|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-228 |
3.80e-159 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 439.21 E-value: 3.80e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAENIVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEE 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 ARAQLRARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQEEA 228
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEEA 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-228 |
1.94e-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: 369.46 E-value: 1.94e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 2 PAENIVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEA 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 RAQLRARHVGFVFQSFMLIPTLNALENVELPALLRGEnsGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQEEA 228
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDT 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-227 |
6.22e-114 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 325.07 E-value: 6.22e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARA 83
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 84 QLRARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059485 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 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 |
3.56e-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: 299.79 E-value: 3.56e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLR 86
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQL 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 |
2.82e-82 |
|
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: 244.57 E-value: 2.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-226 |
8.79e-71 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 215.30 E-value: 8.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHelsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RaRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAARCDRR-LRLVNGQLQE 226
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRvLELEDGRLVR 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-227 |
1.24e-66 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 205.43 E-value: 1.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-215 |
3.56e-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: 199.93 E-value: 3.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 2 PAENIVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeea 81
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 raqlraRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
Cdd:COG1116 80 ------PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDR 215
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADR 208
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-223 |
1.24e-60 |
|
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: 189.38 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHelsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVA---ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RaRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTHDPQLAARCDRR-LRLVNGQ 223
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRvIILDDGR 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-224 |
3.21e-60 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 199.56 E-value: 3.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAARCDRRLRLVNGQL 224
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-206 |
7.57e-60 |
|
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: 187.29 E-value: 7.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTmdeearaqlR 86
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-228 |
9.67e-60 |
|
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: 187.33 E-value: 9.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaQL 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RARHVGFVFQSFM--LIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLG---KRLDHLPAQLSGGEQQRVALARA 160
Cdd:cd03257 80 RRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEEA 228
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-215 |
3.29e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 186.80 E-value: 3.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHelsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RARhVGFVFQSFMLIPTLNALENVELPAL--------LRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
Cdd:COG3638 79 RRR-IGMIFQQFNLVPRLSVLTNVLAGRLgrtstwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDR 215
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADR 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-228 |
6.85e-58 |
|
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: 183.47 E-value: 6.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAqlr 86
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSFMLipTLNALENVE--LPALLRGENSGKSRDGAKTLLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNG 163
Cdd:COG1124 79 -RRVQMVFQDPYA--SLHPRHTVDriLAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEEA 228
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-219 |
6.91e-58 |
|
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: 182.04 E-value: 6.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 11 HLKKSVGqgDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRARHV 90
Cdd:TIGR03608 3 NISKKFG--DKV--ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 91 GFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059485 171 DEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAARCDRRLRL 219
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
6-224 |
3.40e-57 |
|
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: 180.60 E-value: 3.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RaRHVGFVFQSFMLIPTLNALENVELPA-LLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQL 224
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-227 |
5.82e-57 |
|
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: 180.95 E-value: 5.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 2 PAENIVEVHHLKKSvgQGDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEA 81
Cdd:COG1127 1 MSEPMIEVRNLTKS--FGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 RAQLRaRHVGFVFQSFMLIPTLNALENVELPalLRgENSGKSRDGAKTL----LEQLGLGKRLDHLPAQLSGGEQQRVAL 157
Cdd:COG1127 77 LYELR-RRIGMLFQGGALFDSLTVFENVAFP--LR-EHTDLSEAEIRELvlekLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEE 227
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAE 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-228 |
5.18e-56 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 178.26 E-value: 5.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGqgDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhTMDEEARAQL 85
Cdd:COG1126 1 MIEIENLHKSFG--DLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RaRHVGFVFQSFMLIPTLNALENVEL-PALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEEA 228
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREvADRVVFMDGGRIVEEG 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-228 |
8.52e-54 |
|
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: 180.10 E-value: 8.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKS-VGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEA 81
Cdd:COG1123 257 AEPLLEVRNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 RAQLRaRHVGFVFQ--SFMLIPTLNALENVELPALLRGENSGKSRDG-AKTLLEQLGLGKR-LDHLPAQLSGGEQQRVAL 157
Cdd:COG1123 337 LRELR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRErVAELLERVGLPPDlADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEEA 228
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-223 |
1.56e-53 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 171.98 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLKKSVGQGDHelsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRa 87
Cdd:cd03256 2 EVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFVFQSFMLIPTLNALENVELPAL--------LRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQ 223
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGR 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-226 |
3.98e-53 |
|
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: 170.01 E-value: 3.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDhelsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlr 86
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 arHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03259 73 --NIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQE 226
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-227 |
4.71e-53 |
|
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: 170.76 E-value: 4.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLR 86
Cdd:cd03261 1 IELRGLTKSFG----GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSFMLIPTLNALENVELPalLRgENSGKS----RDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFP--LR-EHTRLSeeeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PQLAARCDRRLRLVNGQLQEE 227
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIVAE 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-224 |
5.03e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.61 E-value: 5.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 14 KSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEaraQLRaRHVGFV 93
Cdd:COG4619 4 EGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP---EWR-RQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 94 FQ-SFMLIPTLnaLENVELPALLRGENSgkSRDGAKTLLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
Cdd:COG4619 80 PQePALWGGTV--RDNLPFPFQLRERKF--DRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059485 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-227 |
7.00e-53 |
|
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: 170.07 E-value: 7.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RaRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEE 227
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-210 |
2.10e-52 |
|
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: 168.09 E-value: 2.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhTMDEEARAQLR 86
Cdd:cd03262 1 IEIKNLHKSFG----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSFMLIPTLNALENVEL-PALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLA 210
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFA 198
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-207 |
3.90e-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: 169.12 E-value: 3.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAR 82
Cdd:COG3842 2 AMPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 83 aqlrarHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
Cdd:COG3842 78 ------NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496059485 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDP 207
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQ 196
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-227 |
4.30e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 168.72 E-value: 4.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RaRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEE 227
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-224 |
1.93e-50 |
|
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: 163.35 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRaRHVGFVFQSFMLIPTLNA 105
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059485 186 ADLLFSLNREhGTTLILVTHDPQLAARCDRR-LRLVNGQL 224
Cdd:cd03292 176 MNLLKKINKA-GTTVVVATHAKELVDTTRHRvIALERGKL 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-215 |
2.88e-48 |
|
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: 160.99 E-value: 2.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG---TSGEVSLVGQALHTMDEEAR 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 83 AQLRARHVGFVFQSFM--LIPTLNALENVELPALLRGENSGKSRDG-AKTLLEQLGL---GKRLDHLPAQLSGGEQQRVA 156
Cdd:COG0444 81 RKIRGREIQMIFQDPMtsLNPVMTVGDQIAEPLRIHGGLSKAEARErAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDR 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 |
6.09e-48 |
|
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: 155.81 E-value: 6.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDhelsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQlr 86
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQSFMLIPTLNALENVELPallrgensgksrdgaktlleqlglgkrldhlpaqLSGGEQQRVALARAFNGRPD 166
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQ 223
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-215 |
1.86e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 159.54 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQgdheLSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTmdeeaRAQLR 86
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-----NLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQSFMLIPTLNALENVE--LPALLRGEnsGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
Cdd:COG1118 74 ERRVGFVFQHYALFPHMTVAENIAfgLRVRPPSK--AEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059485 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDR 215
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADR 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-215 |
2.06e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.38 E-value: 2.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlr 86
Cdd:COG1131 1 IEVRGLTKRYG--DKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDR 215
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERlCDR 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
2.79e-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: 162.77 E-value: 2.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKKSVGQGDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGT---SGEVSLVGQALHTMDEe 80
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 araQLRARHVGFVFQSFM--LIPtLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
Cdd:COG1123 79 ---ALRGRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 159 RAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEEA 228
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDG 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-212 |
7.53e-47 |
|
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: 155.88 E-value: 7.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRARHVGFVFQSFMLIPTLNALEN 108
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 109 VELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
Cdd:cd03294 123 VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180
....*....|....*....|....
gi 496059485 189 LFSLNREHGTTLILVTHDPQLAAR 212
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEALR 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-223 |
1.30e-46 |
|
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: 153.39 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLkkSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqlRA 87
Cdd:cd03225 1 ELKNL--SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFVFQSF--MLIpTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:cd03225 75 RKVGLVFQNPddQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRLVNGQ 223
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-224 |
1.93e-46 |
|
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: 153.99 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHelsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RaRHVGFVFQSFMLIPTLNALENVELPAL--------LRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGRLgykptwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEI 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-228 |
7.05e-46 |
|
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: 151.95 E-value: 7.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLkkSVGQGDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG-----TSGEVSLVGQALHTMDEEa 81
Cdd:cd03260 1 IELRDL--NVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 RAQLRARhVGFVFQSFMLIPtLNALENVELPALLRGENSGKSRDG-AKTLLEQLGLGKRL-DHLPA-QLSGGEQQRVALA 158
Cdd:cd03260 76 VLELRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALWDEVkDRLHAlGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 159 RAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDPQLAARC-DRRLRLVNGQLQEEA 228
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFG 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
25-224 |
1.42e-45 |
|
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: 151.33 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhTMDEEARAQLRaRHVGFVFQS-----FMl 99
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK---DITKKNLRELR-RKVGLVFQNpddqlFA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 iPTLnaLENVEL-PallrgENSGKSRDGAKT----LLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
Cdd:COG1122 91 -PTV--EEDVAFgP-----ENLGLPREEIRErveeALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059485 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:COG1122 163 AGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-207 |
4.11e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 153.69 E-value: 4.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEearaqlR 86
Cdd:COG3839 4 LELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP------K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDP 207
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-217 |
4.45e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 150.24 E-value: 4.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQgdheLSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEvsLVGQALHTMDEEARAQL 85
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGD--LIVDGLKVNDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RARHVGFVFQSFMLIPTLNALENVEL-PALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059485 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAARCDRRL 217
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRL 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-215 |
1.21e-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: 147.11 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLkkSVGQGDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMdeeaRAQL 85
Cdd:COG1120 1 MLEAENL--SVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL----SRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RARHVGFVFQSFMLIPTLNALENVEL---PAL-LRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRELVALgryPHLgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 162 NGRPDVLFADEPTGNLD--RQTgdKIADLLFSLNREHGTTLILVTHDPQLAAR-CDR 215
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDlaHQL--EVLELLRRLARERGRTVVMVLHDLNLAARyADR 207
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-227 |
1.42e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.87 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLR 86
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:PRK11153 82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEE 227
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQ 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-174 |
2.67e-41 |
|
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: 137.78 E-value: 2.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLRaRHVGFVFQSFMLIPTLNA 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE---RKSLR-KEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 106 LENVELPALLRGENSGKSRDGAKTLLEQLGLG----KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
3.38e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 140.61 E-value: 3.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAENIVEVHHLkkSVGQGDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHtmdee 80
Cdd:COG1121 1 MMMMPAIELENL--TVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 araqLRARHVGFVFQSFMLIPT--LNALENVELPAL----LRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQR 154
Cdd:COG1121 72 ----RARRRIGYVPQRAEVDWDfpITVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 155 VALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-228 |
4.65e-41 |
|
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: 146.37 E-value: 4.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAENIVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKS-TLLAILAGLDDG---TSGEVSLVGQALHT 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 77 MDEEARAQLRARHVGFVFQSFMlipT-LNALENV-----ELPALLRGENSGKSRDGAKTLLEQLGL---GKRLDHLPAQL 147
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPM---TsLNPLHTIgkqiaEVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 148 SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQE 226
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
..
gi 496059485 227 EA 228
Cdd:COG4172 238 QG 239
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-210 |
6.38e-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: 6.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGdhelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlr 86
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 arHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03300 73 --PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLA 210
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEA 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
9.34e-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: 146.06 E-value: 9.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 2 PAENIVEVHHLkkSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEA 81
Cdd:COG4987 329 PGGPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 raqLRaRHVGFVFQSFMLIP-TLnaLENvelpalLRGENSGKSRDGAKTLLEQLGLGKRLDHLP-----------AQLSG 149
Cdd:COG4987 407 ---LR-RRIAVVPQRPHLFDtTL--REN------LRLARPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSG 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-210 |
4.03e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 138.01 E-value: 4.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHT---------- 76
Cdd:COG4598 9 LEVRDLHKSFG--DLE--VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 77 MDEEARAQLRARhVGFVFQSFMLIPTLNALENV-ELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRV 155
Cdd:COG4598 85 ADRRQLQRIRTR-LGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLA 210
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFA 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
25-219 |
8.01e-40 |
|
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: 135.68 E-value: 8.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlraRHVGFVFQSFMLIPTLN 104
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-----RRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVELPALLRGENSgkSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
Cdd:COG4133 92 VRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL 169
|
170 180 190
....*....|....*....|....*....|....*
gi 496059485 185 IADLLfSLNREHGTTLILVTHDPqLAARCDRRLRL 219
Cdd:COG4133 170 LAELI-AAHLARGGAVLLTTHQP-LELAAARVLDL 202
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-226 |
9.59e-40 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 136.47 E-value: 9.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhtmdEEARAQLR 86
Cdd:TIGR00968 1 IEIANISKRFG----SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ------DATRVHAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQE 226
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEvADRIVVMSNGKIEQ 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-224 |
1.05e-39 |
|
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: 134.45 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDhelsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlr 86
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSFMLIPTLNALENVElpallrgensgksrdgaktlleqlglgkrldhlpaqLSGGEQQRVALARAFNGRPD 166
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-210 |
1.43e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 136.30 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQgdHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQAL---HTMDEEARA 83
Cdd:COG4161 3 IQLKNINCFYGS--HQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 84 QLRaRHVGFVFQSFMLIPTLNALEN-VELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
Cdd:COG4161 79 LLR-QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496059485 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDPQLA 210
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFA 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-223 |
2.94e-39 |
|
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: 133.28 E-value: 2.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLkkSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLR 86
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSfmliptlnalenvelPALLRGensgksrdgakTLLEQLglgkrldhlpaqLSGGEQQRVALARAFNGRPD 166
Cdd:cd03228 76 -KNIAYVPQD---------------PFLFSG-----------TIRENI------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLnrEHGTTLILVTHDPQLAARCDRRLRLVNGQ 223
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-226 |
3.90e-39 |
|
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: 135.12 E-value: 3.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDHELSILTgveLVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEaraQLR 86
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLN---LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV---ELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGL--GKRLDHLPAQLSGGEQQRVALARAFNGR 164
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQE 226
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQ 216
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-206 |
4.92e-39 |
|
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: 137.86 E-value: 4.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLKKSVGQgdheLSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmdeeARAQLRA 87
Cdd:TIGR03265 6 SIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI------TRLPPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
Cdd:TIGR03265 76 RDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 496059485 168 LFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:TIGR03265 156 LLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHD 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-210 |
8.88e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 137.14 E-value: 8.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQgdheLSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhtmdEEARAQLR 86
Cdd:PRK10851 3 IEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT------DVSRLHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQSFMLIPTLNALENVE--LPALLRGE--NSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAfgLTVLPRRErpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496059485 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLA 210
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-219 |
9.05e-39 |
|
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: 133.71 E-value: 9.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSV---GQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQA----LHTMD 78
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 79 EEARAQLRARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHL-PAQLSGGEQQRVAL 157
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRL 219
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAvADRVVDV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-227 |
9.23e-39 |
|
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: 134.21 E-value: 9.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLKKSVGQGdhelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlra 87
Cdd:COG4555 3 EVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 168 LFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEE 227
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQ 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-226 |
1.12e-38 |
|
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: 133.15 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLvgqalhtmDEEARAQLR 86
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI--------GGRDVTDLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 A--RHVGFVFQSFMLIPTLNALENVELPALLRG----ENSGKSRDGAKTLleqlGLGKRLDHLPAQLSGGEQQRVALARA 160
Cdd:cd03301 69 PkdRDIAMVFQNYALYPHMTVYDNIAFGLKLRKvpkdEIDERVREVAELL----QIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLA-ARCDRRLRLVNGQLQE 226
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQIQQ 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-225 |
3.72e-38 |
|
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: 131.65 E-value: 3.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 18 QGDHELSILTGVElvvkrAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtMDEEARAQL--RARHVGFVFQ 95
Cdd:cd03297 10 LPDFTLKIDFDLN-----EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL--FDSRKKINLppQQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 96 SFMLIPTLNALENVELPalLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
Cdd:cd03297 83 QYALFPHLNVRENLAFG--LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059485 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQ 225
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQ 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-224 |
7.44e-38 |
|
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: 131.69 E-value: 7.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgDHELSIltgVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlr 86
Cdd:cd03299 1 LKVENLSKDWK--EFKLKN---VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 arHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03299 72 --DISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PQLAARCDRRLRLVNGQL 224
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKL 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-224 |
1.15e-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: 129.48 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLkkSVGQGDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeearAQLRA 87
Cdd:cd03214 1 EVENL--SVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----PKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFVFQSfmliptlnalenvelpallrgensgksrdgaktlLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
Cdd:cd03214 73 RKIAYVPQA----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 168 LFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
25-227 |
1.46e-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: 138.43 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLRaRHVGFVFQSFMLIP-TL 103
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR-RQIGVVLQDVFLFSgTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 104 naLENvelpalLRGENSGKSRDGAKTLLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
Cdd:COG2274 566 --REN------ITLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 173 PTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-226 |
1.53e-37 |
|
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: 130.92 E-value: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQgdheLSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhtmdEEARAQLR 86
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE------DATDVPVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQSFMLIPTLNALENV----ELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVafglRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQE 226
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRIEQ 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-223 |
1.73e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 130.65 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 31 LVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQAlHTMDEEARaqlraRHVGFVFQSFMLIPTLNALENVE 110
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-LTALPPAE-----RPVSMLFQENNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 111 L---PAL-LRGENsgksRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF-NGRPdVLFADEPTGNLD---RQtg 182
Cdd:COG3840 94 LglrPGLkLTAEQ----RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLvRKRP-ILLLDEPFSALDpalRQ-- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059485 183 dKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQ 223
Cdd:COG3840 167 -EMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGR 207
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
28-206 |
2.05e-37 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 132.52 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 28 GVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEaraQLRaRHVGFVFQSFMLIPTLNALE 107
Cdd:COG1125 20 DLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPV---ELR-RRIGYVIQQIGLFPHMTVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 108 NVELPALLRGENSGKSRDGAKTLLEQLGL--GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
Cdd:COG1125 96 NIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQL 175
|
170 180
....*....|....*....|.
