqLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLD 178
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-226 |
6.69e-13 |
|
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: 67.13 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 29 VELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmDEEARAALRaQHVGFVFQSFMLIPTLNALEN 108
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAYR-QLFSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 109 VELPALlrgasdsesqgdARALLEQLGLGKRLHH-----LPAQLSGGEQQRVALARAF-NGRPALLFaDEPTgnldrqtg 182
Cdd:COG4615 427 EADPAR------------ARELLERLELDHKVSVedgrfSTTDLSQGQRKRLALLVALlEDRPILVF-DEWA-------- 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 183 dkiAD------------LLFSLnREHGTTLILVTHDPLLAARCDRRLRLVDGQLRE 226
Cdd:COG4615 486 ---ADqdpefrrvfyteLLPEL-KARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-226 |
6.70e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 29 VELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmDEEARAALRaQHVGFVFQSFMLiptlnalen 108
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR-KLFSAVFTDFHL--------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 109 veLPALLRGASDSESQGDARALLEQLGLGKRLHH-----LPAQLSGGEQQRVALARAF-NGRPALLFaDEPTGNLDRQTG 182
Cdd:PRK10522 409 --FDQLLGPEGKPANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALaEERDILLL-DEWAADQDPHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496080956 183 DKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLRE 226
Cdd:PRK10522 486 REFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-226 |
7.79e-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: 65.13 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 2 PAENILEVHHLkkSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGK-----PLHR 76
Cdd:cd03369 2 PEHGEIEVENL--SVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 77 MdeeaRAALraqhvGFVFQSfmliPTLnalenveLPALLRGASDSESQGDARALLEQLglgkRLHHLPAQLSGGEQQRVA 156
Cdd:cd03369 80 L----RSSL-----TIIPQD----PTL-------FSGTIRSNLDPFDEYSDEEIYGAL----RVSEGGLNLSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 157 LARAFNGRPALLFADEPTGNLDRQTGDKIADLLfslnREH--GTTLILVTHDPLLAARCDRRLRLVDGQLRE 226
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQKTI----REEftNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
41-228 |
1.17e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.90 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 41 LIGESGSGKSTLLAILAGL---------DDGSSGEVSMLgkplhRMDEEARAALRAQHVGFVFQSfmliPT--LNALENV 109
Cdd:PRK15093 38 LVGESGSGKSLIAKAICGVtkdnwrvtaDRMRFDDIDLL-----RLSPRERRKLVGHNVSMIFQE----PQscLDPSERV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 110 ELpALLRGASDSESQGD-----------ARALLEQLGLGKR---LHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTG 175
Cdd:PRK15093 109 GR-QLMQNIPGWTYKGRwwqrfgwrkrrAIELLHRVGIKDHkdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTN 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496080956 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHD-PLLAARCDRRLRLVDGQLREEA 228
Cdd:PRK15093 188 AMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADKINVLYCGQTVETA 241
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-206 |
2.31e-11 |
|
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: 61.61 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 32 VVKPRQTIALIGESGSGKSTLLAILAGL---------DDGSSGEV------SMLGKPLHRM-DEEARAALRAQHVGfvfq 95
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKlkpnlgkfdDPPDWDEIldefrgSELQNYFTKLlEGDVKVIVKPQYVD---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 96 sfmLIPtlNALE-NVElpALLRGASDSESQGDaraLLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:cd03236 98 ---LIP--KAVKgKVG--ELLKKKDERGKLDE---LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|..
gi 496080956 175 GNLDRQTGDKIADLLFSLNrEHGTTLILVTHD 206
Cdd:cd03236 168 SYLDIKQRLNAARLIRELA-EDDNYVLVVEHD 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-188 |
5.08e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPL----HRMDEEARAAlraqhvgfvfqsFM--- 98
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarHRRAVCPRIA------------YMpqg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 99 ----LIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:NF033858 85 lgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
170
....*....|....*...
gi 496080956 175 GNLD----RQTGDKIADL 188
Cdd:NF033858 165 TGVDplsrRQFWELIDRI 182
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-178 |
5.67e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.79 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmDEEARA--ALRaQHVGFVFQSfmliPT 102
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKRGllALR-QQVATVFQD----PE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 103 LNALE---NVELPALLRGASDSESQgDARALLEQLGL--GKRLHHLPAQ-LSGGEQQRVALARAFNGRPALLFADEPTGN 176
Cdd:PRK13638 88 QQIFYtdiDSDIAFSLRNLGVPEAE-ITRRVDEALTLvdAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
..
