|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-228 |
4.70e-154 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 426.50 E-value: 4.70e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEE 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ERAKLRAQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARA 160
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 161 FCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKEES 228
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEEA 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-228 |
5.81e-133 |
|
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: 373.31 E-value: 5.81e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEE 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 RAKLRAQHVGFVFQSFMLIPTLNALENVQLPALLKGESEkhSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAF 161
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 162 CTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKEES 228
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDT 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-228 |
4.69e-115 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 327.77 E-value: 4.69e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERA 83
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 84 KLRAQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCT 163
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 164 QPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKEES 228
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-224 |
8.24e-103 |
|
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: 296.32 E-value: 8.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLR 86
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQL 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 |
8.70e-86 |
|
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: 253.43 E-value: 8.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKL 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RAQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQP 165
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKE 226
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-226 |
4.27e-70 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 213.76 E-value: 4.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKL 85
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RaQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQP 165
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLFSLNRdYATTLILVTHDNELAARCQRR-LRLVDGQLKE 226
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRvLELEDGRLVR 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-227 |
5.80e-65 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 201.20 E-value: 5.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEE 81
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 RAKLRAQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAF 161
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493580923 162 CTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
4.19e-61 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 191.84 E-value: 4.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEK-VLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmne 79
Cdd:COG1116 1 MSAAApALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 80 eeraklRAQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALAR 159
Cdd:COG1116 78 ------PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493580923 160 AFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-224 |
8.10e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 191.04 E-value: 8.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 5 KVLEVHQLTKQVGEGDSqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAK 84
Cdd:COG3638 1 PMLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 85 LRAQhVGFVFQSFMLIPTLNALENV------QLP---ALLKGESEKHsYARAVDLLKQLGLGERLYHMPAQLSGGEQQRV 155
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLSVLTNVlagrlgRTStwrSLLGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 156 ALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-223 |
9.17e-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: 187.07 E-value: 9.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKL 85
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RaQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQP 165
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLFSLNRdYATTLILVTHDNELAARCQRR-LRLVDGQ 223
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRvIILDDGR 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-224 |
1.02e-58 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 195.71 E-value: 1.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLR 86
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHDNELAARCQRRLRLVDGQL 224
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-227 |
1.60e-57 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 181.94 E-value: 1.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaKL 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RAQHVGFVFQSFM--LIPTLNALENVQLPALLKGESEKHSYARAV--DLLKQLGLGERLYHM-PAQLSGGEQQRVALARA 160
Cdd:cd03257 80 RRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAvlLLLVGVGLPEEVLNRyPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 161 FCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-206 |
3.88e-57 |
|
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: 180.75 E-value: 3.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmneeeraklR 86
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
12-219 |
2.15e-56 |
|
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: 178.19 E-value: 2.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 12 LTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVG 91
Cdd:TIGR03608 4 ISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 92 FVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFAD 171
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493580923 172 EPTGNLDRKTGDKIADLLFSLNrDYATTLILVTHDNELAARCQRRLRL 219
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELN-DEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-227 |
5.88e-56 |
|
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: 178.16 E-value: 5.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKL 85
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RaQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQP 165
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
6-225 |
4.55e-55 |
|
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: 175.21 E-value: 4.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKL 85
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RaQHVGFVFQSFMLIPTLNALENVQLPA-LLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQ 164
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLK 225
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-206 |
9.62e-55 |
|
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: 175.17 E-value: 9.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQVGegdSQIsILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEE 81
Cdd:COG1127 1 MSEPMIEVRNLTKSFG---DRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 RAKLRaQHVGFVFQSFMLIPTLNALENVQLPalLK-----GESEKHsyARAVDLLKQLGLGERLYHMPAQLSGGEQQRVA 156
Cdd:COG1127 77 LYELR-RRIGMLFQGGALFDSLTVFENVAFP--LRehtdlSEAEIR--ELVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493580923 157 LARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHD 201
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-206 |
6.53e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 172.87 E-value: 6.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkMNEEERAKL 85
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RaQHVGFVFQSFMLIPTLNALENVQL-PALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQ 164
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493580923 165 PAILFADEPTGNLD-RKTGDkIADLLFSLNRDyATTLILVTHD 206
Cdd:COG1126 155 PKVMLFDEPTSALDpELVGE-VLDVMRDLAKE-GMTMVVVTHE 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-212 |
6.86e-54 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 171.93 E-value: 6.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDsqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklr 86
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03259 73 --NIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR 212