gi 496059485 186 ADLLFSLNREHGTTLILVTHD 206
Cdd:COG1125 176 QDELLRLQRELGKTIVFVTHD 196
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-224 |
5.23e-37 |
|
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: 128.53 E-value: 5.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLkkSVGQGdHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeearaqlRA 87
Cdd:cd03226 1 RIENI--SFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFV-----FQSFMliptlnalENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
Cdd:cd03226 71 KSIGYVmqdvdYQLFT--------DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-221 |
6.88e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 128.37 E-value: 6.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 15 SVGQGDHELsiLTGVELVVKRAETIALIGESGSGKSTLLAILAG-LDDG--TSGEVSLVGQALHTMDEEARaqlrarHVG 91
Cdd:COG4136 8 TITLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQR------RIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 92 FVFQSFMLIPTLNALENVELpALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVN 221
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-222 |
8.54e-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: 128.74 E-value: 8.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEaraqlraRHVgfVFQSFMLIPTLNA 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD-------RMV--VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENVELP--ALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
Cdd:TIGR01184 72 RENIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059485 184 KIADLLFSLNREHGTTLILVTHDPQLAA-RCDRRLRLVNG 222
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-210 |
1.93e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 128.21 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 19 GDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQAL---HTMDEEARAQLRaRHVGFVFQ 95
Cdd:PRK11124 13 GAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 96 SFMLIPTLNALEN-VELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
Cdd:PRK11124 90 QYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 496059485 175 GNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLA 210
Cdd:PRK11124 170 AALDPEITAQIVSIIREL-AETGITQVIVTHEVEVA 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
25-228 |
2.33e-36 |
|
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: 134.12 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqlRARHVGFVFQSFMLIP-TL 103
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS----WRRQIAWVPQNPYLFAgTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 104 naLENvelpalLRGENSGKSRDGAKTLLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
Cdd:COG4988 428 --REN------LRLGRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 173 PTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPQLAARCDRRLRLVNGQLQEEA 228
Cdd:COG4988 500 PTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIVEQG 553
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-227 |
2.53e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 128.11 E-value: 2.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 5 NIVEVHHLKKSVGQgdheLSILTGVELVVKRAETIALIGESGSGKSTLLAILAGL-----DDGTSGEVSLVGQALHTMDe 79
Cdd:PRK14247 2 NKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 80 eaRAQLRaRHVGFVFQSFMLIPTLNALENVEL-PALLRGENSGKS-RDGAKTLLEQLGL----GKRLDHLPAQLSGGEQQ 153
Cdd:PRK14247 77 --VIELR-RRVQMVFQIPNPIPNLSIFENVALgLKLNRLVKSKKElQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDPQLAARC-DRRLRLVNGQLQEE 227
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARIsDYVAFLYKGQIVEW 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
21-224 |
2.80e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 128.26 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 21 HELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVsLVGQA-LHTMDEEARaqlrarhvgFVFQSFML 99
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTApLAEAREDTR---------LMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 IPTLNALENVELPAllrgenSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
Cdd:PRK11247 93 LPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496059485 180 QTGDKIADLLFSLNREHGTTLILVTHDPQLA-ARCDRRLRLVNGQL 224
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-224 |
3.45e-36 |
|
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: 127.85 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAR 82
Cdd:COG0411 1 SDPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 83 AQLR-ARhvgfVFQSFMLIPTLNALENVELPALLRGENSGKS---------------RDGAKTLLEQLGLGKRLDHLPAQ 146
Cdd:COG0411 77 ARLGiAR----TFQNPRLFPELTVLENVLVAAHARLGRGLLAallrlprarreereaRERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-206 |
4.36e-36 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 127.67 E-value: 4.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqlra 87
Cdd:COG4525 5 TVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 rhvGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 496059485 168 LFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-210 |
7.82e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 126.79 E-value: 7.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVgqgdHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSlVGQAlhTMD-----EEA 81
Cdd:PRK11264 4 IEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIR-VGDI--TIDtarslSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 RAQLRA--RHVGFVFQSFMLIPTLNALENV-ELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
Cdd:PRK11264 77 KGLIRQlrQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059485 159 RAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgTTLILVTHDPQLA 210
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFA 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-224 |
1.51e-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: 124.95 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLkkSVGQGDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeearaqlra 87
Cdd:cd03235 1 EVEDL--TVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFVFQSFMLIPT--LNALENVELPALLR----GENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
Cdd:cd03235 68 KRIGYVPQRRSIDRDfpISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLrLVNGQL 224
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEyFDRVL-LLNRTV 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-225 |
2.37e-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: 124.54 E-value: 2.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDHelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlr 86
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPQLAAR-CDRRLRLVNGQLQ 225
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-223 |
2.54e-35 |
|
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: 122.74 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLKKSVGQGdhelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAqlra 87
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFVFQsfmliptlnalenvelpallrgensgksrdgaktlleqlglgkrldhlpaqLSGGEQQRVALARAFNGRPDV 167
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 168 LFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAAR-CDRRLRLVNGQ 223
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-224 |
7.13e-35 |
|
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: 124.09 E-value: 7.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRa 87
Cdd:cd03219 2 EVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 rhVGFVFQSFMLIPTLNALENVELPALLRGENSGKS----------RDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
Cdd:cd03219 77 --IGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
26-205 |
1.37e-34 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 125.96 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAqlrarhVGFVFQSFMLIPTLNA 105
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG------IAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
Cdd:NF040840 90 FENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180
....*....|....*....|
gi 496059485 186 ADLLFSLNREHGTTLILVTH 205
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTH 189
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-228 |
1.79e-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: 125.30 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 41 LIGESGSGKSTLLAILAGLDDGTSGEVslvgqalhTMDEEARAQLRA--RHVGFVFQSFMLIPTLNALENVELPALLRGE 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSI--------MLDGEDVTNVPPhlRHINMVFQSYALFPHMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 119 NSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGT 198
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190
....*....|....*....|....*....|.
gi 496059485 199 TLILVTHDPQLA-ARCDRRLRLVNGQLQEEA 228
Cdd:TIGR01187 153 TFVFVTHDQEEAmTMSDRIAIMRKGKIAQIG 183
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-215 |
7.22e-34 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 120.94 E-value: 7.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQgdheLSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqalHTMDEEARaQLR 86
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVREPR-EVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARhVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03265 73 RR-IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLA-ARCDR 215
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDR 201
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-224 |
8.90e-34 |
|
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: 122.17 E-value: 8.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRaRHVGFVFQS----- 96
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQFpehql 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 97 FMliptlnalENVEL-----PALLrGENSGKSRDGAKTLLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
Cdd:TIGR04521 96 FE--------ETVYKdiafgPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PQLAARCDRRLRLVNGQL 224
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKI 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-224 |
1.05e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 120.75 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRaRHVGFVFQSFMLIPTLNA 105
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059485 186 ADLLFSLNREhGTTLILVTHDPQLAARCD-RRLRLVNGQL 224
Cdd:PRK10908 177 LRLFEEFNRV-GVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-217 |
1.38e-33 |
|
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: 119.91 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 31 LVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAqlrarhVGFVFQSFMLIPTLNALENVE 110
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 111 L---PAL-LRGENSGKsrdgAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
Cdd:cd03298 93 LglsPGLkLTAEDRQA----IEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|.
gi 496059485 187 DLLFSLNREHGTTLILVTHDPQLAARCDRRL 217
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRV 199
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
9-227 |
1.56e-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: 121.45 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 9 VHHLKKSVGQGDHE-LSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRa 87
Cdd:TIGR02769 9 THTYRTGGLFGAKQrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFVFQSfmLIPTLNALENVE--LPALLRG-ENSGKSRDGAKT--LLEQLGL-GKRLDHLPAQLSGGEQQRVALARAF 161
Cdd:TIGR02769 88 RDVQLVFQD--SPSAVNPRMTVRqiIGEPLRHlTSLDESEQKARIaeLLDMVGLrSEDADKLPRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEE 227
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
25-227 |
4.68e-33 |
|
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: 120.23 E-value: 4.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqaLHTMDEEARAQLRaRHVGFVFQ--------- 95
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR-KKVGMVFQnpdnqfvga 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 96 ------SFmliptlnALENvelpallRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLF 169
Cdd:TIGR04520 94 tveddvAF-------GLEN-------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIII 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 170 ADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:TIGR04520 160 LDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-206 |
5.80e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 121.38 E-value: 5.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAENIVEVHHLKKS--VGQG-----DHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQA 73
Cdd:COG4608 2 AMAEPLLEVRDLKKHfpVRGGlfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 74 LHTMDEEARAQLRaRHVGFVFQ----SfmLIPTLNALENVELPALLRGENSGKSRDG-AKTLLEQLGLgkRLDHL---PA 145
Cdd:COG4608 82 ITGLSGRELRPLR-RRMQMVFQdpyaS--LNPRMTVGDIIAEPLRIHGLASKAERRErVAELLELVGL--RPEHAdryPH 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 146 QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
40-223 |
2.63e-32 |
|
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: 120.21 E-value: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 40 ALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHtmDEEARAQLRA--RHVGFVFQSFMLIPTLNALENVELPalLRG 117
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ--DSARGIFLPPhrRRIGYVFQEARLFPHLSVRGNLLYG--RKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 118 ENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHG 197
Cdd:COG4148 105 APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELD 184
|
170 180
....*....|....*....|....*..
gi 496059485 198 TTLILVTHDPQLAAR-CDRRLRLVNGQ 223
Cdd:COG4148 185 IPILYVSHSLDEVARlADHVVLLEQGR 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-227 |
5.13e-32 |
|
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: 121.72 E-value: 5.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSV-------GQGDHELSILTGVELVVKRAETIALIGESGSGKSTL-LAILaGLDDgTSGEVSLVGQAL 74
Cdd:COG4172 272 APPLLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLIP-SEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 75 HTMDEEARAQLRaRHVGFVFQ----SfmLIPTLNALENVELP-ALLRGENSGKSRDG-AKTLLEQLGLGKR-LDHLPAQL 147
Cdd:COG4172 350 DGLSRRALRPLR-RRMQVVFQdpfgS--LSPRMTVGQIIAEGlRVHGPGLSAAERRArVAEALEEVGLDPAaRHRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 148 SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDpqLA---ARCDRRLRLVNGQL 224
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHD--LAvvrALAHRVMVMKDGKV 504
|
...
gi 496059485 225 QEE 227
Cdd:COG4172 505 VEQ 507
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
23-228 |
5.61e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.48 E-value: 5.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 23 LSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRaRHVGFVFQSfmLIPT 102
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFR-RDIQMVFQD--SISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 103 LNALENVE------LPALLRGENSGKSRDgAKTLLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
Cdd:PRK10419 102 VNPRKTVReiirepLRHLLSLDKAERLAR-ASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059485 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEEA 228
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQ 234
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
6-228 |
7.34e-32 |
|
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: 116.24 E-value: 7.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDD-----GTSGEVSLVGQALHTMDEE 80
Cdd:TIGR00972 1 AIEIENLNLFYG----EKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 ArAQLRaRHVGFVFQSFMLIPtLNALENVELPALLRGENSGKSRDG-AKTLLEQLGL----GKRLDHLPAQLSGGEQQRV 155
Cdd:TIGR00972 77 V-VELR-RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEiVEESLKKAALwdevKDRLHDSALGLSGGQQQRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059485 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPQLAARC-DRRLRLVNGQLQEEA 228
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARIsDRTAFFYDGELVEYG 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-215 |
7.73e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 116.67 E-value: 7.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 2 PAENIVEVHHLkkSVGQGDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG-----TSGEVSLVGQALHT 76
Cdd:COG1117 7 TLEPKIEVRNL--NVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 77 MDEEArAQLRaRHVGFVFQsfmlipTLNAL-----ENVELPALLRGENSGKSRDGA-KTLLEQLGLGK----RLDHLPAQ 146
Cdd:COG1117 83 PDVDV-VELR-RRVGMVFQ------KPNPFpksiyDNVAYGLRLHGIKSKSELDEIvEESLRKAALWDevkdRLKKSALG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPQLAARC-DR 215
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVsDY 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-226 |
9.10e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.90 E-value: 9.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGqgDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaql 85
Cdd:PRK09452 14 LVELRGISKSFD--GKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 rarHVGFVFQSFMLIPTLNALENVELPalLRGENSGKSrDGAKTLLEQLGLgKRLDHL----PAQLSGGEQQRVALARAF 161
Cdd:PRK09452 87 ---HVNTVFQSYALFPHMTVFENVAFG--LRMQKTPAA-EITPRVMEALRM-VQLEEFaqrkPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLA-ARCDRRLRLVNGQLQE 226
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQ 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
25-227 |
1.40e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.02 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRA-----RHVGFVFqsfml 99
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAvlpqhSSLSFPF----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 iptlNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF------NGRPDVLFADEP 173
Cdd:PRK13548 92 ----TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 174 TGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEE 227
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVAD 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-219 |
8.48e-31 |
|
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: 118.54 E-value: 8.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmdEEARAQLRARHVGFVFQS-FMLIPTLn 104
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL----ADADADSWRDQIAWVPQHpFLFAGTI- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 aLENVelpALLRGENSGK------SRDGAKTLLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
Cdd:TIGR02857 413 -AENI---RLARPDASDAeirealERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496059485 177 LDRQTGDKIADLLFSLNRehGTTLILVTHDPQLAARCDRRLRL 219
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-227 |
1.07e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 113.91 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSVGQgdHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTM----- 77
Cdd:PRK10619 2 SENKLNVIDLHKRYGE--HE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 78 -----DEEARAQLRARhVGFVFQSFMLIPTLNALENV-ELPALLRGENSGKSRDGAKTLLEQLGLGKRL-DHLPAQLSGG 150
Cdd:PRK10619 78 qlkvaDKNQLRLLRTR-LTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAARCDRR-LRLVNGQLQEE 227
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHvIFLHQGKIEEE 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-206 |
2.46e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.82 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAENIVEVHHLKKSVGQGdhelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhtmDEE 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE-----DVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 ARAqLRARHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
Cdd:PRK11432 72 HRS-IQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 161 FNGRPDVLFADEPTGNLD----RQTGDKIADLLFSLNrehgTTLILVTHD 206
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDanlrRSMREKIRELQQQFN----ITSLYVTHD 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-224 |
3.08e-30 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 110.00 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQlrarHVGFVFQSFMLIP-TL 103
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD----HVGYLPQDDELFSgSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 104 NalENVelpallrgensgksrdgaktlleqlglgkrldhlpaqLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
Cdd:cd03246 93 A--ENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496059485 184 KIADLLFSLnREHGTTLILVTHDPQLAARCDRRLRLVNGQL 224
Cdd:cd03246 134 ALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-228 |
3.66e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.80 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLkkSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmDEEAR 82
Cdd:PRK13635 2 KEEIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 83 AQLRaRHVGFVFQSfmliPtlnalENVELPALLRG------ENSGKSRDG----AKTLLEQLGLGKRLDHLPAQLSGGEQ 152
Cdd:PRK13635 77 WDVR-RQVGMVFQN----P-----DNQFVGATVQDdvafglENIGVPREEmverVDQALRQVGMEDFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQEEA 228
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-223 |
4.60e-30 |
|
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: 110.99 E-value: 4.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLkkSVGQGdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAqlrA 87
Cdd:cd03224 2 EVENL--NAGYG--KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFVFQSFMLIPTLNALENVELPALLRGensgksRDGAKTLLEQL-----GLGKRLDHLPAQLSGGEQQRVALARAFN 162
Cdd:cd03224 75 AGIGYVPEGRRIFPELTVEENLLLGAYARR------RAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRLVNGQ 223
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEiADRAYVLERGR 209
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
34-209 |
1.14e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 111.08 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 34 KRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeearAQLRARHVGFVFQ--SFMLIPTLNALENVEL 111
Cdd:COG4167 37 EAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD----YKYRCKHIRMIFQdpNTSLNPRLNIGQILEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 112 PALLRGENSGKSRDGA-KTLLEQLGLgkRLDHL---PAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
Cdd:COG4167 113 PLRLNTDLTAEEREERiFATLRLVGL--LPEHAnfyPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIIN 190
|
170 180
....*....|....*....|..