gi 496080956 177 LD 178
Cdd:PRK13638 167 LD 168
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
22-224 |
5.84e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 22 QLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmDEEARAALRAQHVGFVFQSFMLIP 101
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQTAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 TLNALENvelpaLLRGASDSESQGDARALLEQLGLGKRLHHLPAQ----LSGGEQQRVALARAFNGRPALLFADEPTGNL 177
Cdd:PRK11614 94 RMTVEEN-----LAMGGFFAERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496080956 178 DRQTGDKIADLLFSLnREHGTTLILVTHDPLLAAR-CDRRLRLVDGQL 224
Cdd:PRK11614 169 APIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHV 215
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-221 |
1.92e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 3 AENILEVHHLKKSVGQgehqLSILTGVELVVKPRQTIALIGESGSG--KSTLLAILAGLDDGSsgevsmlgKPLHRMDEE 80
Cdd:NF000106 10 ARNAVEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGR--------RPWRF*TWC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 81 A-RAALRAQHVGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALAR 159
Cdd:NF000106 78 AnRRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 160 AFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLAARCDRRLRLVD 221
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVID 218
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-205 |
2.17e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 6 ILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDG--SSGEVSMLGKPLHRMDEEARA 83
Cdd:PRK09580 1 MLSIKDLHVSVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 alrAQHVGFVFQ----------SFMLIPTLNALENV-ELPALLRgasdsesqGDARALLEQlglGKRLHHLPAQL----- 147
Cdd:PRK09580 77 ---GEGIFMAFQypveipgvsnQFFLQTALNAVRSYrGQEPLDR--------FDFQDLMEE---KIALLKMPEDLltrsv 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496080956 148 ----SGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205
Cdd:PRK09580 143 nvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-206 |
2.48e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 30 ELVVKPRQTIALIGESGSGKSTLLAILAG---LDDG-----SSGEVSMLGKPLHRMDEEARAALRA---QHVGFVFQSFM 98
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDGriiyeQDLIVARLQQDPPRNVEGTVYDFVAegiEEQAEYLKRYH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 99 LIPTLNALENVE--LPALLRGASDSESQG----DAR--ALLEQLGLG--KRLhhlpAQLSGGEQQRVALARAFNGRPALL 168
Cdd:PRK11147 103 DISHLVETDPSEknLNELAKLQEQLDHHNlwqlENRinEVLAQLGLDpdAAL----SSLSGGWLRKAALGRALVSNPDVL 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 496080956 169 FADEPTGNLDRQTGDKIADLLFSLNrehgTTLILVTHD 206
Cdd:PRK11147 179 LLDEPTNHLDIETIEWLEGFLKTFQ----GSIIFISHD 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-223 |
2.58e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRmdEEARAALRaQHVGFVFQSFMLIPTLNA 105
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--KSSKEALE-NGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 LENVEL---PalLRGASDSESQ--GDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDrq 180
Cdd:PRK10982 91 MDNMWLgryP--TKGMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT-- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496080956 181 tgDKIADLLFSLNR---EHGTTLILVTH--DPLLAArCDRRLRLVDGQ 223
Cdd:PRK10982 167 --EKEVNHLFTIIRklkERGCGIVYISHkmEEIFQL-CDEITILRDGQ 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-213 |
7.51e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGlD--DGSSGEVSMLGKplHRMDEEARAALRaQHVGFVFQSFMLIPT 102
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DhpQGYSNDLTLFGR--RRGSGETIWDIK-KHIGYVSSSLHLDYR 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 103 LNA-LENVELP------ALLRGASDSESQgDARALLEQLGLGKRLHHLPAQ-LSGGeQQRVAL-ARAFNGRPALLFADEP 173
Cdd:PRK10938 351 VSTsVRNVILSgffdsiGIYQAVSDRQQK-LAQQWLDILGIDKRTADAPFHsLSWG-QQRLALiVRALVKHPTLLILDEP 428
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496080956 174 TGNLD---RQTGDKIADLLFSlnrEHGTTLILVTHDPLLAARC 213
Cdd:PRK10938 429 LQGLDplnRQLVRRFVDVLIS---EGETQLLFVSHHAEDAPAC 468
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-226 |
1.06e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.59 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 17 GQGEHQLSiLTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKplhrmdeearAALRAQHVGFVFQs 96
Cdd:PRK13545 32 KDGEYHYA-LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAISSGLNGQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 97 fmliptLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGN 176
Cdd:PRK13545 100 ------LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496080956 177 LDRQTGDKIADLLFSLnREHGTTLILVTHD-PLLAARCDRRLRLVDGQLRE 226
Cdd:PRK13545 174 GDQTFTKKCLDKMNEF-KEQGKTIFFISHSlSQVKSFCTKALWLHYGQVKE 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-219 |
1.08e-09 |
|
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: 55.44 E-value: 1.08e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 146 QLSGGEQQRVALA-----RAFNGRPaLLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPLLAARCDRRLRL 219
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEH-LVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-206 |
1.16e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSG-------EVSMLgkPLHrmdEEARaalraQHVGFVFQSF 97
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddeDISLL--PLH---ARAR-----RGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 98 MLIPTLNALENVELPALLRGASDSESQGD-ARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGN 176
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190
....*....|....*....|....*....|
gi 496080956 177 LDRQTGDKIADLLFSLnREHGTTLILVTHD 206
Cdd:PRK10895 168 VDPISVIDIKRIIEHL-RDSGLGVLITDHN 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
40-212 |
2.61e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.76 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAalraQHVGFVFQSFMLIPTLNALENV------ELPA 113
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDITVQELVargrypHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 114 LLRGASDSEsQGDARALLeqlglGKRLHHLPAQ----LSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLL 189
Cdd:PRK10253 113 FTRWRKEDE-EAVTKAMQ-----ATGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
|
170 180
....*....|....*....|...
gi 496080956 190 FSLNREHGTTLILVTHDPLLAAR 212
Cdd:PRK10253 187 SELNREKGYTLAAVLHDLNQACR 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-178 |
2.81e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 1 MPAEnilevhhlKKSVGQGEHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS--SGEVSMLGKPlHRMD 78
Cdd:PLN03140 879 MPAE--------MKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP-KKQE 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 79 EEARAAlraqhvGFVFQSFMLIPTLNALENVELPALLRGASDSESQGDAR------ALLEQLGLGKRLHHLPA--QLSGG 150
Cdd:PLN03140 950 TFARIS------GYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMfvdevmELVELDNLKDAIVGLPGvtGLSTE 1023
|
170 180
....*....|....*....|....*...