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALA 196
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-227 |
2.06e-53 |
|
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: 171.91 E-value: 2.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMneeeRAKLR 86
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR----RRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQSFMLipTLNALENVQ----LPALLKGESEKHsyARAVDLLKQLGLGERLYHM-PAQLSGGEQQRVALARAF 161
Cdd:COG1124 78 RRRVQMVFQDPYA--SLHPRHTVDrilaEPLRIHGLPDRE--ERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 162 CTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEE 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-206 |
6.42e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 173.75 E-value: 6.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklr 86
Cdd:COG3842 6 LELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:COG3842 78 --NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-224 |
1.31e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.46 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDsqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLR 86
Cdd:COG4619 1 LELEGLSFRVGGKP----ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQhVGFVFQ-SFMLIPTLnaLENVQLPALLKGEseKHSYARAVDLLKQLGLGERLYHMPA-QLSGGEQQRVALARAFCTQ 164
Cdd:COG4619 74 RQ-VAYVPQePALWGGTV--RDNLPFPFQLRER--KFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-224 |
1.38e-52 |
|
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: 168.74 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLR 86
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNrDYATTLILVTHDNELAARCQRR-LRLVDGQL 224
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRvIALERGKL 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-224 |
1.04e-51 |
|
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: 167.29 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLR 86
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDL-LKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQP 165
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD-NELAARCQRRLRLVDGQL 224
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-223 |
1.30e-51 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 166.97 E-value: 1.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLR 86
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQLPAL--------LKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALA 158
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493580923 159 RAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQ 223
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGR 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-215 |
8.76e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 168.02 E-value: 8.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MStekvLEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkmnee 80
Cdd:COG1118 1 MS----IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 erAKLRAQ--HVGFVFQSFMLIPTLNALENVQ--LPALLKGESEKHsyARAVDLLK--QL-GLGERLyhmPAQLSGGEQQ 153
Cdd:COG1118 68 --TNLPPRerRVGFVFQHYALFPHMTVAENIAfgLRVRPPSKAEIR--ARVEELLElvQLeGLADRY---PSQLSGGQRQ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493580923 154 RVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQR 215
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADR 203
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-227 |
1.30e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 167.56 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLR 86
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:COG1135 82 -RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-224 |
1.70e-50 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 164.39 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGDSqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKL 85
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RaQHVGFVFQSFMLIPTLNALENVQLPAL--------LKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVAL 157
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGRLgykptwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 158 ARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEI 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-206 |
3.71e-50 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 162.70 E-value: 3.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmNEEERAKLR 86
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQL-PALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQP 165
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHD 206
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHE 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-227 |
4.01e-50 |
|
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: 170.47 E-value: 4.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQ-VGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEE 80
Cdd:COG1123 256 AAEPLLEVRNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ERAKLRaQHVGFVFQ--SFMLIPTLNALENVQLPA-LLKGESEKHSYARAVDLLKQLGLGERLYH-MPAQLSGGEQQRVA 156
Cdd:COG1123 336 SLRELR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 157 LARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVED 486
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
1.85e-48 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 165.85 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTKQVGEGDsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGS---TGSVKLMGEDLTKMNEe 80
Cdd:COG1123 2 TPLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 eraKLRAQHVGFVFQSFM--LIPtLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALA 158
Cdd:COG1123 79 ---ALRGRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 159 RAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVED 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-223 |
2.34e-47 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 154.27 E-value: 2.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeEERAKLR 86
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQLPallkgesekhsyaravdllkqlglgerlyhmpaqLSGGEQQRVALARAFCTQPA 166
Cdd:cd03229 76 -RRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQ 223
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-206 |
1.23e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 157.54 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTekvLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEE 80
Cdd:COG3839 1 MAS---LELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ERaklraqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARA 160
Cdd:COG3839 74 DR------NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493580923 161 FCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-223 |
5.61e-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: 151.85 E-value: 5.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 8 EVHQLTKQVGEGDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKlra 87
Cdd:cd03225 1 ELKNLSFSYPDGARPA--LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 88 qHVGFVFQS-----FMliPTLN-----ALENVQLPallkgesEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVAL 157
Cdd:cd03225 76 -KVGLVFQNpddqfFG--PTVEeevafGLENLGLP-------EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 158 ARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHDNELAAR-CQRRLRLVDGQ 223
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-215 |
1.37e-45 |
|
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: 154.06 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDG---STGSVKLMGEDLTKMNEEER 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 83 AKLRAQHVGFVFQSFM--LIPTLNALENVQLPALL-KGESEKHSYARAVDLLKQLGL---GERLYHMPAQLSGGEQQRVA 156
Cdd:COG0444 81 RKIRGREIQMIFQDPMtsLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 157 LARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQR 215
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADR 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-215 |
3.00e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.60 E-value: 3.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmneeERAKLR 86
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHD-NELAARCQR 215
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYlEEAERLCDR 200
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-224 |
8.96e-45 |
|
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: 150.49 E-value: 8.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVGFVFQSFMLIPTLNA 105
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKI 185
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493580923 186 ADLLFSLNRDYATTLILVTHDNELAARCQRRLRLV-DGQL 224
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMkDGRL 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-227 |
2.75e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.11 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 8 EVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRa 87
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 88 QHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAI 167
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 168 LFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQ 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
25-224 |
5.95e-44 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 147.09 E-value: 5.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeeRAKLRaQHVGFVFQS-----FMl 99
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELR-RKVGLVFQNpddqlFA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 100 iPTLN-----ALENVQLPallkgESEKHsyARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:COG1122 91 -PTVEedvafGPENLGLP-----REEIR--ERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493580923 175 GNLDRKTGDKIADLLFSLNRDyATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:COG1122 163 AGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-211 |
2.10e-43 |
|
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: 145.94 E-value: 2.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDsqisiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklr 86
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03299 72 --DISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAA 211
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAW 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-222 |
6.07e-43 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 144.85 E-value: 6.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAkL 85
Cdd:PRK09493 1 MIEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RaQHVGFVFQSFMLIPTLNALENVQL-PALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQ 164
Cdd:PRK09493 76 R-QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHDNELAARCQRRLRLVDG 222
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-210 |
5.54e-42 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 141.99 E-value: 5.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklr 86
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03300 73 --PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELA 210
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEA 194
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-210 |
5.79e-42 |
|
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: 142.48 E-value: 5.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklr 86
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYA----RAVDLLK--QL-GLGERLyhmPAQLSGGEQQRVALAR 159
Cdd:cd03296 75 --NVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAeiraKVHELLKlvQLdWLADRY---PAQLSGGQRQRVALAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493580923 160 AFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELA 210
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEA 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-226 |
1.24e-41 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 141.16 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDG-----STGSVKLMGEDLTKMNEEe 81
Cdd:cd03260 1 IELRDLNVYYGD----KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 RAKLRAQhVGFVFQSFMLIPtLNALENVQLPALLKGESEKHSYARAV-DLLKQLGLGERLYH--MPAQLSGGEQQRVALA 158
Cdd:cd03260 76 VLELRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVeEALRKAALWDEVKDrlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 159 RAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYatTLILVTHDNELAARCQRR-LRLVDGQLKE 226
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRtAFLLNGRLVE 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-174 |
2.27e-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: 138.16 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKlraqHVGFVFQSFMLIPTLNA 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493580923 106 LENVQLPALLKGESEKHSYARAVDLLKQLGLG----ERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-210 |
3.17e-41 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 140.32 E-value: 3.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMneeeraKLR 86
Cdd:TIGR00968 1 IEIANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRV------HAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLK--QL-GLGERlyhMPAQLSGGEQQRVALARAFCT 163
Cdd:TIGR00968 71 DRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLElvQLeGLGDR---YPNQLSGGQRQRVALARALAV 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493580923 164 QPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELA 210
Cdd:TIGR00968 148 EPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEA 194
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-224 |
4.06e-41 |
|
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: 140.56 E-value: 4.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMneeeRAKL 85
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL----SRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RAQHVGFVFQSFMLIPTLNALENVQL---P--ALLKGESEkHSYARAVDLLKQLGLG---ERLYHmpaQLSGGEQQRVAL 157
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRELVALgryPhlGLFGRPSA-EDREAVEEALERTGLEhlaDRPVD---ELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493580923 158 ARAFCTQPAILFADEPTGNLDrktgdkIA------DLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLD------LAhqlevlELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRI 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-224 |
4.96e-40 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 136.93 E-value: 4.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQhVGFVFQSFMLIPTLNA 105
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKI 185
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493580923 186 ADLLFSLNRdYATTLILVTHDNEL-AARCQRRLRLVDGQL 224
Cdd:PRK10908 177 LRLFEEFNR-VGVTVLMATHDIGLiSRRSYRMLTLSDGHL 215
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
7-210 |
8.96e-40 |
|
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: 139.79 E-value: 8.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklr 86
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGL--GERLYhmPAQLSGGEQQRVALARAFCTQ 164
Cdd:TIGR03265 77 --DYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLpgSERKY--PGQLSGGQQQRVALARALATS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELA 210
Cdd:TIGR03265 153 PGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEA 198
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-210 |
1.27e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 136.92 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTekvLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEE 80
Cdd:COG4525 1 MSM---LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 EraklraqhvGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARA 160
Cdd:COG4525 78 R---------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493580923 161 FCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELA 210
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-223 |
3.59e-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: 134.87 E-value: 3.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTekVLEVHQLTKQV---GEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGE----D 73
Cdd:COG4778 1 MTT--LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 74 LTKMNEEERAKLRAQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHM-PAQLSGGEQ 152
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 153 QRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHDNELAAR-CQRRLRLVDGQ 223
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-206 |
6.53e-39 |
|
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: 134.78 E-value: 6.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKL 85
Cdd:COG0411 4 LLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 raqhvGFV--FQSFMLIPTLNALENVQLPALLKG---------------ESEKHSYARAVDLLKQLGLGERLYHMPAQLS 148
Cdd:COG0411 80 -----GIArtFQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 149 GGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-219 |