gi 496059485 188 LLFSLNREHGTTLILVTHDPQL 209
Cdd:COG4167 191 LMLELQEKLGISYIYVSQHLGI 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-224 |
1.67e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.87 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKKSVgqgdHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGL---DDGTSGEVSLVGQALHTMDEE 80
Cdd:PRK09984 2 QTIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 ARAQLRAR-HVGFVFQSFMLIPTLNALENVELPALlrGEN----------SGKSRDGAKTLLEQLGLGKRLDHLPAQLSG 149
Cdd:PRK09984 78 ARDIRKSRaNTGYIFQQFNLVNRLSVLENVLIGAL--GSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
15-224 |
1.70e-29 |
|
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: 112.51 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 15 SVGQGDHELSiltgVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHtmDEEARAQLRA--RHVGF 92
Cdd:TIGR02142 6 SKRLGDFSLD----ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLPPekRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 93 VFQSFMLIPTLNALENVELPallRGENSGKSRDGA-KTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
Cdd:TIGR02142 80 VFQEARLFPHLSVRGNLRYG---MKRARPSERRISfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059485 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRV 210
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
28-228 |
1.78e-29 |
|
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: 109.77 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 28 GVELVVKRAETIALIGESGSGKS-TLLAILAGLDDG---TSGEVSLVGQALhtmdeeARAQLRARHVGFVFQSFM--LIP 101
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPPGltqTSGEILLDGRPL------LPLSIRGRHIATIMQNPRtaFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 TLNALENVELPALLRGENSGKSRDGAKTLLEQLGL--GKRLDHL-PAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:TIGR02770 78 LFTMGNHAIETLRSLGKLSKQARALILEALEAVGLpdPEEVLKKyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059485 179 RQTGDKIADLLFSLNREHGTTLILVTHDPQLAARC-DRRLRLVNGQLQEEA 228
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLFGTGILLITHDLGVVARIaDEVAVMDDGRIVERG 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-206 |
3.17e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.03 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKS-TLLAILAGLDDG----TSGEVSLVGQALHTMDEE 80
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 ARAQLRARHVGFVFQSFMLipTLNALENVE-----LPALLRGENSGKSRDGAKTLLEQLGL---GKRLDHLPAQLSGGEQ 152
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMV--SLNPLHTLEkqlyeVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGER 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059485 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHN 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-227 |
8.30e-29 |
|
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: 112.97 E-value: 8.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDD--GTSGEV----------------S 68
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 69 LVGQA--------------LHTMDEEARAQLRARhVGFVFQ-SFMLIPTLNALENVeLPALLRGENSGK-SRDGAKTLLE 132
Cdd:TIGR03269 77 KVGEPcpvcggtlepeevdFWNLSDKLRRRIRKR-IAIMLQrTFALYGDDTVLDNV-LEALEEIGYEGKeAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 133 QLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR 212
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250
....*....|....*.
gi 496059485 213 -CDRRLRLVNGQLQEE 227
Cdd:TIGR03269 235 lSDKAIWLENGEIKEE 250
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-212 |
1.01e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.39 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGL-----DDGTSGEVSLVGQALHTMDEEArAQLRaRHVGFVFQSFML 99
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDP-IEVR-REVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 IPTLNALENVELPALLRGENSGKSR--DGAKTLLEQLGL----GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 496059485 174 TGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPQLAAR 212
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAAR 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-206 |
1.10e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 110.89 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhTMDEEARAQlraRHVGFVFQSFMLIPTLNALEN 108
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPAE---RGVGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 109 VELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR----QTGDK 184
Cdd:PRK11000 96 MSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvQMRIE 175
|
170 180
....*....|....*....|..
gi 496059485 185 IADLLFSLNRehgtTLILVTHD 206
Cdd:PRK11000 176 ISRLHKRLGR----TMIYVTHD 193
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-227 |
1.41e-28 |
|
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: 106.89 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDhelsILTGVELVVKRAeTIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlr 86
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPQ-LAARCDRRLRLVNGQLQEE 227
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEdVESLCNQVAVLNKGKLVFE 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-215 |
1.87e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSVGqGDHELSiltGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMD-EEA 81
Cdd:COG1129 1 AEPLLEMRGISKSFG-GVKALD---GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 RAQlrarHVGFVFQSFMLIPTLNALENVELPALLRGE---NSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
Cdd:COG1129 77 QAA----GIAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 159 RAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-PQLAARCDR 215
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRlDEVFEIADR 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-206 |
3.95e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.09 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQG-DHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraq 84
Cdd:COG1101 1 MLELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 85 lRARHVGFVFQSFML--IPTLNALENVELpALLRGENSG-------KSRDGAKTLLEQLGLG--KRLDHLPAQLSGGEQQ 153
Cdd:COG1101 78 -RAKYIGRVFQDPMMgtAPSMTIEENLAL-AYRRGKRRGlrrgltkKRRELFRELLATLGLGleNRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059485 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-221 |
4.63e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.15 E-value: 4.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVgQGDHELSiltGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmdeeARAQL 85
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL------SHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RARHVGFVFQSFMLIPTLNALENVEL----PALLRGENSGKSRDgAKTLLEQLGLGKRLDHlpaQLSGGEQQRVALARAF 161
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFglkqDKLPKAEIASRVNE-MLGLVHMQEFAKRKPH---QLSGGQRQRVALARSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVN 221
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-224 |
6.41e-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: 104.56 E-value: 6.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSV--GQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG--TSGEVSLVGQALHtmdeear 82
Cdd:cd03213 4 LSFRNLTVTVksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLD------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 83 AQLRARHVGFVFQSFMLIPTLNALENVELPALLRGensgksrdgaktlleqlglgkrldhlpaqLSGGEQQRVALARAFN 162
Cdd:cd03213 77 KRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059485 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDP--QLAARCDRRLRLVNGQL 224
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-206 |
1.80e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.17 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqlrarhvGFVFQSFMLIPTLN 104
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 496059485 185 IADLLFSLNREHGTTLILVTHD 206
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-225 |
1.96e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.20 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRA-----RHVGFVFqsfml 99
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAvlpqhSSLAFPF----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 iptlNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF-------NGRPDVLFADE 172
Cdd:COG4559 91 ----TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 173 PTGNLDrqtgdkIA------DLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRLVNGQLQ 225
Cdd:COG4559 167 PTSALD------LAhqhavlRLARQLARR-GGGVVAVLHDLNLAAQyADRILLLHQGRLV 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-224 |
2.70e-27 |
|
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: 103.79 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 30 ELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQAlHTMDEEARaqlraRHVGFVFQSFMLIPTLNALENV 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS-HTGLAPYQ-----RPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 110 EL---PAL-LRGENSGKSRDGAKtlleQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
Cdd:TIGR01277 92 GLglhPGLkLNAEQQEKVVDAAQ----QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059485 186 ADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:TIGR01277 168 LALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-225 |
2.71e-27 |
|
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: 104.34 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhtMDEEARAQLRARhVGFVF-QSFMLIPTLN 104
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKFLRR-IGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059485 185 IADLLFSLNREHGTTLILVTHDPQ-LAARCDRRLRLVNGQLQ 225
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRLL 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-224 |
8.43e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 102.74 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 31 LVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQAlHTMDEEARaqlraRHVGFVFQSFMLIPTLNALENVE 110
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSR-----RPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 111 L---PALlrgENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
Cdd:PRK10771 94 LglnPGL---KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059485 188 LLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRI 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-206 |
9.21e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 104.66 E-value: 9.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAR 82
Cdd:PRK11308 8 AIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 83 AQLRaRHVGFVFQSfmliP--TLNALENV----ELPALLRGENSGKSR-DGAKTLLEQLGLgkRLDH---LPAQLSGGEQ 152
Cdd:PRK11308 88 KLLR-QKIQIVFQN----PygSLNPRKKVgqilEEPLLINTSLSAAERrEKALAMMAKVGL--RPEHydrYPHMFSGGQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059485 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-225 |
1.12e-26 |
|
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: 107.14 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAqlraRHVGFVFQSFMLIP-TL 103
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG----RHIGYLPQDVELFDgTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 104 NalENVelpALLRGENSGK-----SRDGAKTLLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
Cdd:COG4618 423 A--ENI---ARFGDADPEKvvaaaKLAGVHEMILRLpdGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059485 177 LDRQtGDK-----IADLlfslnREHGTTLILVTHDPQLAARCDRRLRLVNGQLQ 225
Cdd:COG4618 498 LDDE-GEAalaaaIRAL-----KARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-227 |
1.13e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.17 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLRaRHVGFVFQSFMLIpTLN 104
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR-RQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENvelpalLRGENSGKSRDGAKTLLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
Cdd:COG1132 430 IREN------IRYGRPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059485 174 TGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:COG1132 504 TSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
2.11e-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: 106.04 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKK---SVGQGdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVS-LVGQALHTM-- 77
Cdd:TIGR03269 277 EPIIKVRNVSKryiSVDRG--VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMtk 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 78 ---DEEARAQlraRHVGFVFQSFMLIPTLNALEN------VELP-------ALLRGENSGKSRDGAKTLLEQLglgkrld 141
Cdd:TIGR03269 355 pgpDGRGRAK---RYIGILHQEYDLYPHRTVLDNlteaigLELPdelarmkAVITLKMVGFDEEKAEEILDKY------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 142 hlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLV 220
Cdd:TIGR03269 425 --PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMR 502
|
....
gi 496059485 221 NGQL 224
Cdd:TIGR03269 503 DGKI 506
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-207 |
5.06e-26 |
|
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: 100.42 E-value: 5.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 20 DHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG---TSGEVSLVGQALHtmdeeaRAQLRaRHVGFVFQS 96
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK------PDQFQ-KCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 97 FMLIPTLNALENVELPALLRGENSGKSRDGAK----TLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
Cdd:cd03234 90 DILLPGLTVRETLTYTAILRLPRKSSDAIRKKrvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|....*
gi 496059485 173 PTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDP 207
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQP 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-223 |
5.11e-26 |
|
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: 100.83 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAqlrARHVGFVFQSFMLIPTLN 104
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA---RLGIGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVELPALLRgensgKSRDGAKTLLEQLG-----LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTgnldr 179
Cdd:COG0410 95 VEENLLLGAYAR-----RDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS----- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059485 180 qTG------DKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRLVNGQ 223
Cdd:COG0410 165 -LGlaplivEEIFEIIRRLNRE-GVTILLVEQNARFALEiADRAYVLERGR 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-223 |
6.46e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.89 E-value: 6.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQAlHTMdeearaqlrarhvgFVFQ-SFMLIPTL 103
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-RVL--------------FLPQrPYLPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 104 NAlenvelpALLR-GENSGKSRDGAKTLLEQLGLGKRLDHL------PAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
Cdd:COG4178 443 RE-------ALLYpATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496059485 177 LDRQTGDKIADLLfsLNREHGTTLILVTHDPQLAARCDRRLRLVNGQ 223
Cdd:COG4178 516 LDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-225 |
1.02e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.84 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhTMDEEARAQLRaRHVGFVFQS----F 97
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLKEIR-KKIGIIFQNpdnqF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 98 MLIpTLNA-----LENvelpallRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
Cdd:PRK13632 97 IGA-TVEDdiafgLEN-------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059485 173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQ 225
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-227 |
1.02e-25 |
|
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: 98.54 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLkkSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQlr 86
Cdd:cd03247 1 LSINNV--SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 arhVGFVFQSFMLIPTlnalenvelpallrgensgksrdgakTLLEQLGlgkrldhlpAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03247 77 ---ISVLNQRPYLFDT--------------------------TLRNNLG---------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-215 |
1.07e-25 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 99.75 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 rarhvGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:cd03266 81 -----GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAAR-CDR 215
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERlCDR 205
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-227 |
1.35e-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: 104.05 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDhelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLR 86
Cdd:TIGR01193 474 IVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQS-FMLIPTLnaLENvelpaLLRGENSGKSRDGAKTLLE-----------QLGLGKRLDHLPAQLSGGEQQR 154
Cdd:TIGR01193 548 -QFINYLPQEpYIFSGSI--LEN-----LLLGAKENVSQDEIWAACEiaeikddienmPLGYQTELSEEGSSISGGQKQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 155 VALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhgtTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-223 |
1.69e-25 |
|
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: 98.89 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqalHTMDEEARaqlr 86
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAAR---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 aRHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03269 70 -NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAAR-CDRRLRLVNGQ 223
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGR 205
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-226 |
1.75e-25 |
|
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: 99.90 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDHelsiLTGVELVVKRAETIALIGESGSGKSTLLAILAG---LDDGTSGEVSLVGQA--LHTMDEE 80
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrlaPDHGTATYIMRSGAEleLYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 ARAQLRARHVGFVFQSFM--LIPTLNALENV-ELPALLRGENSGKSRDGAKTLLEQLGLGK-RLDHLPAQLSGGEQQRVA 156
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQNPRdgLRMRVSAGANIgERLMAIGARHYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAA-RCDRRLRLVNGQLQE 226
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVVE 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-206 |
1.80e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.00 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAENIVEVHHLKKSVGQGDHelsiLTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQA-----LH 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 76 TMDEEARAQLRARHVGFVFQSFM--LIPTLNALENVELPALLRGENS-GKSRDGAKTLLEQLGLG-KRLDHLPAQLSGGE 151
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIDaARIDDLPTTFSGGM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHD 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-224 |
2.11e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.42 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 31 LVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRARHVGFVFQSFMLIPTLNALENVE 110
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 111 LPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|....*
gi 496059485 191 SLNREHGTTLILVTHDPQLAARCDRRLRLV-NGQL 224
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEV 243
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-207 |
3.00e-25 |
|
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: 102.82 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqLRARhVGFVFQSFMLIPTlN 104
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VRRR-VSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVelpALLRGENSGksrDGAKTLLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
Cdd:TIGR02868 425 VRENL---RLARPDATD---EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....
gi 496059485 174 TGNLDRQTGDKIADLLFSLNRehGTTLILVTHDP 207
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-201 |
4.60e-25 |
|
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: 97.67 E-value: 4.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGdhelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQAlhtMDEEARAqlr 86
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS---YQKNIEA--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQSFMLIPTLNALENVELPALLRGensgKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLG----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190
....*....|....*....|....*....|....*
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLI 201
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLI 181
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-227 |
5.14e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.47 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 21 HELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALH--TMDEEARaQLRARhVGFVFQsfm 98
Cdd:PRK13646 18 YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThkTKDKYIR-PVRKR-IGMVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 99 lIPTLNALE-NVELPALLRGENSG----KSRDGAKTLLEQLGLGKRLDHL-PAQLSGGEQQRVALARAFNGRPDVLFADE 172
Cdd:PRK13646 93 -FPESQLFEdTVEREIIFGPKNFKmnldEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVN-GQLQEE 227
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKeGSIVSQ 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-206 |
5.97e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 9 VHHLKKSVGqgDHELsiLTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLvgqalhtmdeeaRAQLRar 88
Cdd:COG0488 1 LENLSKSFG--GRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------------PKGLR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 89 hVGFVFQSFMLIPTLNALENV-----ELPALLR-----------GENSGK----------SRDG------AKTLLEQLGL 136
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVldgdaELRALEAeleeleaklaePDEDLErlaelqeefeALGGweaearAEEILSGLGF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 137 GKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
Cdd:COG0488 142 PEEdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-212 |
6.09e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.32 E-value: 6.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLvGQalHTMDEEARA-QLRA--RHVGFVFQsfmlIPT 102
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GE--RVITAGKKNkKLKPlrKKVGIVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 103 LNALENVELPALLRG-ENSGKSRDGA----KTLLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
Cdd:PRK13634 96 HQLFEETVEKDICFGpMNFGVSEEDAkqkaREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 496059485 177 LDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR 212
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-205 |
6.14e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.64 E-value: 6.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 28 GVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHtMDEEARAqlRARHVGFVFQSFMLIPTLNALE 107
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRSPRDA--IALGIGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 108 NVEL---PALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
Cdd:COG3845 100 NIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADE 179
|
170 180
....*....|....*....|.