gi 496080956 151 EQQRVALARAFNGRPALLFADEPTGNLD 178
Cdd:PLN03140 1024 QRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-206 |
2.86e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 32 VVKPRQTIALIGESGSGKSTLLAILAGL---------DDGSSGEV------SMLGKPLHRM-DEEARAALRAQHVGfvfq 95
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEVlkrfrgTELQNYFKKLyNGEIKVVHKPQYVD---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 96 sfmLIPtlNALE-NVElpALLRGASDSesqGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFnGRPA-LLFADEP 173
Cdd:PRK13409 171 ---LIP--KVFKgKVR--ELLKKVDER---GKLDEVVERLGLENILDRDISELSGGELQRVAIAAAL-LRDAdFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....
gi 496080956 174 TGNLD-RQTgDKIADLLFSLNREHgtTLILVTHD 206
Cdd:PRK13409 240 TSYLDiRQR-LNVARLIRELAEGK--YVLVVEHD 270
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
41-206 |
4.78e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 41 LIGESGSGKSTLLAILAGLDDGSSGEVSMlgKPLHRMdeearAALRAQHvgFVFQSFMLIPTLnALENVELPALLR---- 116
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSL--DPNERL-----GKLRQDQ--FAFEEFTVLDTV-IMGHTELWEVKQerdr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 117 -------------GASDSESQ--------GDARA--LLEQLGLGKRLHHLP-AQLSGGEQQRVALARAFNGRPALLFADE 172
Cdd:PRK15064 102 iyalpemseedgmKVADLEVKfaemdgytAEARAgeLLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDE 181
|
170 180 190
....*....|....*....|....*....|....
gi 496080956 173 PTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
Cdd:PRK15064 182 PTNNLDINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-226 |
6.73e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKplhrmdeearaalraqhVGFVFQSfMLIPTLNA 105
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------------VAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 LENVelpalLRGASDSESQgdARALLEQLGLGKRLHHLPA-----------QLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:TIGR00957 716 RENI-----LFGKALNEKY--YQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496080956 175 GNLDRQTGDKIAD-LLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLRE 226
Cdd:TIGR00957 789 SAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-206 |
7.00e-09 |
|
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: 55.18 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 32 VVKPRQTIALIGESGSGKSTLLAILAGL---------DDGSSGEV------SMLGKPLHRM-DEEARAALRAQHVGFVFQ 95
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGElkpnlgdydEEPSWDEVlkrfrgTELQDYFKKLaNGEIKVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 96 SFmlipTLNALEnvelpaLLRGASDsesQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFnGRPA-LLFADEPT 174
Cdd:COG1245 175 VF----KGTVRE------LLEKVDE---RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAAL-LRDAdFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|...
gi 496080956 175 GNLD-RQTgDKIADLLFSLNREhGTTLILVTHD 206
Cdd:COG1245 241 SYLDiYQR-LNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-224 |
7.44e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 13 KKSVGQGEHqlSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSmLGKPLhrmdeeaRAALRAQHvgf 92
Cdd:PRK10636 317 KVSAGYGDR--IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG-LAKGI-------KLGYFAQH--- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 93 vfqsfmLIPTLNALENvELPALLRGAsDSESQGDARALLEQLGL-GKRLHHLPAQLSGGEQQRVALARAFNGRPALLFAD 171
Cdd:PRK10636 384 ------QLEFLRADES-PLQHLARLA-PQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496080956 172 EPTGNLDRQTGDKIADLLFSLNrehgTTLILVTHDPLLAARCDRRLRLV-DGQL 224
Cdd:PRK10636 456 EPTNHLDLDMRQALTEALIDFE----GALVVVSHDRHLLRSTTDDLYLVhDGKV 505
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-97 |
1.07e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 5 NILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS--SGEVSMLGKPLHRMDEEAR 82
Cdd:CHL00131 6 PILEIKNLHASVNENE----ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEER 81
|
90
....*....|....*
gi 496080956 83 AalraqHVGfVFQSF 97
Cdd:CHL00131 82 A-----HLG-IFLAF 90
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-206 |
1.07e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 5 NILEVHHLKKSVGQGEhqlsILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVsmlgkplhRMDEEARAA 84
Cdd:PRK15064 318 NALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENANIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 85 LRAQHVGFVFQSFMlipTLnalenVELPALLRGASDSESQgdARALLEQLGLGKRLHHLPAQ-LSGGEQQRVALARAFNG 163
Cdd:PRK15064 386 YYAQDHAYDFENDL---TL-----FDWMSQWRQEGDDEQA--VRGTLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496080956 164 RPALLFADEPTGNLDRQTgdkIADLLFSLNREHGtTLILVTHD 206
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMES---IESLNMALEKYEG-TLIFVSHD 494
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-205 |
1.75e-08 |
|
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: 53.10 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 23 LSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEARAALRAQHVGFVFQSFMLipt 102
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 103 LNAL--ENVELPALL-----RGASDSES-QGDARALL--EQLGLGKRlhhlPAQLSGGEQQRVALARAFNGRPALLFADE 172
Cdd:cd03290 91 LNATveENITFGSPFnkqryKAVTDACSlQPDIDLLPfgDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190
....*....|....*....|....*....|....