2.01e-38 |
|
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: 132.22 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERakl 85
Cdd:COG4133 2 MLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 raQHVGFVFQSFMLIPTLNALENVQLPALLKGESekHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQP 165
Cdd:COG4133 75 --RRLAYLGHADGLKPELTVRENLRFWAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLfslnRDYA---TTLILVTHDnELAARCQRRLRL 219
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELI----AAHLargGAVLLTTHQ-PLELAAARVLDL 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
2.19e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.29 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTkqVGEGDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmnee 80
Cdd:COG1121 1 MMMMPAIELENLT--VSYGGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 eraklRAQHVGFVFQSFMLIPT--LNALENVQLPA-----LLKGESEKHsYARAVDLLKQLGLGERLYHMPAQLSGGEQQ 153
Cdd:COG1121 73 -----ARRRIGYVPQRAEVDWDfpITVRDVVLMGRygrrgLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 154 RVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRdYATTLILVTHD-NELAARCQRRLRLVDGQL 224
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-210 |
2.30e-38 |
|
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: 135.31 E-value: 2.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 41 LIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklraqHVGFVFQSFMLIPTLNALENVQLPALLKGESE 120
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR------HINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 121 KHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTL 200
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170
....*....|
gi 493580923 201 ILVTHDNELA 210
Cdd:TIGR01187 155 VFVTHDQEEA 164
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-210 |
2.90e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 135.98 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklr 86
Cdd:PRK10851 3 IEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYA----RAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFC 162
Cdd:PRK10851 75 --KVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAaikaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493580923 163 TQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELA 210
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-222 |
4.13e-38 |
|
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: 132.42 E-value: 4.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLR 86
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQL-PALLKGESEKHSyARAVDLLKQLGLGERLY--HMPAQLSGGEQQRVALARAFCT 163
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENIALvPKLLKWPKEKIR-ERADELLALVGLDPAEFadRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 164 QPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDG 222
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
25-227 |
4.31e-38 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 139.97 E-value: 4.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeeRAKLRaQHVGFVFQSFMLIP-TL 103
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR-RQIGVVLQDVFLFSgTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 naLENVQLpallkgESEKHSYARAVDLLKQLGLGERLYHMP-----------AQLSGGEQQRVALARAFCTQPAILFADE 172
Cdd:COG2274 566 --RENITL------GDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 173 PTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-206 |
6.25e-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: 131.22 E-value: 6.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklr 86
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03301 73 --DIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-223 |
8.05e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.42 E-value: 8.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 31 LVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAklraqhVGFVFQSFMLIPTLNALENVQ 110
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP------VSMLFQENNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 111 L---PALLKGESEKhsyARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIAD 187
Cdd:COG3840 94 LglrPGLKLTAEQR---AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 493580923 188 LLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQ 223
Cdd:COG3840 171 LVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGR 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-206 |
9.39e-38 |
|
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: 137.51 E-value: 9.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKS-TLLGIIAGLDDGS---TGSVKLMGEDLTK 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 77 MNEEERAKLRAQHVGFVFQSFMlipT-LNALENV--QLP---ALLKGESEKHSYARAVDLLKQLGLGE---RLYHMPAQL 147
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPM---TsLNPLHTIgkQIAevlRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 148 SGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD 216
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-206 |
1.45e-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: 132.91 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 8 EVHQLTKQVGEGDSqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLRa 87
Cdd:COG1125 3 EFENVTKRYPDGTV---AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 88 QHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYH--MPAQLSGGEQQRVALARAFCTQP 165
Cdd:COG1125 76 RRIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEYRdrYPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG1125 156 PILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHD 196
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-222 |
2.08e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 131.03 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQV-GEgdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLmGE---DLTKMNEEER 82
Cdd:PRK11264 4 IEVKNLVKKFhGQ-----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDitiDTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 83 AKLRA--QHVGFVFQSFMLIPTLNALENV-QLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALAR 159
Cdd:PRK11264 78 GLIRQlrQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493580923 160 AFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHDNELAARCQRRLRLVDG 222
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQ 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-226 |
3.48e-37 |
|
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: 136.43 E-value: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTkqVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLR 86
Cdd:COG4987 334 LELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIP-TLnaLENVQL--PALlkgesekhSYARAVDLLKQLGLGERLYHMP-----------AQLSGGEQ 152
Cdd:COG4987 409 -RRIAVVPQRPHLFDtTL--RENLRLarPDA--------TDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493580923 153 QRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLRLVDGQLKE 226
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
25-210 |
1.48e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 128.59 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDL---TKMNEEERAKLRaQHVGFVFQSFMLIP 101
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLR-QKVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 102 TLNALEN-VQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRK 180
Cdd:COG4161 96 HLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190
....*....|....*....|....*....|
gi 493580923 181 TGDKIADLLFSLNrDYATTLILVTHDNELA 210
Cdd:COG4161 176 ITAQVVEIIRELS-QTGITQVIVTHEVEFA 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-206 |
4.96e-36 |
|
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: 126.78 E-value: 4.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLR 86
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqhVGFVFQSFMLIPTLNALENVQLPALLKG----------ESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVA 156
Cdd:cd03219 77 ---IGRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493580923 157 LARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHD 206
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHD 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-224 |
5.59e-36 |
|
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: 124.82 E-value: 5.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDsqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmneeERAKLR 86