gi 496059485 185 IADLLFSLnREHGTTLILVTH 205
Cdd:COG3845 180 LFEILRRL-AAEGKSIIFITH 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-226 |
7.41e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLvGQALhtmdeearaql 85
Cdd:COG0488 315 VLELEGLSKSYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 rarHVGFVFQSF-MLIPTLNALENvelpalLRGENSGKSRDGAKTLLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNG 163
Cdd:COG0488 379 ---KIGYFDQHQeELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059485 164 RPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQE 226
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEAL----DDFPGTVLLVSHDRYFLDRvATRILEFEDGGVRE 509
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-224 |
7.52e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 97.28 E-value: 7.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 20 DHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLRaRHVGFVFQSFML 99
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 IP-TLNalENVELPA-------LLRGENSGksrdGAKTLLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLF 169
Cdd:cd03245 90 FYgTLR--DNITLGApladderILRAAELA----GVTDFVNKHpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 170 ADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPQLAARCDRRLRLVNGQL 224
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-226 |
7.93e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.20 E-value: 7.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 24 SILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARA---QLRaRHVGFVFQSFMLI 100
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIdaiKLR-KEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 101 PTLNALENVELPalLRGENSGKSRDGAKTL---LEQLGLGK----RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
Cdd:PRK14246 103 PHLSIYDNIAYP--LKSHGIKEKREIKKIVeecLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059485 174 TGNLDRQTGDKIADLLFSLNREhgTTLILVTHDPQLAAR-CDRRLRLVNGQLQE 226
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
33-227 |
1.13e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 99.05 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 33 VKRAETIALIGESGSGKS-TLLAILaGLDDG----TSGEVSLVGQALHTMDEEARAQLRARHVGFVFQSFMliPTLNALE 107
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSvSSLAIM-GLIDYpgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPM--TSLNPCY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 108 NV-----ELPALLRGENSGKSRDGAKTLLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
Cdd:PRK11022 107 TVgfqimEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059485 180 QTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLV-NGQLQEE 227
Cdd:PRK11022 187 TIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMyAGQVVET 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-210 |
2.66e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.07 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQGDhelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmDEEARAQL 85
Cdd:PRK13639 1 ILETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI---KYDKKSLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RARH-VGFVFQS---FMLIPTLnaLENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
Cdd:PRK13639 75 EVRKtVGIVFQNpddQLFAPTV--EEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLA 210
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLV 200
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-225 |
2.87e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.11 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKKSVGQgDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmDEEARA 83
Cdd:PRK13650 2 SNIIEVKNLTFKYKE-DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 84 QLRaRHVGFVFQSfmliPTlNAL--ENVELPALLRGENSGKSRDGAKT----LLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
Cdd:PRK13650 78 DIR-HKIGMVFQN----PD-NQFvgATVEDDVAFGLENKGIPHEEMKErvneALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQ 225
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVE 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-224 |
4.10e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.79 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 2 PAENIVEVHHLkkSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGL---DDGTSGEVSLVGQalhTMD 78
Cdd:PRK13640 1 MKDNIVEFKHV--SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGI---TLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 79 EEARAQLRARhVGFVFQSfmliPTlNAL--ENVELPALLRGENSGKSRDGAKTL----LEQLGLGKRLDHLPAQLSGGEQ 152
Cdd:PRK13640 76 AKTVWDIREK-VGIVFQN----PD-NQFvgATVGDDVAFGLENRAVPRPEMIKIvrdvLADVGMLDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQL 224
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
25-223 |
6.88e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 95.54 E-value: 6.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSG-EVSLVGqalHTMDEEARAQLRaRHVGFVFQSFML-IPT 102
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFG---ERRGGEDVWELR-KRIGLVSPALQLrFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 103 LNALENVELPAL-----LRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
Cdd:COG1119 94 DETVLDVVLSGFfdsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496059485 178 DRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARC-DRRLRLVNGQ 223
Cdd:COG1119 174 DLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-226 |
7.34e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 97.10 E-value: 7.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGL--DDG-TSGEVSLVGQALHTMDE 79
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaANGrIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 80 EARAQLRARHVGFVFQSFMliPTLNALENV-----ELPALLRGENSGKSRDGAKTLLEQLGLG---KRLDHLPAQLSGGE 151
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPM--TSLNPYMRVgeqlmEVLMLHKGMSKAEAFEESVRMLDAVKMPearKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PQLAARCDRRLRLVNGQLQE 226
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGRTME 242
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-211 |
9.87e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 97.22 E-value: 9.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 12 LKKSVGqGDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEearaqlRARHVG 91
Cdd:PRK11650 9 VRKSYD-GKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP------ADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 92 FVFQSFMLIPTLNALENVELPALLRG----ENSGKSRDGAKTLleqlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGmpkaEIEERVAEAARIL----ELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059485 168 LFADEPTGNLDrqtgdkiADL-------LFSLNREHGTTLILVTHDpQLAA 211
Cdd:PRK11650 156 FLFDEPLSNLD-------AKLrvqmrleIQRLHRRLKTTSLYVTHD-QVEA 198
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-226 |
1.35e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.36 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 20 DHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEearAQLRArHVGFVFQSFML 99
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALRQ-AISVVSQRVHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 ------------IPT------LNALENVELPALLrgensgksrDGAKTLLEQLGLGKRldhlpaQLSGGEQQRVALARAF 161
Cdd:PRK11160 426 fsatlrdnlllaAPNasdealIEVLQQVGLEKLL---------EDDKGLNAWLGEGGR------QLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFslnrEH--GTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLA----EHaqNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-224 |
1.36e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.92 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSVgqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAR 82
Cdd:PRK13651 5 VKNIVKIFNKKLPT-----ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 83 A---------------------QLRaRHVGFVFQ--SFMLIPTlNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKR 139
Cdd:PRK13651 80 KekvleklviqktrfkkikkikEIR-RRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 140 -LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD-PQLAARCDRRL 217
Cdd:PRK13651 158 yLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDlDNVLEWTKRTI 236
|
....*..
gi 496059485 218 RLVNGQL 224
Cdd:PRK13651 237 FFKDGKI 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
28-228 |
1.99e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 94.38 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 28 GVELVVKRAETIALIGESGSGKS-TLLAILAGLDDG---TSGEVSLVGQALhtmdeeARAQLRARHVGFVFQSfmliP-- 101
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAGvrqTAGRVLLDGKPV------APCALRGRKIATIMQN----Prs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 TLNALENVELPALLRGENSGKSRDGAKTL--LEQLGLGKR---LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
Cdd:PRK10418 91 AFNPLHTMHTHARETCLALGKPADDATLTaaLEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059485 177 LDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARC-DRRLRLVNGQLQEEA 228
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
25-227 |
2.16e-23 |
|
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: 93.75 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQAlhtmdeearAQLRARHVGFVfqsfmliPTLN 104
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---------SSLLGLGGGFN-------PELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVELPALLrgenSGKSRDGAKTLLEQL----GLGKRLDhLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
Cdd:cd03220 101 GRENIYLNGRL----LGLSRKEIDEKIDEIiefsELGDFID-LPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059485 180 QTGDKIADLLFSLnREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEE 227
Cdd:cd03220 176 AFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFD 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-215 |
4.56e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.49 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQl 85
Cdd:PRK13537 7 PIDFRNVEKRYG----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 rarhVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:PRK13537 82 ----VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAAR-CDR 215
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERlCDR 207
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-204 |
6.51e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 93.32 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKKSVGQGD-----HELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMD 78
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 79 EEARAQlRARhvgFVFQ--SFMLIPTLNALENVELPALLRGENSGKSRDGA-KTLLEQLGLgkRLDHL---PAQLSGGEQ 152
Cdd:PRK15112 82 YSYRSQ-RIR---MIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQiIETLRQVGL--LPDHAsyyPHMLAPGQK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059485 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVT 204
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-227 |
1.16e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.54 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 12 LKKSVGQGdhelSILTGVELVVKRAETIALIGESGSGKSTL-LAILAGLddGTSGEVSLVGQALHTMDEEARAQLRARhV 90
Cdd:PRK15134 292 LKRTVDHN----VVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLNRRQLLPVRHR-I 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 91 GFVFQ--SFMLIPTLNALE------NVELPALlrgeNSGKSRDGAKTLLEQLGLGKRLDH-LPAQLSGGEQQRVALARAF 161
Cdd:PRK15134 365 QVVFQdpNSSLNPRLNVLQiieeglRVHQPTL----SAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLA-ARCDRRLRLVNGQLQEE 227
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVrALCHQVIVLRQGEVVEQ 507
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
26-226 |
1.16e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDD-----GTSGEVSLVGQALHTMDEEArAQLRaRHVGFVFQSFMLI 100
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDT-VDLR-KEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 101 PtLNALENVELPALLRGENSGKSRDGA-KTLLEQLGLGKRL-DHLPAQ---LSGGEQQRVALARAFNGRPDVLFADEPTG 175
Cdd:PRK14239 99 P-MSIYENVVYGLRLKGIKDKQVLDEAvEKSLKGASIWDEVkDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059485 176 NLDRQTGDKIADLLFSLNREHgtTLILVTHDPQLAAR-CDRRLRLVNGQLQE 226
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRiSDRTGFFLDGDLIE 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-219 |
1.63e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqalhtmdeearaqlrARHVGFVFQSFMLIPTLNA 105
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 --LENVEL----PALLRGENSGKSRDGAKTLLEQLGLGkRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:NF040873 73 tvRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLA-DLAGRQlGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496059485 179 RQTGDKIADLLFSLNREhGTTLILVTHDPQLAARCDRRLRL 219
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
25-226 |
1.79e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.31 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQlrarHVGFVFQSfmliPTL- 103
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ----QVSYCAQT----PTLf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 104 --NALENVELPALLRGensgKSRDGAKTL--LEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:PRK10247 94 gdTVYDNLIFPWQIRN----QQPDPAIFLddLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 179 RQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLV--NGQLQE 226
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQphAGEMQE 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-207 |
1.85e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG---TSGEVSLVGQALHtmdeeaRAQLRARhVGFVFQSFM 98
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID------AKEMRAI-SAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 99 LIPTLNALENVELPALLR-GENSGKS--RDGAKTLLEQLGLGKRLDHL---PAQ---LSGGEQQRVALARAFNGRPDVLF 169
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRmPRRVTKKekRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059485 170 ADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDP 207
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQP 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-227 |
2.18e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 91.13 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 20 DHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLRaRHVGFVFQSFML 99
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLR-SMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 IPTlNALENVELpallrgENSGKSRDGAKTLLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVL 168
Cdd:cd03254 89 FSG-TIMENIRL------GRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 169 FADEPTGNLDRQTGDKIADLLFSLNreHGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEE 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-227 |
2.30e-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: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqLRaRHVGFVFQSFMLIPT-- 102
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR-RAIGVVPQDTVLFNDti 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 103 --------LNAL-ENVELPALLRG--ENSGKSRDGAKTLLEQLGLgkrldhlpaQLSGGEQQRVALARAFNGRPDVLFAD 171
Cdd:cd03253 92 gynirygrPDATdEEVIEAAKAAQihDKIMRFPDGYDTIVGERGL---------KLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 172 EPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVER 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-215 |
8.39e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.53 E-value: 8.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqaLHTMDEEARAQLRARhVGFVFQS--FMLIPTLnal 106
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNK-AGMVFQNpdNQIVATI--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 107 enVELPALLRGENSG----KSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
Cdd:PRK13633 103 --VEEDVAFGPENLGippeEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190
....*....|....*....|....*....|...
gi 496059485 183 DKIADLLFSLNREHGTTLILVTHDPQLAARCDR 215
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVEADR 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-215 |
1.06e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.55 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGqgDHElsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmDEEARaql 85
Cdd:COG4152 1 MLELKGLTKRFG--DKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDR--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 raRHVGFvfqsfM-----LIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
Cdd:COG4152 71 --RRIGY-----LpeergLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDR 215
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEElCDR 198
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
28-206 |
1.50e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 90.92 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 28 GVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRaRHVGFVFQSFM--LIPTLNA 105
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLasLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LE------NVELPALLRGEnsgkSRDGAKTLLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:PRK15079 118 GEiiaeplRTYHPKLSRQE----VKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180
....*....|....*....|....*...
gi 496059485 179 RQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-206 |
1.98e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.44 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAENIVEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEE 80
Cdd:PRK11831 2 QSVANLVDMRGVSFTRG----NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 ARAQLRARhVGFVFQSFMLIPTLNALENVELP---------ALLRGENSGKsrdgaktlLEQLGLGKRLDHLPAQLSGGE 151
Cdd:PRK11831 78 RLYTVRKR-MSMLFQSGALFTDMNVFDNVAYPlrehtqlpaPLLHSTVMMK--------LEAVGLRGAAKLMPSELSGGM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-226 |
3.68e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.46 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAENIVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALH----- 75
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 76 --TMDEEARAQL---RARHVGFVFQSFM--LIPTLNALENV-ELPALLRGENSGKSRDGAKTLLEQLGLGKR---LDHLP 144
Cdd:PRK10261 87 viELSEQSAAQMrhvRGADMAMIFQEPMtsLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 145 AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQ 223
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGE 246
|
...
gi 496059485 224 LQE 226
Cdd:PRK10261 247 AVE 249
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
28-221 |
3.71e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.51 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 28 GVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeearAQLRARHvGFV--FQSFMLIPTLNA 105
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP----GHQIARM-GVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENV-----------------ELPALLRGENSGKSRdgAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVL 168
Cdd:PRK11300 98 IENLlvaqhqqlktglfsgllKTPAFRRAESEALDR--AATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059485 169 FADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVN 221
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-205 |
3.98e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.65 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRARHVGFVFQsfmlIPTLNA 105
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENVELPALLRG-ENSGKSRDGAKTL----LEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
Cdd:PRK13649 99 FEETVLKDVAFGpQNFGVSQEEAEALarekLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180
....*....|....*....|....*.
gi 496059485 180 QTGDKIADLLFSLNREhGTTLILVTH 205
Cdd:PRK13649 179 KGRKELMTLFKKLHQS-GMTIVLVTH 203
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-225 |
4.81e-21 |
|
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: 90.87 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEaraQLrARHVGFVFQSFMLIPTLN 104
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE---TF-GKHIGYLPQDVELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 AlENVElpallRGENSGKSRD--------GAKTLLEQLGLGKRLDHLP--AQLSGGEQQRVALARAFNGRPDVLFADEPT 174
Cdd:TIGR01842 409 A-ENIA-----RFGENADPEKiieaaklaGVHELILRLPDGYDTVIGPggATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059485 175 GNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAARCDRRLRLVNGQLQ 225
Cdd:TIGR01842 483 SNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRIA 532
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-219 |
5.07e-21 |
|
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: 86.78 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALH-TMDEEARAQLRARHVGfvfqsfMLI 100
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfQRDSIARGLLYLGHAP------GIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 101 PTLNALENvelpalLRGENSGKSRDGAKTLLEQLGLGKrLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
Cdd:cd03231 86 TTLSVLEN------LRFWHADHSDEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496059485 180 QTGDKIADLLFSlNREHGTTLILVTHDP-QLAARCDRRLRL 219
Cdd:cd03231 159 AGVARFAEAMAG-HCARGGMVVLTTHQDlGLSEAGARELDL 198
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
5.85e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKKSVGQGDHELSiltGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmDEEARA 83
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALK---GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI---DYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 84 QLRARH-VGFVFQSfmliP-----TLNALENVELPALLRGENSGKSRDGAKTLLEQLGLgKRLDHLPAQ-LSGGEQQRVA 156
Cdd:PRK13636 77 LMKLREsVGMVFQD----PdnqlfSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAA-RCDR 215
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDN 211
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-224 |
6.57e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGtSGEVSLVGQALHTMDEEARAQLRA------RHVGF--VFQSF 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAylsqqqSPPFAmpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 98 ML-IPTLNALENVELpALLRgensgksrdgaktLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF-------NGRPDVLF 169
Cdd:COG4138 91 ALhQPAGASSEAVEQ-LLAQ-------------LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 170 ADEPTGNLDrqtgdkIA-----DLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:COG4138 157 LDEPMNSLD------VAqqaalDRLLRELCQQGITVVMSSHDLNHTLRhADRVWLLKQGKL 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-205 |
6.64e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.18 E-value: 6.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqaLHTMDEEARAQLRARHVGFVFQsfmlIPTLNA 105
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKLSDIRKKVGLVFQ----YPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LE-----NVELPALLRGENSGKSRDGAKTLLEQLGLGKR--LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:PRK13637 97 FEetiekDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180
....*....|....*....|....*..
gi 496059485 179 RQTGDKIADLLFSLNREHGTTLILVTH 205
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSH 203
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-215 |
7.09e-21 |
|
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: 85.56 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGdhelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLR 86
Cdd:cd03216 1 LELRGITKRFGGV----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS---PRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQsfmliptlnalenvelpallrgensgksrdgaktlleqlglgkrldhlpaqLSGGEQQRVALARAFNGRPD 166
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAAR-CDR 215
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEiADR 151
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-215 |
7.20e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.57 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlraRHVGFVFQSFMLIPTLNALEN 108
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR-----RRVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 109 VELPALLRG--ENSGKSRdgAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
Cdd:NF033858 360 LELHARLFHlpAAEIAAR--VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180
....*....|....*....|....*....
gi 496059485 187 DLLFSLNREHGTTLILVTHDPQLAARCDR 215
Cdd:NF033858 438 RLLIELSREDGVTIFISTHFMNEAERCDR 466
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-205 |
7.55e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.25 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRARHVGFVFQsfmlIPTLNA 105
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----FPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENVELPALLRG-ENSGKSRDGAKTL----LEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
Cdd:PRK13643 98 FEETVLKDVAFGpQNFGIPKEKAEKIaaekLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180
....*....|....*....|....*.