gi 496080956 173 PTGNLDRQTGDKI-ADLLFSLNREHGTTLILVTH 205
Cdd:cd03290 167 PFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTH 200
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-223 |
2.32e-08 |
|
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: 52.80 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 11 HLKKSVGQGEHQLSILTGVelvVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVsmlGKPLHRMdeearaALRAQHV 90
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGS---ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTV------SYKPQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 91 GFVFQSfmlipTLNALenveLPALLRGA-SDSESQGDaraLLEQLGLGKRLHHLPAQLSGGEQQRVALArAFNGRPALLF 169
Cdd:cd03237 71 KADYEG-----TVRDL----LSSITKDFyTHPYFKTE---IAKPLQIEQILDREVPELSGGELQRVAIA-ACLSKDADIY 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 170 -ADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQ 223
Cdd:cd03237 138 lLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-178 |
3.01e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.48 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGkplHRMDEEARAALRaQHVGFVFQSFMLIPTLNA 105
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG---HDLRDYTLASLR-NQVALVSQNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 ------------LENVELPALLRGASDSESQgdaralLEQlGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEP 173
Cdd:PRK11176 435 nniayarteqysREQIEEAARMAYAMDFINK------MDN-GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
....*
gi 496080956 174 TGNLD 178
Cdd:PRK11176 508 TSALD 512
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-224 |
3.13e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVsmlgkplhrmdeearaaLRAQHVGFVFQSFMLiptLN 104
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------------WAERSIAYVPQQAWI---MN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 AleNVELPALLRGASDSESQGDA------RALLEQL--GLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGN 176
Cdd:PTZ00243 735 A--TVRGNILFFDEEDAARLADAvrvsqlEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496080956 177 LDRQTGDKIADLLFsLNREHGTTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:PTZ00243 813 LDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-225 |
3.40e-08 |
|
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: 53.29 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 29 VELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS-SGEVSMLGKPLhrmdeEARAALRAQHVGFVF-----QSFMLIPT 102
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV-----DIRNPAQAIRAGIAMvpedrKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 103 LNALENVELPALLRGASdsESQGDARALLEQLGLG-KRLH------HLP-AQLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:TIGR02633 354 LGVGKNITLSVLKSFCF--KMRIDAAAELQIIGSAiQRLKvktaspFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496080956 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHD-PLLAARCDRRLRLVDGQLR 225
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQE-GVAIIVVSSElAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-227 |
3.83e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKKSVGQGEHQLSILTG-----VELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMDEEA 81
Cdd:PRK15439 255 LPGNRRQQAAGAPVLTVEDLTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 82 RAALraqhvGFVF-----QS---FMLIP---TLNALENVELPALLRGASDsesqgdaRALLEQL--GLGKRLHHL--PAQ 146
Cdd:PRK15439 335 RLAR-----GLVYlpedrQSsglYLDAPlawNVCALTHNRRGFWIKPARE-------NAVLERYrrALNIKFNHAeqAAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 147 -LSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHD----PLLAarcDRRLRLVD 221
Cdd:PRK15439 403 tLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDleeiEQMA---DRVLVMHQ 478
|
....*.
gi 496080956 222 GQLREE 227
Cdd:PRK15439 479 GEISGA 484
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
46-227 |
4.60e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 46 GSGKSTLLAILAGLDDGSSGEVSMLGKPLH-RMDEEARAAlraqhvGFVFQSF-----MLIPTLNALENVELPAL----- 114
Cdd:PRK10762 288 GAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLAN------GIVYISEdrkrdGLVLGMSVKENMSLTALryfsr 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 115 ----LRGASDSESQGDARALL--------EQLGLgkrlhhlpaqLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTG 182
Cdd:PRK10762 362 aggsLKHADEQQAVSDFIRLFniktpsmeQAIGL----------LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAK 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496080956 183 DKIADLLFSLNREhGTTLILVTHD-PLLAARCDRRLRLVDGQLREE 227
Cdd:PRK10762 432 KEIYQLINQFKAE-GLSIILVSSEmPEVLGMSDRILVMHEGRISGE 476
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-222 |
6.23e-08 |
|
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: 50.45 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 35 PRQTIALIGESGSGKSTLLAILAGLddgssgevsmlgkplhrmdeearaaLRAQHVGFVFqsfmliptLNAlenvelpal 114
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE-------------------------LGPPGGGVIY--------IDG--------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 115 lrgasdsesqGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKI-----ADLL 189
Cdd:smart00382 39 ----------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLL 108
|
170 180 190
....*....|....*....|....*....|....*....
gi 496080956 190 FSLNREHGTTLILVTHDP------LLAARCDRRLRLVDG 222
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEkdlgpaLLRRRFDRRIVLLLI 147
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
43-227 |
6.87e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 43 GESGSGKSTLLAILAGLDDGSSGEVSMLGKplhrmDEEARAALRA--QHVGFV---------FQSFML---IPTLNALEN 108
Cdd:PRK09700 296 GLVGSGRTELMNCLFGVDKRAGGEIRLNGK-----DISPRSPLDAvkKGMAYItesrrdngfFPNFSIaqnMAISRSLKD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 109 VELPALLRGASDSESQGDARALLEQLGLgkRLHHLP---AQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKI 185
Cdd:PRK09700 371 GGYKGAMGLFHEVDEQRTAENQRELLAL--KCHSVNqniTELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEI 448
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496080956 186 ADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:PRK09700 449 YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-206 |
8.10e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSmLGKPLhrmdEEA-----RAALRaqhvgfvfqsfmliPTLNALENVElpa 113
Cdd:PRK11147 348 IALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKL----EVAyfdqhRAELD--------------PEKTVMDNLA--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 114 llRGASDSESQGDARALL----EQLGLGKRLHHLPAQLSGGEQQRVALARAFNgRPA-LLFADEPTGNLDRQTgdkiADL 188
Cdd:PRK11147 406 --EGKQEVMVNGRPRHVLgylqDFLFHPKRAMTPVKALSGGERNRLLLARLFL-KPSnLLILDEPTNDLDVET----LEL 478
|
170
....*....|....*...