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVqlpallkgesekhsyaravdllkqlglgerlyhmpaQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHD-NELAARCQRRLRLVDGQL 224
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-224 |
5.96e-36 |
|
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: 124.86 E-value: 5.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 8 EVHQLTKQVGEGDsqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeerAKLRA 87
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----PKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 88 QHVGFVFQsfmliptlnALENVQLpallkgesekhsyaravdllkqLGLGERLYHmpaQLSGGEQQRVALARAFCTQPAI 167
Cdd:cd03214 73 RKIAYVPQ---------ALELLGL----------------------AHLADRPFN---ELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 168 LFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
25-223 |
7.13e-36 |
|
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: 124.42 E-value: 7.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLRaQHVGFVFQSFMLIP-TL 103
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LR-KNIAYVPQDPFLFSgTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 naLENVqlpallkgesekhsyaravdllkqlglgerlyhmpaqLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGD 183
Cdd:cd03228 93 --RENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493580923 184 KIADLLFSLNRDyaTTLILVTHDNELAARCQRRLRLVDGQ 223
Cdd:cd03228 134 LILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-227 |
1.89e-35 |
|
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: 125.74 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERakl 85
Cdd:COG4555 1 MIEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 raQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQP 165
Cdd:COG4555 74 --RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHD-NELAARCQRRLRLVDGQLKEE 227
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHImQEVEALCDRVVILHKGKVVAQ 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-206 |
1.92e-35 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 126.07 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGE----------DLT 75
Cdd:COG4598 8 ALEVRDLHKSFGD----LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 76 KMNEEERAKLRAQhVGFVFQSFMLIPTLNALENV-QLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQR 154
Cdd:COG4598 84 PADRRQLQRIRTR-LGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 155 VALARAFCTQPAILFADEPTGNLDRKTgdkIADLLfSLNRDYAT---TLILVTHD 206
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPEL---VGEVL-KVMRDLAEegrTMLVVTHE 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-223 |
5.35e-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: 121.97 E-value: 5.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 8 EVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKlra 87
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 88 qHVGFVFQsfmliptlnalenvqlpallkgesekhsyaravdllkqlglgerlyhmpaqLSGGEQQRVALARAFCTQPAI 167
Cdd:cd00267 74 -RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 168 LFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHDNELAAR-CQRRLRLVDGQ 223
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-224 |
8.41e-35 |
|
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: 123.17 E-value: 8.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 35 SAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVGFVFQSFMLIPTLNALENVQLPal 114
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 115 LKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNR 194
Cdd:cd03297 100 LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|.
gi 493580923 195 DYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
26-210 |
1.36e-34 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 125.96 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAklraqhVGFVFQSFMLIPTLNA 105
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG------IAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKI 185
Cdd:NF040840 90 FENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180
....*....|....*....|....*
gi 493580923 186 ADLLFSLNRDYATTLILVTHDNELA 210
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTHNFEEA 194
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-224 |
4.37e-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: 122.95 E-value: 4.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRaQHVGFVFQsfmlIPtlna 105
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQ----FP---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 lENvQLPAL--LK---------GESEKHSYARAVDLLKQLGLGERLYHM-PAQLSGGEQQRVALARAFCTQPAILFADEP 173
Cdd:TIGR04521 92 -EH-QLFEEtvYKdiafgpknlGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVLAMEPEVLILDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493580923 174 TGNLDRKTGDKIADLLFSLNRDYATTLILVTHD-NELAARCQRRLRLVDGQL 224
Cdd:TIGR04521 170 TAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKI 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
25-227 |
4.45e-34 |
|
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: 127.95 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEEraklRAQHVGFVFQSFMLIP-TL 103
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS----WRRQIAWVPQNPYLFAgTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 naLENVQLPALLKGESEKHSYARAV---DLLKQLGLGerlYHMP-----AQLSGGEQQRVALARAFCTQPAILFADEPTG 175
Cdd:COG4988 428 --RENLRLGRPDASDEELEAALEAAgldEFVAALPDG---LDTPlgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493580923 176 NLDRKTGDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:COG4988 503 HLDAETEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-224 |
5.44e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 122.09 E-value: 5.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklr 86
Cdd:PRK11247 13 LLLNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqhvgFVFQSFMLIPTLNALENVQLPalLKGesekHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:PRK11247 85 -----LMFQDARLLPWKKVIDNVGLG--LKG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD-NELAARCQRRLRLVDGQL 224
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-210 |
8.68e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 124.29 E-value: 8.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTKQVGEGDsqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEE 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ERaklraqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARA 160
Cdd:PRK09452 85 NR------HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493580923 161 FCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELA 210
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEA 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-225 |
1.45e-33 |
|
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: 119.67 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 22 QISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVGFvfQSFMlip 101
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDY--QLFT--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 102 tlnalENVQLPALLKGESEKHSYARAVDLLKQLGL-GERLYHmPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRK 180
Cdd:cd03226 87 -----DSVREELLLGLKELDAGNEQAETVLKDLDLyALKERH-PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493580923 181 TGDKIADLLFSLNRDyATTLILVTHDNELAAR-CQRRLRLVDGQLK 225
Cdd:cd03226 161 NMERVGELIRELAAQ-GKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-221 |
1.70e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.51 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAG-LDDG--STGSVKLMGEDLTKMNEEERa 83
Cdd:COG4136 2 LSLENLTITLG----GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 84 klraqHVGFVFQSFMLIPTLNALENVQ--LPALLKGESEKhsyARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAF 161
Cdd:COG4136 77 -----RIGILFQDDLLFPHLSVGENLAfaLPPTIGRAQRR---ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 162 CTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVD 221
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-221 |
1.90e-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: 119.52 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 31 LVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAklraqhVGFVFQSFMLIPTLNALENVQ 110
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 111 L---PALLKGESEKHSYARAvdlLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIAD 187
Cdd:cd03298 93 LglsPGLKLTAEDRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....