gi 496059485 180 QTGDKIADLLFSLNrEHGTTLILVTH 205
Cdd:PRK13643 178 KARIEMMQLFESIH-QSGQTVVLVTH 202
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-224 |
8.33e-21 |
|
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: 85.56 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLkkSVGQGdhelsiLTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAR 82
Cdd:cd03215 1 GEPVLEVRGL--SVKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 83 aqlRARHVGFV---FQSFMLIPTLNALENVELPALLrgensgksrdgaktlleqlglgkrldhlpaqlSGGEQQRVALAR 159
Cdd:cd03215 73 ---IRAGIAYVpedRKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLAR 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-PQLAARCDRRLRLVNGQL 224
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-224 |
1.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.58 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalHTMDEEARAQLRA--RHVGFVFQ---SFMLI 100
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY--HITPETGNKNLKKlrKKVSLVFQfpeAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 101 PTLnaLENVELPALLRGENSGKSRDGAKTLLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
Cdd:PRK13641 101 NTV--LKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496059485 180 QTGDKIADLLFSLNREhGTTLILVTHD-PQLAARCDRRLRLVNGQL 224
Cdd:PRK13641 179 EGRKEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-211 |
1.36e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.10 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKKSVGQGDHELSiltGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHtmdEEARA 83
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALK---GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 84 QLRARhVGFVFQSfmliP-----TLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
Cdd:PRK13647 76 WVRSK-VGLVFQD----PddqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059485 159 RAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAA 211
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAA 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-215 |
1.56e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSVGqGDHELSiltGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAR 82
Cdd:PRK09700 2 ATPYISMAGIGKSFG-PVHALK---SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 83 AQLrarHVGFVFQSFMLIPTLNALENVELPALLRGENSG-------KSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRV 155
Cdd:PRK09700 78 AQL---GIGIIYQELSVIDELTVLENLYIGRHLTKKVCGvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD-PQLAARCDR 215
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKlAEIRRICDR 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-221 |
1.61e-20 |
|
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: 84.51 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLkkSVGQGDHELsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLvgqalhtmdeearaqLR 86
Cdd:cd03223 1 IELENL--SLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQsfmliptlnalenveLPALLRGensgksrdgakTLLEQLGLgkrldhlP--AQLSGGEQQRVALARAFNGR 164
Cdd:cd03223 63 GEDLLFLPQ---------------RPYLPLG-----------TLREQLIY-------PwdDVLSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 165 PDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDPQLAARCDRRLRLVN 221
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
25-227 |
3.03e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.52 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEV-------SLVGqalhtmdeearaqlrarhVGFVFQsf 97
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVevngrvsALLE------------------LGAGFH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 98 mliPTLNALENVELPALLRgensGKSRDGAKTLLEQL----GLGKRLDhLPAQ-LSGGEQQRVALARAFNGRPDVLFADE 172
Cdd:COG1134 101 ---PELTGRENIYLNGRLL----GLSRKEIDEKFDEIvefaELGDFID-QPVKtYSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 173 PTGnldrqTGD-----KIADLLFSLnREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEE 227
Cdd:COG1134 173 VLA-----VGDaafqkKCLARIREL-RESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMD 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-209 |
3.29e-20 |
|
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: 83.27 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDhelsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVslvgqalhtmdeearaqlr 86
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 arhvgfvfqsfmliptlnalenvelpallrgensgksrdgaktlleQLGLGKRLDHLPaQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03221 58 ----------------------------------------------TWGSTVKIGYFE-QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDPQL 209
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYF 129
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-219 |
4.19e-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: 84.33 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEaraqlRARHVGFVFQSFMLIP 101
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 TLNALENVE-LPALLRGEnsgksRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
Cdd:TIGR01189 87 ELSALENLHfWAAIHGGA-----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059485 181 TGDKIADLLfslnREH---GTTLILVTHDPqLAARCDRRLRL 219
Cdd:TIGR01189 162 GVALLAGLL----RAHlarGGIVLLTTHQD-LGLVEARELRL 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-222 |
5.93e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeearAQLRARHVGFVFQSFMLIP 101
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS----ARAASRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 TLNALENVEL---PALLRGENSGKSRDGA-KTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
Cdd:PRK09536 91 EFDVRQVVEMgrtPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 178 D----RQTGDKIADLLfslnrEHGTTLILVTHDPQLAAR-CDRRLRLVNG 222
Cdd:PRK09536 171 DinhqVRTLELVRRLV-----DDGKTAVAAIHDLDLAARyCDELVLLADG 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-224 |
8.53e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.91 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqalHTMDEEaRAQLrARHVGFVF-QSFMLIPTLN 104
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKR-RKEF-ARRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHlPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
Cdd:COG4586 113 AIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059485 184 KIADLLFSLNREHGTTLILVTHDPQ-LAARCDRRLRLVNGQL 224
Cdd:COG4586 192 AIREFLKEYNRERGTTILLTSHDMDdIEALCDRVIVIDHGRI 233
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-228 |
1.34e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 85.34 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 23 LSILTGVELVVKRAETIALIGESGSGKSTLL-AILAGLDDG---TSGEVSLVGQALHTMDEEARAQLRARHVGFVFQ--S 96
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAkAICGITKDNwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQepS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 97 FMLIPTLNALENVElPALLRGENSGK-------SRDGAKTLLEQLGLGKR---LDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:COG4170 100 SCLDPSAKIGDQLI-EAIPSWTFKGKwwqrfkwRKKRAIELLHRVGIKDHkdiMNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQ-LAARCDRRLRLVNGQLQEEA 228
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLEsISQWADTITVLYCGQTVESG 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-223 |
1.93e-19 |
|
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: 82.52 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQGDHELS-ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqalhtmdeearaql 85
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 rarHVGFVFQSfmliPTLnalenveLPALLRgEN--SGKSRDGA--KTLLEQLGLGKRLDHLPAQ-----------LSGG 150
Cdd:cd03250 67 ---SIAYVSQE----PWI-------QNGTIR-ENilFGKPFDEEryEKVIKACALEPDLEILPDGdlteigekginLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQ 223
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
2.07e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.03 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKKSVgQGDHELSiLTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEara 83
Cdd:PRK13648 5 NSIIVFKNVSFQY-QSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 84 QLRaRHVGFVFQ--------SFMLIPTLNALENVELPallrgenSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRV 155
Cdd:PRK13648 80 KLR-KHIGIVFQnpdnqfvgSIVKYDVAFGLENHAVP-------YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-226 |
3.38e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 37 ETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLRaRHVGFVFQS--FMLIPTLNA----LENVE 110
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLDPRQTVgdsiMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 111 LPALLRGENSGKSrdgAKTLLEQLGLgkRLDH---LPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
Cdd:PRK10261 430 VHGLLPGKAAAAR---VAWLLERVGL--LPEHawrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059485 188 LLFSLNREHGTTLILVTHDPQLAARCDRRLRLVN-GQLQE 226
Cdd:PRK10261 505 LLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYlGQIVE 544
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
26-211 |
3.55e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMD-EEARaqlraRHVGFVFQS---FMLIP 101
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVR-----KFVGLVFQNpddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 TLNalENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
Cdd:PRK13652 95 TVE--QDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190
....*....|....*....|....*....|
gi 496059485 182 GDKIADLLFSLNREHGTTLILVTHDPQLAA 211
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVP 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-224 |
5.59e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.37 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLkkSVGQGDHelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEaraQL 85
Cdd:PRK11231 2 TLRTENL--TVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR---QL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 rARHVGFVFQSFMLIPTLNALENVEL---PAL-LRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
Cdd:PRK11231 75 -ARRLALLPQHHLTPEGITVRELVAYgrsPWLsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRyCDHLVVLANGHV 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-228 |
1.20e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.07 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 24 SILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSG-----EVSLVGQALHTMDEEARAQlraRHVGFVFQS-- 96
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFR---RRVGMLFQRpn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 97 -FMLIPTLNALENVELPALL-RGENSGKsrdgAKTLLEQLGL----GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
Cdd:PRK14271 112 pFPMSIMDNVLAGVRAHKLVpRKEFRGV----AQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 171 DEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDPQLAAR-CDRRLRLVNGQLQEEA 228
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGRLVEEG 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-178 |
1.27e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.00 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 40 ALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHtmDEEARAQLRA--RHVGFVFQSFMLIPTLNALENvelpalLRG 117
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF--DAEKGICLPPekRRIGYVFQDARLFPHYKVRGN------LRY 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 118 ENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:PRK11144 100 GMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-223 |
1.32e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 83.72 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGL-DDGT-SGEVSLVGQAL---HTMDEE 80
Cdd:TIGR02633 1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyPHGTwDGEIYWSGSPLkasNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 ARAqlrarhVGFVFQSFMLIPTLNALENV------ELPALLRGENSGKSRdgAKTLLEQLGLGKRLDHLP-AQLSGGEQQ 153
Cdd:TIGR02633 77 RAG------IVIIHQELTLVPELSVAENIflgneiTLPGGRMAYNAMYLR--AKNLLRELQLDADNVTRPvGDYGGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTHD-PQLAARCDRRLRLVNGQ 223
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-227 |
1.46e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqaLHTMDEEARAQLRaRHVGFVFQS----FMLIP 101
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIR-KLVGIVFQNpetqFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 TLNAL----ENVELPALlrgensgKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
Cdd:PRK13644 95 VEEDLafgpENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 178 DRQTGDKIADLLFSLNREhGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-227 |
2.03e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.37 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDD-----GTSGEVSLVGQALHTMDEEArAQLRaRHVGFVFQSFMLI 100
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDP-VEVR-RRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 101 PTlNALENVELPALLRG---------ENSGKSR---DGAKTLLEQLGLGkrldhlpaqLSGGEQQRVALARAFNGRPDVL 168
Cdd:PRK14243 104 PK-SIYDNIAYGARINGykgdmdelvERSLRQAalwDEVKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 169 FADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVELTEG 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-178 |
2.04e-18 |
|
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: 80.66 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLr 86
Cdd:cd03218 1 LRAENLSKRYG----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 arHVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
Cdd:cd03218 76 --GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170
....*....|..
gi 496059485 167 VLFADEPTGNLD 178
Cdd:cd03218 154 FLLLDEPFAGVD 165
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-219 |
3.11e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.46 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 27 TGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLR--ARHVGfvfqsfmLIPTLN 104
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylGHQPG-------IKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVELPALLRGENSgksRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdk 184
Cdd:PRK13538 91 ALENLRFYQRLHGPGD---DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG--- 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059485 185 IADL--LFSLNREHGTTLILVTHDP-QLAARCDRRLRL 219
Cdd:PRK13538 165 VARLeaLLAQHAEQGGMVILTTHQDlPVASDKVRKLRL 202
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-214 |
3.96e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTS-----GEVSLVGQALHtmdeEARAQLRA--RHVGFVFQSF 97
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIY----ERRVNLNRlrRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 98 MLIPtLNALENVELPALLRGENSGKSRDG-AKTLLEQLGLGKRLDHL----PAQLSGGEQQRVALARAFNGRPDVLFADE 172
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIVGWRPKLEIDDiVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496059485 173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-PQLAARCD 214
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSD 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-205 |
4.29e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGL-DDGT-SGEVSLVGQAL---HTMDEEARAqlrarhVGFVFQSFMLI 100
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyPHGTyEGEIIFEGEELqasNIRDTERAG------IAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 101 PTLNALENVELPA-LLRGE--NSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
Cdd:PRK13549 95 KELSVLENIFLGNeITPGGimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180
....*....|....*....|....*...
gi 496059485 178 DRQTGDKIADLLFSLnREHGTTLILVTH 205
Cdd:PRK13549 175 TESETAVLLDIIRDL-KAHGIACIYISH 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-206 |
4.47e-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: 82.29 E-value: 4.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSVGQGDHelsILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEvslvgqalhtmdeeAR 82
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------------AR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 83 AQLRARhVGFVFQSFMLIPTLNALENVE-----LPALLRGEN------SGKSRDGAKTLLEQLGLGKRLDH--------- 142
Cdd:TIGR03719 64 PQPGIK-VGYLPQEPQLDPTKTVRENVEegvaeIKDALDRFNeisakyAEPDADFDKLAAEQAELQEIIDAadawdldsq 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 143 ---------LP------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkIADLLFSLNREHGtTLILVTHD 206
Cdd:TIGR03719 143 leiamdalrCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPG-TVVAVTHD 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-228 |
5.96e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.14 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAENIVEVHHLKKSVGQgdhelsiLTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTmdeE 80
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQ-------LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 ARAQLRaRHVGFVFQSfmliPTLNAL-ENVELPALLRGENSGKSRDGA-KTLLEQLGLGKRLD---HLPAQLSGGEQQRV 155
Cdd:PRK13642 75 NVWNLR-RKIGMVFQN----PDNQFVgATVEDDVAFGMENQGIPREEMiKRVDEALLAVNMLDfktREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQEEA 228
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-227 |
8.01e-18 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 79.12 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEaraQLRaRHVGFVFQSfmliptln 104
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR---WLR-SQIGLVSQE-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 alenvelPALLRG---ENSGKSRDGAKTLLEQLGLGKRLDH-----LP-----------AQLSGGEQQRVALARAFNGRP 165
Cdd:cd03249 86 -------PVLFDGtiaENIRYGKPDATDEEVEEAAKKANIHdfimsLPdgydtlvgergSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADllfSLNREH-GTTLILVTHdpQLAA--RCDRRLRLVNGQLQEE 227
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQE---ALDRAMkGRTTIVIAH--RLSTirNADLIAVLQNGQVVEQ 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-205 |
8.13e-18 |
|
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: 81.98 E-value: 8.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 37 ETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLrarhvGFVFQSFMLIPTLNALENVELPALLR 116
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSL-----GMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 117 GENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNREH 196
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRS 1109
|
....*....
gi 496059485 197 GTTLILVTH 205
Cdd:TIGR01257 1110 GRTIIMSTH 1118
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-215 |
1.99e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.49 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQAlhtmdEEARAQLRARHVGFVFQSFMLIPTLN 104
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP-----VPARARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
Cdd:PRK13536 131 VRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190
....*....|....*....|....*....|..
gi 496059485 185 IADLLFSLnREHGTTLILVTHDPQLAAR-CDR 215
Cdd:PRK13536 211 IWERLRSL-LARGKTILLTTHFMEEAERlCDR 241
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-226 |
2.27e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqLRaRHVGFVFQSFMLIP 101
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY---LH-RQVALVGQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 T---------LNALENVELPALLRGENS----GKSRDGAKTLLEQLGlgkrldhlpAQLSGGEQQRVALARAFNGRPDVL 168
Cdd:TIGR00958 569 GsvreniaygLTDTPDEEIMAAAKAANAhdfiMEFPNGYDTEVGEKG---------SQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 169 FADEPTGNLDRQtgdkIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:TIGR00958 640 ILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-227 |
3.35e-17 |
|
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: 77.27 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 15 SVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLRaRHVGFVF 94
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLR-RQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 95 QSFMLIPTlNALENVELPAllRGENSGKSRDGAKT-----LLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
Cdd:cd03251 83 QDVFLFND-TVAENIAYGR--PGATREEVEEAARAanaheFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 168 LFADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVER 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-219 |
4.53e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHtmDEEARAQlrARHVGfvFQSFMLiP 101
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--DPDVAEA--CHYLG--HRNAMK-P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 TLNALENVELPALLRGENSGKSRDGaktlLEQLGLGkRLDHLPAQ-LSGGEQQRVALAR-AFNGRPdVLFADEPTGNLDR 179
Cdd:PRK13539 87 ALTVAENLEFWAAFLGGEELDIAAA----LEAVGLA-PLAHLPFGyLSAGQKRRVALARlLVSNRP-IWILDEPTAALDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059485 180 QTGDKIADlLFSLNREHGTTLILVTHDPqLAARCDRRLRL 219
Cdd:PRK13539 161 AAVALFAE-LIRAHLAQGGIVIAATHIP-LGLPGARELDL 198
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
40-224 |
4.96e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 40 ALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqlRARHVGFVFQSfmlIPTLNALENVELPALLR--- 116
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA----FARKVAYLPQQ---LPAAEGMTVRELVAIGRypw 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 117 ----GENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL 192
Cdd:PRK10575 114 hgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190
....*....|....*....|....*....|...
gi 496059485 193 NREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:PRK10575 194 SQERGLTVIAVLHDINMAARyCDYLVALRGGEM 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-207 |
6.39e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.15 E-value: 6.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTsgevSLVGQALHTMDEEARAQLraRHVGFVFQSFMLIP 101
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN----NFTGTILANNRKPTKQIL--KRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 TLNALENVELPALLRGENSGKSRDG---AKTLLEQLGLGKRLDHLPAQ-----LSGGEQQRVALARAFNGRPDVLFADEP 173
Cdd:PLN03211 154 HLTVRETLVFCSLLRLPKSLTKQEKilvAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190
....*....|....*....|....*....|....
gi 496059485 174 TGNLDRQTGDKIADLLFSLNREhGTTLILVTHDP 207
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQP 266
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-224 |
6.89e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 76.66 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 7 VEVHHLKKSVGQgdheLSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqlR 86
Cdd:COG4604 2 IEIKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 87 ARHVGFVFQSfmliPTLNALENV-ELPALLRGENSG---KSRDGAK--TLLEQLGL----GKRLDhlpaQLSGGEQQRVA 156
Cdd:COG4604 74 AKRLAILRQE----NHINSRLTVrELVAFGRFPYSKgrlTAEDREIidEAIAYLDLedlaDRYLD----ELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 157 LARAFNGRPDVLFADEPTGNLD----RQtgdkIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDmkhsVQ----MMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRV 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-205 |
9.36e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 9.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQG-DHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSL----VGQALHTMDEE 80
Cdd:PRK13631 21 ILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 ARA---------QLRaRHVGFVFQ--SFMLIPTLNALENVELPALLrGENSGKSRDGAKTLLEQLGLGKR-LDHLPAQLS 148
Cdd:PRK13631 101 TNPyskkiknfkELR-RRVSMVFQfpEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 149 GGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSlNREHGTTLILVTH 205
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITH 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-209 |
1.07e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 16 VGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGlddgtsgevslvgqalhtmdeearaqlraRHVGFVFQ 95
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-----------------------------ALKGTPVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 96 SFMLIPTLNALENVelpALLRGENSGKSRDGAKTLLEQLGLG-----KRLdhlPAQLSGGEQQRVALARAFNGRPDVLFA 170
Cdd:COG2401 87 GCVDVPDNQFGREA---SLIDAIGRKGDFKDAVELLNAVGLSdavlwLRR---FKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 496059485 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQL 209
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDV 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-210 |
1.16e-16 |
|
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: 75.26 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG--TSGEVSLVGQALHTMDEEARAQL 85
Cdd:cd03217 2 EIKDLHVSVG----GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDITDLPPEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 rarHVGFVFQSFMLIPTLNALEnvelpaLLRGENSGksrdgaktlleqlglgkrldhlpaqLSGGEQQRVALARAFNGRP 165
Cdd:cd03217 78 ---GIFLAFQYPPEIPGVKNAD------FLRYVNEG-------------------------FSGGEKKRNEILQLLLLEP 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496059485 166 DVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLA 210
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLL 167
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-227 |
1.30e-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: 75.99 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLRaRHVGFVFQSFMLIpTLN 104
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD---PAWLR-RQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVEL----PALLRGENSGKSRDGAKTLLE-QLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
Cdd:cd03252 92 IRDNIALadpgMSMERVIEAAKLAGAHDFISElPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496059485 180 QTGDKIADLLFSLNRehGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:cd03252 172 ESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-206 |
1.65e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEvSLVGQ-----ALHTMDEEARaqLRaRHVGFVFQs 96
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDyaipaNLKKIKEVKR--LR-KEIGLVFQ- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 97 fmlIPTLNALE-----NVELPALLRGENSGKSRDGAKTLLEQLGLGKR-LDHLPAQLSGGEQQRVALAR--AFNGRPDVL 168
Cdd:PRK13645 98 ---FPEYQLFQetiekDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGiiAMDGNTLVL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059485 169 faDEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK13645 175 --DEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHN 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-178 |
2.56e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 2 PAENIVEVHHLkkSVgQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeea 81
Cdd:COG3845 253 PGEVVLEVENL--SV-RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS--- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 RAQLRARHVGFV---FQSFMLIPTLNALENVEL-----PALLRG--ENSGKSRDGAKTLLEQLGLGKRLDHLPA-QLSGG 150
Cdd:COG3845 327 PRERRRLGVAYIpedRLGRGLVPDMSVAENLILgryrrPPFSRGgfLDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGG 406
|
170 180
....*....|....*....|....*...