gi 496080956 189 LFSLNREHGTTLILVTHD 206
Cdd:PRK11147 479 LEELLDSYQGTVLLVSHD 496
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-227 |
1.48e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLLAilaglddgssgevSMLGKPLHRmdEEARAALRAqhvgfvfqSFMLIPTLNA 105
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLIS-------------AMLGELSHA--ETSSVVIRG--------SVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 106 LENVELPALLRGASDSESQG-----DARALLEQLGL--GKRLHHLPAQ---LSGGEQQRVALARAFNGRPALLFADEPTG 175
Cdd:PLN03232 690 IFNATVRENILFGSDFESERywraiDVTALQHDLDLlpGRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496080956 176 NLDRQTGDKIADllfSLNRE--HGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:PLN03232 770 ALDAHVAHQVFD---SCMKDelKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
46-225 |
1.53e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 46 GSGKSTLLAILAGLDDG-SSGEVSMLGKPLhrmdeEARAALRAQHVGFVF-----QSFMLIPTLNALENVELPALLRGAS 119
Cdd:PRK13549 298 GAGRTELVQCLFGAYPGrWEGEIFIDGKPV-----KIRNPQQAIAQGIAMvpedrKRDGIVPVMGVGKNITLAALDRFTG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 120 -----DSESQGDARALLEQLGLGKRLHHLP-AQLSGGEQQRVALARAFNGRPALLFADEPTGNLDrqTGDK--IADLLFS 191
Cdd:PRK13549 373 gsridDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID--VGAKyeIYKLINQ 450
|
170 180 190
....*....|....*....|....*....|....*
gi 496080956 192 LNREhGTTLILVTHD-PLLAARCDRRLRLVDGQLR 225
Cdd:PRK13549 451 LVQQ-GVAIIVISSElPEVLGLSDRVLVMHEGKLK 484
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-206 |
2.97e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 39 IALIGESGSGKSTLLAILAGLDDGSSGEVsmlgkplhrmDEEARAALRAQHVGFVFQsfmliptlnalENVElpALLRGA 118
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEV----------DEDLKISYKPQYISPDYD-----------GTVE--EFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 119 -----SDSESQGDaraLLEQLGLGKRLHHLPAQLSGGEQQRVALARAFnGRPALLFA-DEPTGNLDRQTGDKIADLLFSL 192
Cdd:COG1245 426 ntddfGSSYYKTE---IIKPLGLEKLLDKNVKDLSGGELQRVAIAACL-SRDADLYLlDEPSAHLDVEQRLAVAKAIRRF 501
|
170
....*....|....
gi 496080956 193 NREHGTTLILVTHD 206
Cdd:COG1245 502 AENRGKTAMVVDHD 515
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
28-206 |
3.11e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 49.24 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 28 GVELVVKPRQTIALIGESGSGKSTLL-AILAGLDDGSSGEVSMLGKPLHRMDEEARAALRAQHVGFV---------FQSF 97
Cdd:COG0419 15 DTETIDFDDGLNLIVGPNGAGKSTILeAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRyrierrqgeFAEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 98 MLIPT------------LNALENVE--LPALLRGASDSESQGDARALLEQLGLgKRLHHL--PAQLSGGEQQRVALARAF 161
Cdd:COG0419 95 LEAKPserkealkrllgLEIYEELKerLKELEEALESALEELAELQKLKQEIL-AQLSGLdpIETLSGGERLRLALADLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496080956 162 NgrpalLFADepTGNLDRQTGDKIADLLFSLNrehgttliLVTHD 206
Cdd:COG0419 174 S-----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-206 |
4.11e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 33 VKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGK-PLHRMDEEArAALRAQHVGFVF-------QSFMLIPTLN 104
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQET-PALPQPALEYVIdgdreyrQLEAQLHDAN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 ALENVELPALLRGASDS----ESQGDARALLEQLGLGK-RLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDR 179
Cdd:PRK10636 103 ERNDGHAIATIHGKLDAidawTIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
170 180
....*....|....*....|....*..
gi 496080956 180 qtgDKIADLLFSLNREHGtTLILVTHD 206
Cdd:PRK10636 183 ---DAVIWLEKWLKSYQG-TLILISHD 205
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-205 |
4.72e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.71 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 20 EHQLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLH--RMDE-EARAALRAQhVGFVFQS 96
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSwRSRLAVVSQ-TPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 97 fmLIPTLNAL-------ENVELPALLRGASDsesqgDARALLE--QLGLGKRlhhlPAQLSGGEQQRVALARAFNGRPAL 167
Cdd:PRK10789 404 --TVANNIALgrpdatqQEIEHVARLASVHD-----DILRLPQgyDTEVGER----GVMLSGGQKQRISIARALLLNAEI 472
|
170 180 190
....*....|....*....|....*....|....*....
gi 496080956 168 LFADEPTGNLDRQTGDKIadlLFSLNR-EHGTTLILVTH 205
Cdd:PRK10789 473 LILDDALSAVDGRTEHQI---LHNLRQwGEGRTVIISAH 508
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
41-214 |
5.96e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 41 LIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmdEEARAALRAQhVGFVFQSFMLIPTLNALENVelpalLRGASD 120
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQ-LCFVGHRSGINPYLTLRENC-----LYDIHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 121 SESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLfSLNREHGTTL 200
Cdd:PRK13540 102 SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI-QEHRAKGGAV 180
|
170
....*....|....