gi 493580923 188 LLFSLNRDYATTLILVTHDNELAARCQRRLRLVD 221
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-225 |
3.56e-33 |
|
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: 119.15 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmneeERAKLR 86
Cdd:cd03263 1 LQIRNLTKTYKKGTKPA--VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHD-NELAARCQRRLRLVDGQLK 225
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSmDEAEALCDRIAIMSDGKLR 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-206 |
4.71e-33 |
|
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: 119.11 E-value: 4.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAklraqhvgfVFQSFMLIPTLNA 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVQL------PALLKGESEkhsyARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDR 179
Cdd:TIGR01184 72 RENIALavdrvlPDLSKSERR----AIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180
....*....|....*....|....*..
gi 493580923 180 KTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRVTVLMVTHD 174
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-210 |
6.62e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.96 E-value: 6.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 19 GDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGE--DL-TKMNEEERAKLRaQHVGFVFQ 95
Cdd:PRK11124 13 GAHQA--LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFsKTPSDKAIRELR-RNVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 96 SFMLIPTLNALEN-VQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:PRK11124 90 QYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 493580923 175 GNLDRKTGDKIADLLFSLnRDYATTLILVTHDNELA 210
Cdd:PRK11124 170 AALDPEITAQIVSIIREL-AETGITQVIVTHEVEVA 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-203 |
7.40e-33 |
|
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: 118.31 E-value: 7.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLtkQVGEGDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLr 86
Cdd:cd03224 1 LEVENL--NAGYGKSQI--LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqHVGFVFQSFMLIPTLNALENVQLPA-LLKGESEKHSYARAVDLLKQlgLGERLYHMPAQLSGGEQQRVALARAFCTQP 165
Cdd:cd03224 76 --GIGYVPEGRRIFPELTVEENLLLGAyARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILV 203
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLV 188
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-224 |
8.86e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.11 E-value: 8.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKL 85
Cdd:PRK13548 2 MLEARNLSVRLG----GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RA---QH--VGFVFqsfmliptlNALENVQLPALLKGESEKH------SYARAVDLlkqLGLGERLYHmpaQLSGGEQQR 154
Cdd:PRK13548 78 RAvlpQHssLSFPF---------TVEEVVAMGRAPHGLSRAEddalvaAALAQVDL---AHLAGRDYP---QLSGGEQQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 155 VALARAFC------TQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:PRK13548 143 VQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-210 |
6.54e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 116.72 E-value: 6.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEEraklraqhvGFVFQSFMLIPTLN 104
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDK 184
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*.