gi 496059485 151 EQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-224 |
4.09e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 21 HELSILTG-VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTsGEVSLVGQALHTMDEearAQLRaRHVGFVFQSFML 99
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDP---ESWR-KHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 I-PTLnaLENVELpallrgENSGKSRDGAKTLLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDV 167
Cdd:PRK11174 435 PhGTL--RDNVLL------GNPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 168 LFADEPTGNLDRQTGDKIadlLFSLNRE-HGTTLILVTHDPQLAARCDRRLRLVNGQL 224
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLV---MQALNAAsRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-224 |
4.48e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 33 VKRAETIALIGESGSGKSTLLAILAGLDDGtSGEVSLVGQALHTMDEEARAQLRA-----RHVGF---VFQSFMLiptln 104
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAylsqqQTPPFampVFQYLTL----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 alenvELPAllrGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF-------NGRPDVLFADEPTGNL 177
Cdd:PRK03695 93 -----HQPD---KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpdiNPAGQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496059485 178 DrQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:PRK03695 165 D-VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRhADRVWLLKQGKL 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-227 |
5.30e-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: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 2 PAENIVEVHHLkkSVGQGdhelsiLTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeA 81
Cdd:COG1129 252 PGEVVLEVEGL--SVGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS--P 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 RAQLRArhvGFVF-----QSFMLIPTLNALENVELPALLRGENSG-----KSRDGAKTLLEQLGL-GKRLDHLPAQLSGG 150
Cdd:COG1129 322 RDAIRA---GIAYvpedrKGEGLVLDLSIRENITLASLDRLSRGGlldrrRERALAEEYIKRLRIkTPSPEQPVGNLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 151 EQQRVALARAFNGRPDVLFADEPTGNLDrqTGDK--IADLLFSLNREhGTTLILVTHD-PQLAARCDRRLRLVNGQLQEE 227
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGID--VGAKaeIYRLIRELAAE-GKAVIVISSElPELLGLSDRILVMREGRIVGE 475
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-226 |
5.69e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.16 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEA-RAQLRArhvgfVFQSFMLiptlnale 107
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKLFSA-----VFTDFHL-------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 108 nveLPALLRGENSGKSRDGAKTLLEQLGLGKRLDH-----LPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
Cdd:PRK10522 409 ---FDQLLGPEGKPANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496059485 183 DKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:PRK10522 486 REFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-225 |
8.32e-16 |
|
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: 76.21 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 33 VKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARaqlraRHVGFVFQSFMLIPTLNALENVELP 112
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVH-----QNMGYCPQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 113 ALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL 192
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170 180 190
....*....|....*....|....*....|....
gi 496059485 193 NREhGTTLILVTHD-PQLAARCDRRLRLVNGQLQ 225
Cdd:TIGR01257 2117 IRE-GRAVVLTSHSmEECEALCTRLAIMVKGAFQ 2149
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-226 |
9.74e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.38 E-value: 9.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMdeeARAQLRaRHVGFVFQSFML------ 99
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLR-RNIAVVFQDAGLfnrsie 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 ----IPTLNALENVELPALLRGENSG---KSRDGAKTLLEQLGLgkrldhlpaQLSGGEQQRVALARAFNGRPDVLFADE 172
Cdd:PRK13657 427 dnirVGRPDATDEEMRAAAERAQAHDfieRKPDGYDTVVGERGR---------QLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059485 173 PTGNLDRQTGDKIADLLFSLNreHGTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-178 |
1.17e-15 |
|
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: 73.08 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 9 VHHLKKSVGQGdhelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLrar 88
Cdd:TIGR04406 4 AENLIKSYKKR----KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 89 HVGFVFQSFMLIPTLNALENVELPALLRGENSGKSRDG-AKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
Cdd:TIGR04406 77 GIGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREErLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKF 156
|
170
....*....|.
gi 496059485 168 LFADEPTGNLD 178
Cdd:TIGR04406 157 ILLDEPFAGVD 167
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-222 |
1.50e-15 |
|
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: 71.89 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG--TSGEVSLVGQALhtmDEEARaqlraRHVGFVFQSFMLIPT 102
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPL---DKNFQ-----RSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 103 LNALENVELPALLRGensgksrdgaktlleqlglgkrldhlpaqLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
Cdd:cd03232 94 LTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059485 183 DKIADLLFSLnREHGTTLILVTHDP--QLAARCDRRLRLVNG 222
Cdd:cd03232 145 YNIVRFLKKL-ADSGQAILCTIHQPsaSIFEKFDRLLLLKRG 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-205 |
2.96e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeARAQLRArHVGFVFQSFMLIPTLNA 105
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS--TTAALAA-GVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENV---ELPALLRGENSGKSRDGAKTLLEQLGLgkRLD-HLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD-R 179
Cdd:PRK11288 97 AENLylgQLPHKGGIVNRRLLNYEAREQLEHLGV--DIDpDTPlKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSaR 174
|
170 180
....*....|....*....|....*....
gi 496059485 180 QTgdkiaDLLFSLNRE---HGTTLILVTH 205
Cdd:PRK11288 175 EI-----EQLFRVIRElraEGRVILYVSH 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-206 |
4.85e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAENIVEVHHLKKSVGQG-----DHELSILTGVElvvkraetIALIGESGSGKSTLLAILAGLDDGTSGEvslvgqalh 75
Cdd:PRK11819 1 MMAQYIYTMNRVSKVVPPKkqilkDISLSFFPGAK--------IGVLGLNGAGKSTLLRIMAGVDKEFEGE--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 76 tmdeeARAQLRARhVGFVFQSFMLIPTLNALENVE-----LPALLRGEN------SGKSRDGAKTLLEQLGLGKRLDH-- 142
Cdd:PRK11819 64 -----ARPAPGIK-VGYLPQEPQLDPEKTVRENVEegvaeVKAALDRFNeiyaayAEPDADFDALAAEQGELQEIIDAad 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 143 ----------------LP------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkIADLLFSLNREHGtTL 200
Cdd:PRK11819 138 awdldsqleiamdalrCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPG-TV 213
|
....*.
gi 496059485 201 ILVTHD 206
Cdd:PRK11819 214 VAVTHD 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-224 |
6.35e-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: 70.96 E-value: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEaraQLRaRHVGFVFQSfmliPTLN 104
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YLH-SKVSLVGQE----PVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 A----------LENVELPALLrgENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
Cdd:cd03248 101 ArslqdniaygLQSCSFECVK--EAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 175 GNLDRQTGDKIADLLFSLNREHgtTLILVTHDPQLAARCDRRLRLVNGQL 224
Cdd:cd03248 179 SALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
25-226 |
6.48e-15 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 70.99 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeeaRAQLRaRHVGFVFQsfmlIPTL- 103
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR-SRISIIPQ----DPVLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 104 --------------------NALENVELpallrgensgksrdgaKTLLEQL--GLGKRLDHLPAQLSGGEQQRVALARAF 161
Cdd:cd03244 91 sgtirsnldpfgeysdeelwQALERVGL----------------KEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 162 NGRPDVLFADEPTGNLDRQTGDKIADLLfslnREH--GTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTI----REAfkDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-219 |
7.18e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVslvgqalhtmdeEARAQLRarhVGFVFQSFMLIPTLN 104
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR---IGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 AleNVELPALLRGensGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
Cdd:PRK09544 84 L--TVNRFLRLRP---GTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 496059485 185 IADLLFSLNREHGTTLILVTHDPQLA-ARCDRRLRL 219
Cdd:PRK09544 159 LYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCL 194
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-173 |
7.37e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.83 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 8 EVHHLKKSVGQgdheLSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHT--MDEearaql 85
Cdd:COG1137 5 EAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMHK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 RARH-VGF------VFQSfmliptLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
Cdd:COG1137 75 RARLgIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170
....*....|....*
gi 496059485 159 RAFNGRPDVLFADEP 173
Cdd:COG1137 149 RALATNPKFILLDEP 163
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-205 |
1.45e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGL-DDGT-SGEVSLVGQALH---TMDEEARaqlrarhvGFVF--QSFM 98
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyPHGSyEGEILFDGEVCRfkdIRDSEAL--------GIVIihQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 99 LIPTLNALENVelpaLLRGENS-------GKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
Cdd:NF040905 89 LIPYLSIAENI----FLGNERAkrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190
....*....|....*....|....*....|....
gi 496059485 172 EPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-205 |
1.76e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.67 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqLRaRHVGFVFQ-------SF 97
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV---LR-QGVAMVQQdpvvladTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 98 MLIPTL----------NALENVELPALLRGENsgksrDGAKTLLEQLGlgkrldhlpAQLSGGEQQRVALARAFNGRPDV 167
Cdd:PRK10790 432 LANVTLgrdiseeqvwQALETVQLAELARSLP-----DGLYTPLGEQG---------NNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059485 168 LFADEPTGNLDRQTGDKIADLLfSLNREHgTTLILVTH 205
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQAL-AAVREH-TTLVVIAH 533
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-206 |
4.35e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 19 GDHELsiLTGVELVVKRAETIALIGESGSGKSTLLAILAG---LDDG--------------------TSGEV-SLVGQAL 74
Cdd:PRK11147 14 SDAPL--LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDGriiyeqdlivarlqqdpprnVEGTVyDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 75 htmdEEARAQLRARHVgfVFQSFMLIPT---LNALENVElpALLRGENSGKSRDGAKTLLEQLGLGKrlDHLPAQLSGGE 151
Cdd:PRK11147 92 ----EEQAEYLKRYHD--ISHLVETDPSeknLNELAKLQ--EQLDHHNLWQLENRINEVLAQLGLDP--DAALSSLSGGW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNrehgTTLILVTHD 206
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ----GSIIFISHD 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-226 |
1.49e-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: 67.05 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 2 PAENIVEVHHLkkSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEA 81
Cdd:cd03369 2 PEHGEIEVENL--SVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 82 raqLRaRHVGFVFQSfmliPTL------------NALENVELPALLRGENSGKSrdgaktlleqlglgkrldhlpaqLSG 149
Cdd:cd03369 80 ---LR-SSLTIIPQD----PTLfsgtirsnldpfDEYSDEEIYGALRVSEGGLN-----------------------LSQ 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREH--GTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:cd03369 129 GQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI----REEftNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-214 |
2.85e-13 |
|
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: 66.09 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 40 ALIGESGSGKSTLL-AILAGLddgtSGEVSLVGQALHTMDEEARAQLRARHVGFVFQSFM-----LIPTLNALENVelpA 113
Cdd:cd03240 26 LIVGQNGAGKTTIIeALKYAL----TGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANgkkytITRSLAILENV---I 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 114 LLRGENSgksrdgAKTLLEQLGlgkrldhlpaQLSGGEQQ------RVALARAFNGRPDVLFADEPTGNLDRQTGD-KIA 186
Cdd:cd03240 99 FCHQGES------NWPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLA 162
|
170 180
....*....|....*....|....*...
gi 496059485 187 DLLFSLNREHGTTLILVTHDPQLAARCD 214
Cdd:cd03240 163 EIIEERKSQKNFQLIVITHDEELVDAAD 190
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-201 |
4.54e-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: 65.36 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 17 GQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGT---SGEVSLVGqalHTMDEEARAQlrARHVGFV 93
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG---IPYKEFAEKY--PGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 94 FQSFMLIPTLNALENVELPALLRGENSGKSrdgaktlleqlglgkrldhlpaqLSGGEQQRVALARAFNGRPDVLFADEP 173
Cdd:cd03233 89 SEEDVHFPTLTVRETLDFALRCKGNEFVRG-----------------------ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180
....*....|....*....|....*...
gi 496059485 174 TGNLDRQTGDKIADLLFSLNREHGTTLI 201
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-224 |
5.28e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.39 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGT--------SGEVSLVGQALHTMDEEARAQLRA-----RHVG 91
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAvlpqaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 92 FVFqsfmliptlNALENVEL---PALLR-GENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF------ 161
Cdd:PRK13547 96 FAF---------SAREIVLLgryPHARRaGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059485 162 ---NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAI 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-195 |
5.34e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQlraRHVGFVFQSFMLIPTLNA 105
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE---AGIGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENV----ELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL-DRQ 180
Cdd:PRK10762 97 AENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
|
170
....*....|....*
gi 496059485 181 TgdkiaDLLFSLNRE 195
Cdd:PRK10762 177 T-----ESLFRVIRE 186
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-226 |
6.44e-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: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmDEEARAQLRARhvgF--VFQSFMLIPTLNAL 106
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAYRQL---FsaVFSDFHLFDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 107 ENVELPALLRgensgksrdgakTLLEQLglgkRLDHLPA---------QLSGGEQQRVALARAF-NGRPDVLFaDEPTgn 176
Cdd:COG4615 425 DGEADPARAR------------ELLERL----ELDHKVSvedgrfsttDLSQGQRKRLALLVALlEDRPILVF-DEWA-- 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 177 ldrqtgdkiAD------------LLFSLnREHGTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:COG4615 486 ---------ADqdpefrrvfyteLLPEL-KARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-224 |
8.42e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.30 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQlraRHVGFVFQSFMLIPTLN 104
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR---RGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVELPALLRGENSGKSR-DGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
Cdd:PRK10895 95 VYDNLMAVLQIRDDLSAEQReDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059485 184 KIADLLFSLnREHGTTLILVTHD-PQLAARCDRRLRLVNGQL 224
Cdd:PRK10895 175 DIKRIIEHL-RDSGLGVLITDHNvRETLAVCERAYIVSQGHL 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
29-228 |
1.25e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.98 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDG----TSGEVSLVGQALHTMDEEARAQLRARHVGFVFQSfmliPT-- 102
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE----PQsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 103 LNALENVE------LPA-LLRGE-----NSGKSRdgAKTLLEQLGLGKRLD---HLPAQLSGGEQQRVALARAFNGRPDV 167
Cdd:PRK15093 102 LDPSERVGrqlmqnIPGwTYKGRwwqrfGWRKRR--AIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 168 LFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAAR-CDRRLRLVNGQLQEEA 228
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETA 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-222 |
1.53e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG---TSGEVSLVGQALhtmDEE 80
Cdd:TIGR00956 757 EDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL---DSS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 81 AraqlrARHVGFVFQSFMLIPTLNALENVELPALLRGENS----GKSR--DGAKTLLEQLGLGKRLDHLPAQ-LSGGEQQ 153
Cdd:TIGR00956 834 F-----QRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSvsksEKMEyvEEVIKLLEMESYADAVVGVPGEgLNVEQRK 908
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 154 RVALARAFNGRPDVL-FADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDPQ--LAARCDRRLRLVNG 222
Cdd:TIGR00956 909 RLTIGVELVAKPKLLlFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSaiLFEEFDRLLLLQKG 979
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
33-206 |
1.69e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 33 VKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmdeeaRAQLRARHVGFVFQSFML---IPTLnaLENV 109
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-------RQALQKNLVAYVPQSEEVdwsFPVL--VEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 110 ELPA------LLRgENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
Cdd:PRK15056 101 VMMGryghmgWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|...
gi 496059485 184 KIADLLFSLnREHGTTLILVTHD 206
Cdd:PRK15056 180 RIISLLREL-RDEGKTMLVSTHN 201
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
33-178 |
2.74e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 33 VKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDeearaqlRARHVGFVFQSFMLIPTLNALENVELP 112
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 113 ALLRGENSGKSRDGAKTLleqLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
22-224 |
2.93e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.74 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhTMDEEARAQLRArhVGFVFQSFMLIP 101
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTAKIMREA--VAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 TLNALENVELPALLrgensgKSRDGAKTLLEQL-GLGKRLDHLPAQ----LSGGEQQRVALARAFNGRPDVLFADEPTGN 176
Cdd:PRK11614 94 RMTVEENLAMGGFF------AERDQFQERIKWVyELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059485 177 LDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAAR-CDRRLRLVNGQL 224
Cdd:PRK11614 168 LAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHV 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-177 |
3.98e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVGQgdheLSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQL 85
Cdd:PRK15439 11 LLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 86 rarHVGFVFQSFMLIPTLNALENVelpaLLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
Cdd:PRK15439 87 ---GIYLVPQEPLLFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170
....*....|..