gi 496080956 201 ILVTHDPLLAARCD 214
Cdd:PRK13540 181 LLTSHQDLPLNKAD 194
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
41-209 |
7.00e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.36 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 41 LIGESGSGKSTLLAILAGLDDGSSGevsMLGKPlhrmdeearaalRAQHVGFVFQS-FMLIPTLNalENVELP-----AL 114
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGELWPVYGG---RLTKP------------AKGKLFYVPQRpYMTLGTLR--DQIIYPdssedMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 115 LRGASDSEsqgdaralLEQLGLGKRLHHLPAQ-------------LSGGEQQRVALARAFNGRPALLFADEPTGNLDRQT 181
Cdd:TIGR00954 546 RRGLSDKD--------LEQILDNVQLTHILEReggwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180
....*....|....*....|....*...
gi 496080956 182 GDKIadllFSLNREHGTTLILVTHDPLL 209
Cdd:TIGR00954 618 EGYM----YRLCREFGITLFSVSHRKSL 641
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
147-207 |
7.86e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.41 E-value: 7.86e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 147 LSGGEQQRVALARAFN-GRPALLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDP 207
Cdd:cd03270 138 LSGGEAQRIRLATQIGsGLTGVLYVlDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-181 |
9.96e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS----SGEVSMLGKPLHRMDEEARAalraqHVGFVFQSFMLI 100
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKKHYRG-----DVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 101 PTLNALENVELPALLRGAS------DSESQGDARALLEQLGLGkrLHH---------LPAQLSGGEQQRVALARAFNGRP 165
Cdd:TIGR00956 151 PHLTVGETLDFAARCKTPQnrpdgvSREEYAKHIADVYMATYG--LSHtrntkvgndFVRGVSGGERKRVSIAEASLGGA 228
|
170
....*....|....*.
gi 496080956 166 ALLFADEPTGNLDRQT 181
Cdd:TIGR00956 229 KIQCWDNATRGLDSAT 244
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-215 |
1.20e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 129 ALLEQLGLGK-RLHHLPAQLSGGEQQRVALARAFNGRpalLFA-----DEPTGNLDRQTGDKIADLLFSLnREHGTTLIL 202
Cdd:PRK00635 458 SILIDLGLPYlTPERALATLSGGEQERTALAKHLGAE---LIGityilDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLL 533
|
90
....*....|...
gi 496080956 203 VTHDPLLAARCDR 215
Cdd:PRK00635 534 VEHDEQMISLADR 546
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-181 |
2.05e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.01 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 4 ENILEVHHLKKSVGqgeHQLSIlTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSmLGKPLHrmdeeara 83
Cdd:TIGR03719 320 DKVIEAENLTKAFG---DKLLI-DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETVK-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 84 alraqhVGFVFQSF-MLIPTLNALENVElpallrGASDSESQGD----ARALLEQLGL-GKRLHHLPAQLSGGEQQRVAL 157
Cdd:TIGR03719 387 ------LAYVDQSRdALDPNKTVWEEIS------GGLDIIKLGKreipSRAYVGRFNFkGSDQQKKVGQLSGGERNRVHL 454
|
170 180
....*....|....*....|....
gi 496080956 158 ARAFNGRPALLFADEPTGNLDRQT 181
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
7-215 |
2.97e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 7 LEVHHLKK-SVGQGEHQLSILTGVelvvkprqtialigeSGSGKSTLLaiLAGLDdgssgevsmlgKPLHRMDEEARAAL 85
Cdd:cd03238 6 ANVHNLQNlDVSIPLNVLVVVTGV---------------SGSGKSTLV--NEGLY-----------ASGKARLISFLPKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 86 RAQHVGFVFQsfmliptLNALENVELpallrgasdsesqgdarallEQLGLGKRLhhlpAQLSGGEQQRVALARAFNGRP 165
Cdd:cd03238 58 SRNKLIFIDQ-------LQFLIDVGL--------------------GYLTLGQKL----STLSGGELQRVKLASELFSEP 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496080956 166 --ALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPLLAARCDR 215
Cdd:cd03238 107 pgTLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSSADW 157
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-226 |
3.81e-06 |
|
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: 46.39 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 24 SILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDgSSGEVSMLGKPLHRMD-EEARAALraqhvGFVFQSFMLipt 102
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPlQKWRKAF-----GVIPQKVFI--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 103 lnalenveLPALLRGASDSESQGDARALL---EQLGLGKRLHHLPAQL-----------SGGEQQRVALARAFNGRPALL 168
Cdd:cd03289 89 --------FSGTFRKNLDPYGKWSDEEIWkvaEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 169 FADEPTGNLDRQTGDKIADLL---FSlnrehGTTLILVTH--DPLLaaRCDRRLRLVDGQLRE 226
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLkqaFA-----DCTVILSEHriEAML--ECQRFLVIEENKVRQ 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
36-215 |
4.00e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 36 RQTIALIGESGSGKSTLLAILAGLDDGSSGEVsMLGKPLHRMD---EEARAALRAQHVGF-------------------V 93
Cdd:PTZ00265 1194 KKTTAIVGETGSGKSTVMSLLMRFYDLKNDHH-IVFKNEHTNDmtnEQDYQGDEEQNVGMknvnefsltkeggsgedstV 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 94 FQS----------------------FMLIPTLNALENVELPALLRGASDSESQGDARALLEQLGLGKRLHHLPAQ----- 146
Cdd:PTZ00265 1273 FKNsgkilldgvdicdynlkdlrnlFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKydtnv 1352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496080956 147 ------LSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDR 215
Cdd:PTZ00265 1353 gpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDK 1427
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-206 |
7.69e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKplhrmdeeARAALRAQHV--GFVFQSFMLIPTLNALENVELPALlr 116
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK--------VRMAVFSQHHvdGLDLSSNPLLYMMRCFPGVPEQKL-- 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 117 gasdsesqgdaRALLEQLGLGKRLHHLPA-QLSGGEQQRVALARAFNGRPALLFADEPTGNLDRqtgDKIADLLFSLNRE 195
Cdd:PLN03073 608 -----------RAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL---DAVEALIQGLVLF 673
|
170
....*....|.