gi 493580923 185 IADLLFSLNRDYATTLILVTHDNELA 210
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-227 |
6.66e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 118.31 E-value: 6.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDD--GSTGSVKLM--GEDLTKMNEEE 81
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypGRVMAEKLEfnGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 RAKLRAQHVGFVFQSFMliPTLNALENV--QLPALLK---GESEKHSYARAVDLLKQLGL---GERLYHMPAQLSGGEQQ 153
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPM--TSLNPCYTVgfQIMEAIKvhqGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 154 RVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVET 235
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-227 |
2.32e-31 |
|
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: 115.67 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEG-----DSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEE 80
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ERAKLRaQHVGFVFQSFM--LIPTLNALENVQLPAL-LKGESEKHSYARAVDLLKQLGL-GERLYHMPAQLSGGEQQRVA 156
Cdd:TIGR02769 82 QRRAFR-RDVQLVFQDSPsaVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 157 LARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-206 |
2.52e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 115.57 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEG-DSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKl 85
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 raqHVGFVFQSFML--IPTLNALENVQLpALLKGesEKHSYARAV---------DLLKQLGLG--ERLYHMPAQLSGGEQ 152
Cdd:COG1101 81 ---YIGRVFQDPMMgtAPSMTIEENLAL-AYRRG--KRRGLRRGLtkkrrelfrELLATLGLGleNRLDTKVGLLSGGQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493580923 153 QRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
26-227 |
5.59e-31 |
|
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: 114.31 E-value: 5.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDD-----GSTGSVKLMGEDLT--KMNEEErakLRAqHVGFVFQSFM 98
Cdd:TIGR00972 17 LKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYdkKIDVVE---LRR-RVGMVFQKPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 99 LIPtLNALENVQLPALLKGESEKHSY-ARAVDLLKQLGLGE----RLYHMPAQLSGGEQQRVALARAFCTQPAILFADEP 173
Cdd:TIGR00972 93 PFP-MSIYDNIAYGPRLHGIKDKKELdEIVEESLKKAALWDevkdRLHDSALGLSGGQQQRLCIARALAVEPEVLLLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 174 TGNLDRKTGDKIADLLFSLNRDYatTLILVTHDNELAARC-QRRLRLVDGQLKEE 227
Cdd:TIGR00972 172 TSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARIsDRTAFFYDGELVEY 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
40-206 |
6.70e-31 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 116.35 E-value: 6.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 40 ALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVGFVFQSFMLIPTLNALENVQ--LPALLKG 117
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEARLFPHLSVRGNLLygRKRAPRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 118 ESeKHSYARAVDLLkqlGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYA 197
Cdd:COG4148 109 ER-RISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELD 184
|
....*....
gi 493580923 198 TTLILVTHD 206
Cdd:COG4148 185 IPILYVSHS 193
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-227 |
7.60e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.40 E-value: 7.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQ------VGEGDSQiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEE 80
Cdd:PRK10419 4 LNVSGLSHHyahgglSGKHQHQ-TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ERAKLRaQHVGFVFQSfmLIPTLNALENVQ------LPALLkGESEKHSYARAVDLLKQLGLG-ERLYHMPAQLSGGEQQ 153
Cdd:PRK10419 83 QRKAFR-RDIQMVFQD--SISAVNPRKTVReiirepLRHLL-SLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 154 RVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVET 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
25-206 |
1.50e-30 |
|
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: 112.24 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEeeraklraqHVGFVFQSFMLIPT-- 102
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK---------RIGYVPQRRSIDRDfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 103 LNALENVQLPA-----LLKGESEKHsYARAVDLLKQLGLGErLYHMP-AQLSGGEQQRVALARAFCTQPAILFADEPTGN 176
Cdd:cd03235 85 ISVRDVVLMGLyghkgLFRRLSKAD-KAKVDEALERVGLSE-LADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190
....*....|....*....|....*....|
gi 493580923 177 LDRKTGDKIADLLFSLNRDyATTLILVTHD 206
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTHD 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-227 |
2.36e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 111.52 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDsqisILQGVELVVESAQTiALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklr 86
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHDNE-LAARCQRRLRLVDGQLKEE 227
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEdVESLCNQVAVLNKGKLVFE 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-210 |
2.87e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 112.75 E-value: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 3 TEKVLEVHQLTKQVGEGDsqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLT------- 75
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 76 --KMNEEERAKLRAQHVGFVFQSFMLIPTLNALENV-QLPALLKGESEKHSYARAVDLLKQLGLGERLY-HMPAQLSGGE 151
Cdd:PRK10619 78 qlKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 152 QQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHDNELA 210
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFA 215
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-213 |
4.53e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.05 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTkqVGEGDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDD---GS--TGSVKLMGEDL-- 74
Cdd:COG1117 7 TLEPKIEVRNLN--VYYGDKQA--LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipGArvEGEILLDGEDIyd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 75 TKMNEEErakLRAQhVGFVFQsfmlipTLNAL-----ENVQLPALLKGESEKHSYARAV-DLLKQLGLGE----RLyHMP 144
Cdd:COG1117 83 PDVDVVE---LRRR-VGMVFQ------KPNPFpksiyDNVAYGLRLHGIKSKSELDEIVeESLRKAALWDevkdRL-KKS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 145 AQ-LSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYatTLILVTHDNELAARC 213
Cdd:COG1117 152 ALgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARV 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-224 |