gi 496059485 166 DVLFADEPTGNL 177
Cdd:PRK15439 160 RILILDEPTASL 171
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-201 |
4.92e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 64.46 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQ--------ALHTM------------------- 77
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirdvtqaSLRAAigivpqdtvlfndtiayni 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 78 --------DEEARAQLRARHV-GFVfqsfmliptlnalenVELPallrgensgksrDGAKTLLEQLGLgkrldhlpaQLS 148
Cdd:COG5265 453 aygrpdasEEEVEAAARAAQIhDFI---------------ESLP------------DGYDTRVGERGL---------KLS 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059485 149 GGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgTTLI 201
Cdd:COG5265 497 GGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR-TTLV 548
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-226 |
2.25e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGevslvgqalhTMDEEARAQLRARHVGFVFQsfmliptLNA 105
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG----------TVDIKGSAALIAISSGLNGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059485 186 ADLLFSLnREHGTTLILVTHD-PQLAARCDRRLRLVNGQLQE 226
Cdd:PRK13545 183 LDKMNEF-KEQGKTIFFISHSlSQVKSFCTKALWLHYGQVKE 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-214 |
3.86e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.10 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVslvgqalhtmdeearaqLRARHVGFVFQSFMLiptln 104
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------------WAERSIAYVPQQAWI----- 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 alenveLPALLRG-------ENSGKSRDGAKTL-----LEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
Cdd:PTZ00243 733 ------MNATVRGnilffdeEDAARLADAVRVSqleadLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496059485 171 DEPTGNLDRQTGDKIADLLFsLNREHGTTLILVTHDPQLAARCD 214
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPRAD 849
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-227 |
3.91e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmdeEARAQLRA------------RHVGFvFQS 96
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI-----SPRSPLDAvkkgmayitesrRDNGF-FPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 97 FML---IPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
Cdd:PRK09700 356 FSIaqnMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-227 |
4.23e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 11 HLKKSVGQGDHELSILTG-----VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMD-EEARAQ 84
Cdd:PRK10762 248 RLDKAPGEVRLKVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLAN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 85 lrarhvGFVFQSF-----MLIPTLNALENVELPALLRGENSGKSRDGAKtllEQLGLG--KRL--------DHLPAQLSG 149
Cdd:PRK10762 328 ------GIVYISEdrkrdGLVLGMSVKENMSLTALRYFSRAGGSLKHAD---EQQAVSdfIRLfniktpsmEQAIGLLSG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD-PQLAARCDRRLRLVNGQLQEE 227
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEmPEVLGMSDRILVMHEGRISGE 476
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-214 |
4.39e-11 |
|
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: 60.42 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 23 LSILTGVELVVKRAETIALIGESGSGKSTLL-AILaglddgtsGEVSLVGQALH----TMDEEARAQLRARHVGFVFQSF 97
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAIL--------GEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 98 MLIPTLNAL--ENVELpallrGENSGKSRdgAKTLLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGR 164
Cdd:cd03290 86 QKPWLLNATveENITF-----GSPFNKQR--YKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059485 165 PDVLFADEPTGNLDRQTGDKI-ADLLFSLNREHGTTLILVTHDPQLAARCD 214
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQYLPHAD 209
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-206 |
6.33e-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: 60.46 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 32 VVKRAETIALIGESGSGKSTLLAILAGL---------DDGTSGEV--SLVGQALHT-----MDEEARAQLRARHVGfvfq 95
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKlkpnlgkfdDPPDWDEIldEFRGSELQNyftklLEGDVKVIVKPQYVD---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 96 sfmLIPtlNALENVELPALLRGENSGKsrdgAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
Cdd:cd03236 98 ---LIP--KAVKGKVGELLKKKDERGK----LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|.
gi 496059485 176 NLDRQTGDKIADLLFSLNrEHGTTLILVTHD 206
Cdd:cd03236 169 YLDIKQRLNAARLIRELA-EDDNYVLVVEHD 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
40-212 |
1.10e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.61 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 40 ALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmdEEARAQLRARHVGFVFQSFMLIPTLNALENV------ELPA 113
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI----QHYASKEVARRIGLLAQNATTPGDITVQELVargrypHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 114 LLRGENsgKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLN 193
Cdd:PRK10253 113 FTRWRK--EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELN 190
|
170
....*....|....*....
gi 496059485 194 REHGTTLILVTHDPQLAAR 212
Cdd:PRK10253 191 REKGYTLAAVLHDLNQACR 209
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-221 |
1.25e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSG--KSTLLAILAGLDDGTS----GEVSLVGQALHT 76
Cdd:NF000106 10 ARNAVEVRGLVKHFG----EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRpwrf*TWCANRRALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 77 MDEEARAQLRARHVGFvfqsfmliptlNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVA 156
Cdd:NF000106 86 TIG*HRPVR*GRRESF-----------SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLAARCDRRLRLVN 221
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVID 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-226 |
2.05e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhtmdeearaqlrarhVGFVFQSfMLIPTLNA 105
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------------VAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENVelpalLRGENSGKSRdgAKTLLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEPT 174
Cdd:TIGR00957 716 RENI-----LFGKALNEKY--YQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059485 175 GNLDRQTGDKIAD-LLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:TIGR00957 789 SAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
114-219 |
3.87e-10 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 56.60 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 114 LLRGEN-SGKSrdgakTLLEQLGLG---------KRLDHLPA---------------QLSGGEQQRVALA-----RAFNG 163
Cdd:cd03227 25 IITGPNgSGKS-----TILDAIGLAlggaqsatrRRSGVKAGcivaavsaeliftrlQLSGGEKELSALAlilalASLKP 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 164 RPDVLFaDEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAARCDRRLRL 219
Cdd:cd03227 100 RPLYIL-DEIDRGLDPRDGQALAEAILEH-LVKGAQVIVITHLPELAELADKLIHI 153
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-85 |
4.55e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 5 NIVEVHHLKKSVGqgdhELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLD--DGTSGEVSLVGQALHTMDEEAR 82
Cdd:CHL00131 6 PILEIKNLHASVN----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEER 81
|
...
gi 496059485 83 AQL 85
Cdd:CHL00131 82 AHL 84
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
123-215 |
5.44e-10 |
|
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: 57.27 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 123 SRDGAKTLLEQL---GLGK-RLDHLPAQLSGGEQQRVALARAFN-GRPDVLFA-DEPTGNLDRQTGDKIADLLFSLnREH 196
Cdd:cd03270 110 ARVGIRERLGFLvdvGLGYlTLSRSAPTLSGGEAQRIRLATQIGsGLTGVLYVlDEPSIGLHPRDNDRLIETLKRL-RDL 188
|
90
....*....|....*....
gi 496059485 197 GTTLILVTHDPQLAARCDR 215
Cdd:cd03270 189 GNTVLVVEHDEDTIRAADH 207
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-205 |
8.96e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 6 IVEVHHLKKSVgqgdHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG--TSGEVSLVGQALHTMDEEARA 83
Cdd:PRK09580 1 MLSIKDLHVSV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 84 qlrARHVGFVFQ----------SFMLIPTLNALENvelpalLRGENSGKSRDGAKTLLEQLGLGKrldhLPAQL------ 147
Cdd:PRK09580 77 ---GEGIFMAFQypveipgvsnQFFLQTALNAVRS------YRGQEPLDRFDFQDLMEEKIALLK----MPEDLltrsvn 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059485 148 ---SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205
Cdd:PRK09580 144 vgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-188 |
1.11e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqalHTM-DEEARAQLRARhvgfvfQSFM------ 98
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG---GDMaDARHRRAVCPR------IAYMpqglgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 99 -LIPTLNALENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
Cdd:NF033858 88 nLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 167
|
170
....*....|....*
gi 496059485 178 D----RQTGDKIADL 188
Cdd:NF033858 168 DplsrRQFWELIDRI 182
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-206 |
1.12e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 32 VVKRAETIALIGESGSGKSTLLAILAGL---------DDGTSGEV--SLVGQALHTMDEEARA-QLRARHVgfvFQSFML 99
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEVlkRFRGTELQNYFKKLYNgEIKVVHK---PQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 IPtlNALE-NV-ELpaLLRGENSGKSRDgaktLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
Cdd:PRK13409 172 IP--KVFKgKVrEL--LKKVDERGKLDE----VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|
gi 496059485 178 D-RQTgDKIADLLFSLNREHgtTLILVTHD 206
Cdd:PRK13409 244 DiRQR-LNVARLIRELAEGK--YVLVVEHD 270
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-209 |
2.25e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.17 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmDEEARAQLRAR-HVGFVFQS------F 97
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKRGLLALRqQVATVFQDpeqqifY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 98 MLIPTLNA--LENVELPAllrgENSGKSRDGAKTLLEqlglGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPT 174
Cdd:PRK13638 93 TDIDSDIAfsLRNLGVPE----AEITRRVDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190
....*....|....*....|....*....|....*
gi 496059485 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQL 209
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDL 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-225 |
4.44e-09 |
|
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: 55.99 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDGT-SGEVSLVGQALHTmdeeaRAQLRARHVGFVF-----QSFMLIPT 102
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDI-----RNPAQAIRAGIAMvpedrKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 103 LNALENVELPALLRgeNSGKSR-DGAKTL------LEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPT 174
Cdd:TIGR02633 354 LGVGKNITLSVLKS--FCFKMRiDAAAELqiigsaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059485 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHD-PQLAARCDRRLRLVNGQLQ 225
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQE-GVAIIVVSSElAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-178 |
4.56e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.80 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqalHTMDEEARAQLRaRHVGFVFQSFMLIPTLNA 105
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG---HDLRDYTLASLR-NQVALVSQNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 lENVELPAllRGENSGKSRDGAKTLLEQLGLGKRLDHL--------PAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
Cdd:PRK11176 435 -NNIAYAR--TEQYSREQIEEAARMAYAMDFINKMDNGldtvigenGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
.
gi 496059485 178 D 178
Cdd:PRK11176 512 D 512
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-208 |
1.05e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 33 VKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSlVGQALhtmdEEAR-AQLRARhvgfvfqsfmLIPTLNALENVel 111
Cdd:PRK11147 342 VQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKL----EVAYfDQHRAE----------LDPEKTVMDNL-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 112 pallrGEN------SGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdki 185
Cdd:PRK11147 405 -----AEGkqevmvNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET---- 475
|
170 180
....*....|....*....|...
gi 496059485 186 ADLLFSLNREHGTTLILVTHDPQ 208
Cdd:PRK11147 476 LELLEELLDSYQGTVLLVSHDRQ 498
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-206 |
1.11e-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: 53.95 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 11 HLKKSVGQGDHELSILTGVelvVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVslvGQALHTmdeearaqlrarhV 90
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGS---ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDT-------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 91 GFVFQsfmlipTLNALENVELPALLRGENSGKSRDGA-KT-LLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVL 168
Cdd:cd03237 64 SYKPQ------YIKADYEGTVRDLLSSITKDFYTHPYfKTeIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIY 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059485 169 FADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHD 175
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
28-206 |
1.29e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 53.09 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 28 GVELVVKRAETIALIGESGSGKSTLL-AILAGLDDGTSGEVSLVGQALHTMDEEARAQLRARHVGFV---------FQSF 97
Cdd:COG0419 15 DTETIDFDDGLNLIVGPNGAGKSTILeAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRyrierrqgeFAEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 98 MLIPTLNALENVElpALLRGENSGKSRDGAKTLLEQLGL------------GKRLDHL-----PAQLSGGEQQRVALARA 160
Cdd:COG0419 95 LEAKPSERKEALK--RLLGLEIYEELKERLKELEEALESaleelaelqklkQEILAQLsgldpIETLSGGERLRLALADL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496059485 161 FNgrpdvLFADepTGNLDRQTGDKIADLLFSLNrehgttliLVTHD 206
Cdd:COG0419 173 LS-----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-225 |
1.43e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTS-GEVSLVGQAL--HTMDEEARAQL------RARHvGfvfqsfmL 99
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVkiRNPQQAIAQGIamvpedRKRD-G-------I 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 IPTLNALENVELPALLRGENSGKSRDGA--KTLLEQLglgKRLD------HLP-AQLSGGEQQRVALARAFNGRPDVLFA 170
Cdd:PRK13549 353 VPVMGVGKNITLAALDRFTGGSRIDDAAelKTILESI---QRLKvktaspELAiARLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 171 DEPTGNLDrqTGDK--IADLLFSLNREhGTTLILVTHD-PQLAARCDRRLRLVNGQLQ 225
Cdd:PRK13549 430 DEPTRGID--VGAKyeIYKLINQLVQQ-GVAIIVISSElPEVLGLSDRVLVMHEGKLK 484
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-227 |
1.74e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAilaglddgtsgevSLVGQALHTmdEEARAQLRARhVGFVFQ-SFMLIPTLN 104
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLIS-------------AMLGELSHA--ETSSVVIRGS-VAYVPQvSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 alENVELPALLRGENSGKSRDgAKTLLEQLGL--GKRLDHLPAQ---LSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
Cdd:PLN03232 697 --ENILFGSDFESERYWRAID-VTALQHDLDLlpGRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 180 QTGDKIADllfSLNRE--HGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:PLN03232 774 HVAHQVFD---SCMKDelKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
41-206 |
1.83e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 41 LIGESGSGKSTLLAILAGLDDGTSGEVSL-VGQALhtmdeearAQLRARHvgFVFQSFMLIPTL----NALENVE----- 110
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERL--------GKLRQDQ--FAFEEFTVLDTVimghTELWEVKqerdr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 111 ---LP----------ALLRGE------NSGKSRDGAktLLeqLGLGKRLD-H--LPAQLSGGEQQRVALARAFNGRPDVL 168
Cdd:PRK15064 102 iyaLPemseedgmkvADLEVKfaemdgYTAEARAGE--LL--LGVGIPEEqHygLMSEVAPGWKLRVLLAQALFSNPDIL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059485 169 FADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
Cdd:PRK15064 178 LLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-215 |
1.84e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.45 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 129 TLLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRpdvLFA-----DEPTGNLDRQTGDKIADLLFSLnREHGTTLIL 202
Cdd:PRK00635 458 SILIDLGLPYlTPERALATLSGGEQERTALAKHLGAE---LIGityilDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLL 533
|
90
....*....|...
gi 496059485 203 VTHDPQLAARCDR 215
Cdd:PRK00635 534 VEHDEQMISLADR 546
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-215 |
2.42e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 29 VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHtmdeeARAQLRARHVGFVF-----QSFMLIPTL 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-----IRSPRDAIRAGIMLcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 104 NALENVELPA---LLRGE---NSGKSRDGAKTLLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
Cdd:PRK11288 347 SVADNINISArrhHLRAGcliNNRWEAENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059485 177 LDRQTGDKIADLLFSLnREHGTTLILVTHD-PQLAARCDR 215
Cdd:PRK11288 427 IDVGAKHEIYNVIYEL-AAQGVAVLFVSSDlPEVLGVADR 465
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-206 |
2.60e-08 |
|
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: 53.63 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 33 VKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLV------GQALHT-MDEEARAQLRARHVGFVFQSFmliptlna 105
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQYISPdYDGTVEEFLRSANTDDFGSSY-------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 lENVELpallrgensgksrdgaktlLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
Cdd:COG1245 435 -YKTEI-------------------IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
170 180
....*....|....*....|.
gi 496059485 186 ADLLFSLNREHGTTLILVTHD 206
Cdd:COG1245 495 AKAIRRFAENRGKTAMVVDHD 515
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-222 |
3.04e-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: 51.22 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 37 ETIALIGESGSGKSTLLAILAGlddgtsgevslvgqalhtmdeearaQLRARHVGFVFqsfmliptLNAlenvelpallr 116
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALAR-------------------------ELGPPGGGVIY--------IDG----------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 117 gensgksrDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI-----ADLLFS 191
Cdd:smart00382 39 --------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLLL 110
|
170 180 190
....*....|....*....|....*....|....*..
gi 496059485 192 LNREHGTTLILVTHDPQ------LAARCDRRLRLVNG 222
Cdd:smart00382 111 LKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLI 147
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-212 |
6.05e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 5 NIVEVHHLKKSVGQGdhelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVslvgqalhTMDEEARaq 84
Cdd:PRK15064 318 NALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENAN-- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 85 lrarhVGFVFQsfmliptlnalenvelpallrgeNSGKSRDGAKTLLEQLG---------------LGKRL---DHLPAQ 146
Cdd:PRK15064 384 -----IGYYAQ-----------------------DHAYDFENDLTLFDWMSqwrqegddeqavrgtLGRLLfsqDDIKKS 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 147 ---LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkIADLLFSLNREHGtTLILVTHDPQ----LAAR 212
Cdd:PRK15064 436 vkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMALEKYEG-TLIFVSHDREfvssLATR 504
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-213 |
8.42e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGlD--DGTSGEVSLVGQALHTmdEEARAQLRaRHVGFVFQSFMLIPT 102
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DhpQGYSNDLTLFGRRRGS--GETIWDIK-KHIGYVSSSLHLDYR 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 103 LNA-LENVELPAL-----LRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTG 175
Cdd:PRK10938 351 VSTsVRNVILSGFfdsigIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQ 430
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496059485 176 NLD---RQTGDKIADLLFSlnrEHGTTLILVTHDPQLAARC 213
Cdd:PRK10938 431 GLDplnRQLVRRFVDVLIS---EGETQLLFVSHHAEDAPAC 468
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-206 |
1.02e-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: 51.71 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 32 VVKRAETIALIGESGSGKSTLLAILAGL---------DDGTSGEVS--LVGQALHT-----MDEEARAQLRARHVGFVFQ 95
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGElkpnlgdydEEPSWDEVLkrFRGTELQDyfkklANGEIKVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 96 SFmlipTLNALEnvelpaLLRGENSgksRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
Cdd:COG1245 175 VF----KGTVRE------LLEKVDE---RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|..
gi 496059485 176 NLD-RQTgDKIADLLFSLNREhGTTLILVTHD 206
Cdd:COG1245 242 YLDiYQR-LNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-178 |
2.21e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 1 MPAEnivevhhlKKSVGQGDHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDG--TSGEVSLVGQAlhtmd 78
Cdd:PLN03140 879 MPAE--------MKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFP----- 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 79 eeARAQLRARHVGFVFQSFMLIPTLNALENVELPALLR--GENSGKSR----DGAKTLLEQLGLGKRLDHLPA--QLSGG 150
Cdd:PLN03140 946 --KKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRlpKEVSKEEKmmfvDEVMELVELDNLKDAIVGLPGvtGLSTE 1023
|
170 180
....*....|....*....|....*...