gi 496080956 196 HGTTLiLVTHD 206
Cdd:PLN03073 674 QGGVL-MVSHD 683
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
147-223 |
9.57e-06 |
|
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: 44.49 E-value: 9.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 147 LSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQ 223
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-206 |
9.83e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 39 IALIGESGSGKSTLLAILAGLDDGSSGEVsmlgkplhrmDEEARAALRAQHVGfvfqsfmliptlnALENVELPALLRGA 118
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEV----------DPELKISYKPQYIK-------------PDYDGTVEDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 119 SD--------SEsqgdaraLLEQLGLGKRLHHLPAQLSGGEQQRVALARAFnGRPALLFA-DEPTGNLDRQTGDKIADLL 189
Cdd:PRK13409 425 TDdlgssyykSE-------IIKPLQLERLLDKNVKDLSGGELQRVAIAACL-SRDADLYLlDEPSAHLDVEQRLAVAKAI 496
|
170
....*....|....*..
gi 496080956 190 FSLNREHGTTLILVTHD 206
Cdd:PRK13409 497 RRIAEEREATALVVDHD 513
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
130-203 |
9.94e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 9.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496080956 130 LLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILV 203
Cdd:PRK10938 119 LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-209 |
2.17e-05 |
|
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: 44.90 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 24 SILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDgSSGEVSMLGKPLHRMD-EEARAALraqhvGFVFQS-FMLIP 101
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTlQTWRKAF-----GVIPQKvFIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 TLNalENVELPALLrgaSDSESQGDArallEQLGLGKRLHHLPAQ-----------LSGGEQQRVALARAFNGRPALLFA 170
Cdd:TIGR01271 1307 TFR--KNLDPYEQW---SDEEIWKVA----EEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496080956 171 DEPTGNLDRQTGDKIADLL---FSlnrehGTTLILVTH--DPLL 209
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLkqsFS-----NCTVILSEHrvEALL 1416
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-205 |
3.75e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 23 LSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMlgKPLHRMDEEARAALRAQhVGFVFQSFMLIP- 101
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSK-IGVVSQDPLLFSn 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 102 --------TLNALENVELPA--LLRGASDSESQGDARALLEQLGLG---------------------------------- 137
Cdd:PTZ00265 475 siknnikySLYSLKDLEALSnyYNEDGNDSQENKNKRNSCRAKCAGdlndmsnttdsneliemrknyqtikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 138 KRLHH-----LP-----------AQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLI 201
Cdd:PTZ00265 555 KVLIHdfvsaLPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
....
gi 496080956 202 LVTH 205
Cdd:PTZ00265 635 IIAH 638
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
39-206 |
4.42e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSmlgkplhRMDEEARAALRAQHVGfvfqsfmlipTLNALENVELPALLRGA 118
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKVD-------RNGEVSVIAISAGLSG----------QLTGIENIEFKMLCMGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 119 SDSESQGDARALLEQLGLGKRLHHLPAQLSGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLnREHGT 198
Cdd:PRK13546 116 KRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNK 194
|
....*...
gi 496080956 199 TLILVTHD 206
Cdd:PRK13546 195 TIFFVSHN 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-180 |
4.48e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 25 ILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLhrmdeeARAALRAqhvgfVFQSFMLIPTLN 104
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI------GAYGLRE-----LRRQFSMIPQDP 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 105 AL------ENVElPAL---------------LRGASDSESQG-DARALleQLGLgkrlhhlpaQLSGGEQQRVALARAFN 162
Cdd:PTZ00243 1394 VLfdgtvrQNVD-PFLeassaevwaalelvgLRERVASESEGiDSRVL--EGGS---------NYSVGQRQLMCMARALL 1461
|
170 180
....*....|....*....|...
gi 496080956 163 GR-PALLFADEPTGN----LDRQ 180
Cdd:PTZ00243 1462 KKgSGFILMDEATANidpaLDRQ 1484
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
22-79 |
5.44e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 5.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 22 QLSILTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGS---SGEVSMLGkplHRMDE 79
Cdd:PLN03140 177 KLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNG---YRLNE 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-224 |
9.77e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 2 PAENILEVHHLKksvgqGEHQLSIlTGVELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRMD--- 78
Cdd:PRK10982 246 PGEVILEVRNLT-----SLRQPSI-RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNane 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 79 ----------EEARAALRAQHVGFVFQSfmLIPTLNALENVElpALLrgaSDSESQGDARALLEQLGLGKRLHHLP-AQL 147
Cdd:PRK10982 320 ainhgfalvtEERRSTGIYAYLDIGFNS--LISNIRNYKNKV--GLL---DNSRMKSDTQWVIDSMRVKTPGHRTQiGSL 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 148 SGGEQQRVALARAFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPLLAARCDRRLRLVDGQL 224
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
32-67 |
2.06e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.46 E-value: 2.06e-04
10 20 30
....*....|....*....|....*....|....*.
gi 496080956 32 VVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEV 67
Cdd:PRK01889 191 WLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
154-218 |
2.75e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496080956 154 RVALARAFNGRPALLFADEPTGNLDRQTGDKIA----DLLFSLNREHGTTLILVTHDPLLAARCDRRLR 218
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESLAhalvEIIKSRSQQRNFQLLVITHDEDFVELLGRSEY 1281
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
147-205 |
3.27e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 3.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496080956 147 LSGGEQQRVALA----RAFNGRPALLFaDEPTgnldrqTG---DKIADLLFSLNR--EHGTTLILVTH 205
Cdd:COG0178 827 LSGGEAQRVKLAselsKRSTGKTLYIL-DEPT------TGlhfHDIRKLLEVLHRlvDKGNTVVVIEH 887
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-228 |
5.33e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 40.66 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 29 VELVVKPRQTIALIGESGSGKSTLLAILAGLDDGSSGEVSMLGKPLHRmdEEARAALRAqhvGFVF-----QSFMLIPTL 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI--RSPRDAIRA---GIMLcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 NALENVELPA---------LLRGASDSESqgdARALLEQLGLGKRLHHLP-AQLSGGEQQRVALARAFNGRPALLFADEP 173
Cdd:PRK11288 347 SVADNINISArrhhlragcLINNRWEAEN---ADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496080956 174 TGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-PLLAARCDRRLRLVDGQL-----REEA 228
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDlPEVLGVADRIVVMREGRIagelaREQA 483
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
130-214 |
5.98e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 130 LLEQLGLGK-RLHHLPAQLSGGEQQRVALARAFNGR---PALLFADEPTgnldrqTG---DKIADLLFSLNR--EHGTTL 200
Cdd:cd03271 152 TLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPT------TGlhfHDVKKLLEVLQRlvDKGNTV 225
|
90
....*....|....
gi 496080956 201 ILVTHDPLLAARCD 214
Cdd:cd03271 226 VVIEHNLDVIKCAD 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-227 |
6.03e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.49 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 26 LTGVELVVKPRQTIALIGESGSGKSTLL-AILAGLDDGSSGEVSMLGKplhrmdeearaalraqhVGFVFQ-SFMLIPTL 103
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRGT-----------------VAYVPQvSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 104 NalENVeLPALLRGASDSESQGDARALLEQLGL---------GKRlhhlPAQLSGGEQQRVALARAFNGRPALLFADEPT 174
Cdd:PLN03130 696 R--DNI-LFGSPFDPERYERAIDVTALQHDLDLlpggdlteiGER----GVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496080956 175 GNLDRQTGDKIADLlfSLNRE-HGTTLILVTHDPLLAARCDRRLRLVDGQLREE 227
Cdd:PLN03130 769 SALDAHVGRQVFDK--CIKDElRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
130-205 |
8.81e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 130 LLEQLGLGK-RLHHLPAQLSGGEQQRVALARAFNGR---PALLFADEPTgnldrqTG---DKIADLLFSLNR--EHGTTL 200
Cdd:TIGR00630 812 TLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPT------TGlhfDDIKKLLEVLQRlvDKGNTV 885
|
....*
gi 496080956 201 ILVTH 205
Cdd:TIGR00630 886 VVIEH 890
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
144-205 |
1.45e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 1.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 144 PA-QLSGGEQQRVALA-----RAfNGRpALLFADEPTgnldrqTG---DKIADLLFSLNR--EHGTTLILVTH 205
Cdd:PRK00349 827 PAtTLSGGEAQRVKLAkelskRS-TGK-TLYILDEPT------TGlhfEDIRKLLEVLHRlvDKGNTVVVIEH 891
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
146-178 |
1.62e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 1.62e-03
10 20 30
....*....|....*....|....*....|...
gi 496080956 146 QLSGGEQQRVALARAFNGRPALLFADEPTGNLD 178
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-219 |
1.69e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 139 RLHHLP-----AQLSGGEQQRVALAR---AFNGRPALLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPLLA 210
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVV 875
|
....*....
gi 496080956 211 ARCDRRLRL 219
Cdd:PRK00635 876 KVADYVLEL 884
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
147-218 |
1.95e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 38.34 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496080956 147 LSGGEQQRVALA-----RAFNGRPALLFaDEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPLLAARCDRRLR 218
Cdd:cd03241 171 ASGGELSRLMLAlkailARKDAVPTLIF-DEIDTGISGEVAQAVGKKLKELSRSH--QVLCITHLPQVAAMADNHFL 244
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
147-214 |
3.40e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.34 E-value: 3.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496080956 147 LSGGEQQ------RVALARAFNGRPALLFADEPTGNLDRQTGDKIADLL-FSLNREHGT-TLILVTHDPLLAARCD 214
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIeYSLKDSSDIpQVIMISHHRELLSVAD 877
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-207 |
3.41e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 3.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496080956 147 LSGGEQQRVALARAFNGR--PALLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDP 207
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDE 550
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
123-215 |
5.94e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain] Cd Length: 197 Bit Score: 36.67 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496080956 123 SQGDARALLEqlGLGKRLHHLpAQLSGGEQQRVALarafngrpALLFA------------DEPTGNLDRQTGDKIADLLF 190
Cdd:cd03278 93 SQGDVSEIIE--APGKKVQRL-SLLSGGEKALTAL--------ALLFAifrvrpspfcvlDEVDAALDDANVERFARLLK 161
|
90 100
....*....|....*....|....*
gi 496080956 191 SLNREhgTTLILVTHDPLLAARCDR 215
Cdd:cd03278 162 EFSKE--TQFIVITHRKGTMEAADR 184
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
30-60 |
7.93e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 36.28 E-value: 7.93e-03
10 20 30
....*....|....*....|....*....|....
gi 496080956 30 ELVVKPRQTIaLIGESGSGKSTLL---AILAGLD 60
Cdd:COG3910 32 GLEFHPPVTF-FVGENGSGKSTLLeaiAVAAGFN 64
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
28-57 |
9.71e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 9.71e-03
10 20 30
....*....|....*....|....*....|.
gi 496080956 28 GVELVVKPRQTIALIGESGSGKSTLL-AILA 57
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLdAIQT 44
|
|
| |