gi 496059485 151 EQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:PLN03140 1024 QRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
130-203 |
2.44e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 2.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059485 130 LLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILV 203
Cdd:PRK10938 119 LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-205 |
3.15e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 21 HELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALhtmdEEARAQLRaRHVGFVFQSFMLI 100
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 101 PTLNALENVelpalLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
Cdd:PRK13540 87 PYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 496059485 181 TGDKIADLLfSLNREHGTTLILVTH 205
Cdd:PRK13540 162 SLLTIITKI-QEHRAKGGAVLLTSH 185
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-223 |
3.80e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALH-TMDEEARAQlrarHVGFVFQSFMLIPTLN 104
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALEN----GISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 105 ALENVEL---PalLRG--ENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDr 179
Cdd:PRK10982 90 VMDNMWLgryP--TKGmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496059485 180 qtgDKIADLLFSLNR---EHGTTLILVTHD-PQLAARCDRRLRLVNGQ 223
Cdd:PRK10982 167 ---EKEVNHLFTIIRklkERGCGIVYISHKmEEIFQLCDEITILRDGQ 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-227 |
4.41e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTG-----VELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEARAQLrarhvGFVF-----Q 95
Cdd:PRK15439 274 LTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR-----GLVYlpedrQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 96 SFMLIptLNALENVELPALLRGENSGKSRDGAKT-LLEQL--GLGKRLDHL--PAQ-LSGGEQQRVALARAFNGRPDVLF 169
Cdd:PRK15439 349 SSGLY--LDAPLAWNVCALTHNRRGFWIKPARENaVLERYrrALNIKFNHAeqAARtLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059485 170 ADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHD----PQLAarcDRRLRLVNGQLQEE 227
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDleeiEQMA---DRVLVMHQGEISGA 484
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-222 |
4.58e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAG---LDDGT---SGEVSLVGQALHTMDEEARAQLRarhVGFVFQSFM 98
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGelePSEGKikhSGRISFSPQTSWIMPGTIKDNII---FGLSYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 99 LIPTLNALENVELPALLRGENsgksrdgaKTLLEQLGLgkrldhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:TIGR01271 518 YTSVIKACQLEEDIALFPEKD--------KTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059485 179 RQTGDKIAD-----LLFSLNRehgttlILVTHDPQLAARCDRRLRLVNG 222
Cdd:TIGR01271 581 VVTEKEIFEsclckLMSNKTR------ILVTSKLEHLKKADKILLLHEG 623
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-205 |
4.66e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVsLVGQAlHTMDEEARAQLRARhVGFVFQSFMLIP 101
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IINDS-HNLKDINLKWWRSK-IGVVSQDPLLFS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 ---------TLNALENVELPALLRGENSGKSRDGA--------------------------------------------- 127
Cdd:PTZ00265 474 nsiknnikySLYSLKDLEALSNYYNEDGNDSQENKnkrnscrakcagdlndmsnttdsneliemrknyqtikdsevvdvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 128 -KTLLEQL--GLGKRLDHL----PAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTL 200
Cdd:PTZ00265 554 kKVLIHDFvsALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
....*
gi 496059485 201 ILVTH 205
Cdd:PTZ00265 634 IIIAH 638
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-209 |
5.89e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 13 KKSVGQGDHelSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLV-GQALHTMDEEARAQLRARHvg 91
Cdd:PRK10636 317 KVSAGYGDR--IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRADE-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 92 fvfqsfmliptlNALENveLPALLRGENSGKSRDgaktLLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
Cdd:PRK10636 393 ------------SPLQH--LARLAPQELEQKLRD----YLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190
....*....|....*....|....*....|....*....
gi 496059485 171 DEPTGNLDRQTGDKIADLLFSLNrehgTTLILVTHDPQL 209
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEALIDFE----GALVVVSHDRHL 489
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-181 |
6.30e-07 |
|
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: 49.55 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 4 ENIVEVHHLKKSVGqgdHELSIlTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSlVGQALHtmdeeara 83
Cdd:TIGR03719 320 DKVIEAENLTKAFG---DKLLI-DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETVK-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 84 qlrarhVGFVFQSF-MLIPTLNALENVElpallrgensgksrDGaktlLEQLGLGKRldHLPA----------------- 145
Cdd:TIGR03719 387 ------LAYVDQSRdALDPNKTVWEEIS--------------GG----LDIIKLGKR--EIPSrayvgrfnfkgsdqqkk 440
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059485 146 --QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
Cdd:TIGR03719 441 vgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
39-206 |
7.09e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 39 IALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQ-ALHTMDEEARAqLRARHVGFVF-------QSFMLIPTLNALENVE 110
Cdd:PRK10636 30 VGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPA-LPQPALEYVIdgdreyrQLEAQLHDANERNDGH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 111 LPALLRGE----NSGKSRDGAKTLLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRqtgDKI 185
Cdd:PRK10636 109 AIATIHGKldaiDAWTIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL---DAV 185
|
170 180
....*....|....*....|.
gi 496059485 186 ADLLFSLNREHGtTLILVTHD 206
Cdd:PRK10636 186 IWLEKWLKSYQG-TLILISHD 205
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
147-209 |
7.26e-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: 7.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIadllFSLNREHGTTLILVTHDPQL 209
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM----YRLCREFGITLFSVSHRKSL 641
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
147-215 |
2.72e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 2.72e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDR 215
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDK 1427
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-206 |
2.87e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 3 AENIVEVHHLKKSvgQGDHELSILTGVelvVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLV------GQALHT 76
Cdd:PRK13409 337 RETLVEYPDLTKK--LGDFSLEVEGGE---IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 77 mDEEARAQLRARHVGFVFQSFMLiptlnaleNVELpallrgensgksrdgaktlLEQLGLGKRLDHLPAQLSGGEQQRVA 156
Cdd:PRK13409 412 -DYDGTVEDLLRSITDDLGSSYY--------KSEI-------------------IKPLQLERLLDKNVKDLSGGELQRVA 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
128-215 |
4.33e-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: 45.39 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 128 KTLLEqLGLGK-RLDHLPAQLSGGEQQRVALAR-AFNGRPDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVT 204
Cdd:cd03238 69 QFLID-VGLGYlTLGQKLSTLSGGELQRVKLASeLFSEPPGTLFIlDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIE 146
|
90
....*....|.
gi 496059485 205 HDPQLAARCDR 215
Cdd:cd03238 147 HNLDVLSSADW 157
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
26-226 |
4.83e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 26 LTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhtmdeearaqlrarhVGFVFQSFMLIPTLNA 105
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------------VSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 106 LENVELPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059485 186 ADLLFSLnREHGTTLILVTHD-PQLAARCDRRLRLVNGQLQE 226
Cdd:PRK13546 183 LDKIYEF-KEQNKTIFFVSHNlGQVRQFCTKIAWIEGGKLKD 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-227 |
5.36e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 22 ELSILTGVELVVKRAETIALIGESGSGKSTLL-AILAGLDDGTSGEVSLVGQalhtmdeearaqlrarhVGFVFQ-SFML 99
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRGT-----------------VAYVPQvSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 100 IPTLNalENVELPALLRGENSGKSRDGAktlleqlGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVL 168
Cdd:PLN03130 692 NATVR--DNILFGSPFDPERYERAIDVT-------ALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 169 FADEPTGNLDRQTGDKIADLlfSLNRE-HGTTLILVTHDPQLAARCDRRLRLVNGQLQEE 227
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFDK--CIKDElRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
147-224 |
6.79e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 6.79e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059485 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQL 224
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-223 |
9.34e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 45.62 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQalhtmdeearaqlrarhVGFVFQSFMLIP-TL 103
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQFSWIMPgTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 104 NalENVeLPALLRGENSGKSRDGAKTLLEQLGLGKRLDHLP-----AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:cd03291 115 K--ENI-IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059485 179 RQTGDKIAD-----LLFSLNRehgttlILVTHDPQLAARCDRRLRLVNGQ 223
Cdd:cd03291 192 VFTEKEIFEscvckLMANKTR------ILVTSKMEHLKKADKILILHEGS 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-226 |
1.86e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 25 ILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGqalHTMDEEARAQLRaRHVGFVFQSFMLIP--- 101
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD---CDVAKFGLTDLR-RVLSIIPQSPVLFSgtv 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 102 --TLNALENVELPALLRGENSGKSRDGAKTllEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
Cdd:PLN03232 1327 rfNIDPFSEHNDADLWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059485 180 QTGDKIADLLfslnREH--GTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:PLN03232 1405 RTDSLIQRTI----REEfkSCTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-223 |
1.97e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.71 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 32 VVKRAETIALIGESGSGKSTLLAILAGlddgtsgevslvgqalhtmdeearaqlrarhvgfvfqsfMLIPTLnalENVEL 111
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAG---------------------------------------QLIPNG---DNDEW 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 112 PallrgensgksrdgaktlleqlglGKRLDHLPA--QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
Cdd:cd03222 59 D------------------------GITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|....
gi 496059485 190 FSLNREHGTTLILVTHDPQLAARCDRRLRLVNGQ 223
Cdd:cd03222 115 RRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-205 |
6.85e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.16 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 20 DHELSILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQALHTMDEEAraqLRARhVGFVFQS-FM 98
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS---WRSR-LAVVSQTpFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 99 LIPTLN---AL-------ENVELPALLRGENSGKSR--DGAKTLLEQLGLgkrldhlpaQLSGGEQQRVALARAFNGRPD 166
Cdd:PRK10789 401 FSDTVAnniALgrpdatqQEIEHVARLASVHDDILRlpQGYDTEVGERGV---------MLSGGQKQRISIARALLLNAE 471
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059485 167 VLFADEPTGNLDRQTGDKIadlLFSLNR-EHGTTLILVTH 205
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQI---LHNLRQwGEGRTVIISAH 508
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-226 |
8.36e-05 |
|
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: 42.53 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 24 SILTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDgTSGEVSLVGQALHTMDeearAQLRARHVGFVFQS-FMLIPT 102
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVP----LQKWRKAFGVIPQKvFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 103 LNalENVELPALLRGENSGKSRD--GAKTLLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:cd03289 93 FR--KNLDPYGKWSDEEIWKVAEevGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059485 179 RQTGDKIADLL---FSlnrehGTTLILVTHDPQLAARCDRRLRLVNGQLQE 226
Cdd:cd03289 171 PITYQVIRKTLkqaFA-----DCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-181 |
1.72e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 5 NIVEVHHLKKSVGqgDHELsiLTGVELVVKRAETIALIGESGSGKSTLLAILAGLDDGTSGEVSlVGQALHtmdeearaq 84
Cdd:PRK11819 323 KVIEAENLSKSFG--DRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGETVK--------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 85 lrarhVGFVFQSfmliptlnalenvelpallRGensgkSRDGAKTL-------LEQLGLGKRldHLPA------------ 145
Cdd:PRK11819 389 -----LAYVDQS-------------------RD-----ALDPNKTVweeisggLDIIKVGNR--EIPSrayvgrfnfkgg 437
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496059485 146 -------QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
Cdd:PRK11819 438 dqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-178 |
1.75e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 28 GVELVVKRAETIA------LIGESGSGKSTLLAILA--------------GLDDGTSGEVSLVGQALHTMDEEaRAQLRA 87
Cdd:PLN03073 189 GRDLIVDASVTLAfgrhygLVGRNGTGKTTFLRYMAmhaidgipkncqilHVEQEVVGDDTTALQCVLNTDIE-RTQLLE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 88 RHVGFVFQSFMLiPTLNALENVELPallrgENSGKSRDGAKTLLEQLGlgKRLDHLPA---------------------- 145
Cdd:PLN03073 268 EEAQLVAQQREL-EFETETGKGKGA-----NKDGVDKDAVSQRLEEIY--KRLELIDAytaearaasilaglsftpemqv 339
|
170 180 190
....*....|....*....|....*....|....*..
gi 496059485 146 ----QLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
Cdd:PLN03073 340 katkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-215 |
1.75e-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: 42.31 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 129 TLLEQLGLGK-RLDHLPAQLSGGEQQRVALARAF-NGRPDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205
Cdd:TIGR00630 470 GFLIDVGLDYlSLSRAAGTLSGGEAQRIRLATQIgSGLTGVLYVlDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEH 548
|
90
....*....|
gi 496059485 206 DPQLAARCDR 215
Cdd:TIGR00630 549 DEDTIRAADY 558
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
154-218 |
2.27e-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: 41.96 E-value: 2.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIA----DLLFSLNREHGTTLILVTHDPQLAARCDRRLR 218
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESLAhalvEIIKSRSQQRNFQLLVITHDEDFVELLGRSEY 1281
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
147-218 |
3.08e-04 |
|
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: 40.65 E-value: 3.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 147 LSGGEQQRVALA--RAFNGRPDV--LFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDPQLAARCDRRLR 218
Cdd:cd03241 171 ASGGELSRLMLAlkAILARKDAVptLIFDEIDTGISGEVAQAVGKKLKELSRSH--QVLCITHLPQVAAMADNHFL 244
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-219 |
3.32e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 139 RLDHLP-----AQLSGGEQQRVALAR---AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDPQLA 210
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVV 875
|
....*....
gi 496059485 211 ARCDRRLRL 219
Cdd:PRK00635 876 KVADYVLEL 884
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
147-174 |
4.45e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 4.45e-04
10 20
....*....|....*....|....*...
gi 496059485 147 LSGGEQQRVALARAFNGRPDVLFADEPT 174
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
147-205 |
7.20e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 7.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059485 147 LSGGEQQRVALA----RAFNGRpdVLFA-DEPTgnldrqTG---DKIADLLFSLNR--EHGTTLILVTH 205
Cdd:COG0178 827 LSGGEAQRVKLAselsKRSTGK--TLYIlDEPT------TGlhfHDIRKLLEVLHRlvDKGNTVVVIEH 887
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
130-214 |
8.80e-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: 39.52 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 130 LLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFnGRPD------VLfaDEPTgnldrqTG---DKIADLLFSLNR--EHG 197
Cdd:cd03271 152 TLCDVGLGYiKLGQPATTLSGGEAQRIKLAKEL-SKRStgktlyIL--DEPT------TGlhfHDVKKLLEVLQRlvDKG 222
|
90
....*....|....*..
gi 496059485 198 TTLILVTHDPQLAARCD 214
Cdd:cd03271 223 NTVVVIEHNLDVIKCAD 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
147-222 |
1.60e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 147 LSGGEqqRVALARAFN--------GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgTTLILVTHDPQLAARCDR--R 216
Cdd:PRK03918 789 LSGGE--RIALGLAFRlalslylaGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKI-PQVIIVSHDEELKDAADYviR 865
|
....*.
gi 496059485 217 LRLVNG 222
Cdd:PRK03918 866 VSLEGG 871
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-209 |
1.64e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 39 IALIGESGSGKSTLLAILAGLDDGTSGEVSLVGQAlhtmdeeARAQLRARHV-GFVFQSFMLIPTLNALENVELPALlrg 117
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-------RMAVFSQHHVdGLDLSSNPLLYMMRCFPGVPEQKL--- 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 118 ensgksrdgaKTLLEQLGLGKRLDHLPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRqtgDKIADLLFSLNREH 196
Cdd:PLN03073 608 ----------RAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL---DAVEALIQGLVLFQ 674
|
170
....*....|...
gi 496059485 197 GTTLiLVTHDPQL 209
Cdd:PLN03073 675 GGVL-MVSHDEHL 686
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-205 |
2.23e-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: 38.84 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 128 KTLLEqLGLGK-RLDHLPAQLSGGEQQRVALARAFNGR---PDVLFADEPTgnldrqTG---DKIADLLFSLNR--EHGT 198
Cdd:TIGR00630 811 QTLCD-VGLGYiRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPT------TGlhfDDIKKLLEVLQRlvDKGN 883
|
....*..
gi 496059485 199 TLILVTH 205
Cdd:TIGR00630 884 TVVVIEH 890
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
146-215 |
3.61e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.62 E-value: 3.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059485 146 QLSGGEQQRVALARAF-----NGRPDVLFaDEPTGNLDRQTGDKIADLLFSLNreHGTTLILVTHDPQLAARCDR 215
Cdd:cd03272 158 QLSGGQKSLVALALIFaiqkcDPAPFYLF-DEIDAALDAQYRTAVANMIKELS--DGAQFITTTFRPELLEVADK 229
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
72-214 |
3.81e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.10 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 72 QALHTMDEEARAQLRARHVG----FVFQSFMLIPTLNALENVELpallrgensgksrDGAKTLLEQLGLGKRLDhlPAQL 147
Cdd:PRK02224 718 EELESMYGDLRAELRQRNVEtlerMLNETFDLVYQNDAYSHIEL-------------DGEYELTVYQKDGEPLE--PEQL 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 148 SGGEQQ------RVA----LARAFNG-RP-DVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLIL-VTHDPQLAARCD 214
Cdd:PRK02224 783 SGGERAlfnlslRCAiyrlLAEGIEGdAPlPPLILDEPTVFLDSGHVSQLVDLVESM-RRLGVEQIVvVSHDDELVGAAD 861
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
144-205 |
4.82e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 4.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059485 144 PA-QLSGGEQQRVALARAFNGRPD-----VLfaDEPTgnldrqTG---DKIADLLFSLNR--EHGTTLILVTH 205
Cdd:PRK00349 827 PAtTLSGGEAQRVKLAKELSKRSTgktlyIL--DEPT------TGlhfEDIRKLLEVLHRlvDKGNTVVVIEH 891
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
145-217 |
7.23e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 37.26 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059485 145 AQLSGGEQQRVALARAF----------NGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDPQLAARCD 214
Cdd:TIGR00618 949 ATLSGGETFLASLSLALaladllstsgGTVLDSLFIDEGFGSLDEDSLDRAIGILDAI-REGSKMIGIISHVPEFRERIP 1027
|
...
gi 496059485 215 RRL 217
Cdd:TIGR00618 1028 HRI 1030
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
147-214 |
7.84e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 37.19 E-value: 7.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059485 147 LSGGEQQ------RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL-FSLNREHGT-TLILVTHDPQLAARCD 214
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIeYSLKDSSDIpQVIMISHHRELLSVAD 877
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
35-68 |
8.08e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.22 E-value: 8.08e-03
10 20 30
....*....|....*....|....*....|....
gi 496059485 35 RAETIALIGESGSGKSTLLAILAGLDDGTSGEVS 68
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
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|
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