4.70e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 112.03 E-value: 4.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTKQVgegdSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGL---DDGSTGSVKLMGEDLTKMNEE 80
Cdd:PRK09984 2 QTIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ER--AKLRAqHVGFVFQSFMLIPTLNALENVQLPALlkGES----------EKHSYARAVDLLKQLGLGERLYHMPAQLS 148
Cdd:PRK09984 78 ARdiRKSRA-NTGYIFQQFNLVNRLSVLENVLIGAL--GSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 149 GGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-227 |
6.09e-30 |
|
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: 111.75 E-value: 6.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 20 DSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtkMNEEERAKLRaQHVGFVFQ---- 95
Cdd:TIGR04520 12 ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIR-KKVGMVFQnpdn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 96 -----------SFmliptlnALENVQLPAllkGESEKhsyaRAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQ 164
Cdd:TIGR04520 89 qfvgatveddvAF-------GLENLGVPR---EEMRK----RVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-227 |
7.85e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.16 E-value: 7.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGL-----DDGSTGSVKLMGEDLTKMNEE 80
Cdd:PRK14247 3 KIEIRDLKVSFG----QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ErakLRaQHVGFVFQSFMLIPTLNALENVQLPALLK--GESEKHSYARAVDLLKQLGLGE----RLYHMPAQLSGGEQQR 154
Cdd:PRK14247 79 E---LR-RRVQMVFQIPNPIPNLSIFENVALGLKLNrlVKSKKELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493580923 155 VALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLR-LVDGQLKEE 227
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAfLYKGQIVEW 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-219 |
1.50e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 115.08 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeerAKLRAQHVGFVFQS-FMLIPTLn 104
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHpFLFAGTI- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 aLENVQL------PALLKGESEKHSYARAVDLLKQlGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:TIGR02857 413 -AENIRLarpdasDAEIREALERAGLDEFVAALPQ-GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493580923 179 RKTGdkiADLLFSLnRDYAT--TLILVTHDNELAARCQRRLRL 219
Cdd:TIGR02857 491 AETE---AEVLEAL-RALAQgrTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-224 |
1.67e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 108.07 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 19 GDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAklraQHVGFVFQSFM 98
Cdd:cd03246 11 PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG----DHVGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 99 LIP-TLNalENVqlpallkgesekhsyaravdllkqlglgerlyhmpaqLSGGEQQRVALARAFCTQPAILFADEPTGNL 177
Cdd:cd03246 87 LFSgSIA--ENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493580923 178 DRKTGDKIADLLFSLnRDYATTLILVTHDNELAARCQRRLRLVDGQL 224
Cdd:cd03246 128 DVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-224 |
1.93e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 110.21 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLR 86
Cdd:COG4559 2 LEAENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 A---QH--VGFVFqsfmliptlNALENVQL---PALLKGESEKHSYARAVDLLKQLGLGERLYHmpaQLSGGEQQRVALA 158
Cdd:COG4559 78 AvlpQHssLAFPF---------TVEEVVALgraPHGSSAAQDRQIVREALALVGLAHLAGRSYQ---TLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 159 RAFC-------TQPAILFADEPTGNLDrktgdkIAD--LLFSLNRDYA---TTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALD------LAHqhAVLRLARQLArrgGGVVAVLHDLNLAAQyADRILLLHQGRL 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-226 |
2.40e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 111.74 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKS----TLLGIIAGldDGST-GSVKLMGEDLTK 76
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA--NGRIgGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 77 MNEEERAKLRAQHVGFVFQSFMliPTLNALENV--QLPALL---KGESEKHSYARAVDLLKQLGLGE---RLYHMPAQLS 148
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPM--TSLNPYMRVgeQLMEVLmlhKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 149 GGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD-NELAARCQRRLRLVDGQLKE 226
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGRTME 242
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
7-206 |
5.92e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 109.16 E-value: 5.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDS-----QISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeee 81
Cdd:COG4167 5 LEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 rAKLRAQHVGFVFQ--SFMLIPTLNALENVQLPALLKGE-SEKHSYARAVDLLKQLGL-GERLYHMPAQLSGGEQQRVAL 157
Cdd:COG4167 82 -YKYRCKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNTDlTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493580923 158 ARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-227 |
6.28e-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: 113.36 E-value: 6.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGST---------------------- 64
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPtsgriiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 65 ----------GSVKLMGEDLTKMNEEERAKLRaQHVGFVFQ-SFMLIPTLNALENVqLPALLK-GESEKHSYARAVDLLK 132
Cdd:TIGR03269 77 kvgepcpvcgGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNV-LEALEEiGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 133 QLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR 212
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250
....*....|....*.
gi 493580923 213 -CQRRLRLVDGQLKEE 227
Cdd:TIGR03269 235 lSDKAIWLENGEIKEE 250
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-174 |
7.74e-29 |
|
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: 108.15 E-value: 7.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTkqVGEGDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKL 85
Cdd:COG0410 3 MLEVENLH--AGYGGIHV--LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 raqHVGFVFQSFMLIPTLNALENVQLPALLKG--ESEKHSYARAVDLLKQLGlgERLYHMPAQLSGGEQQRVALARAFCT 163
Cdd:COG0410 79 ---GIGYVPEGRRIFPSLTVEENLLLGAYARRdrAEVRADLERVYELFPRLK--ERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170
....*....|.
gi 493580923 164 QPAILFADEPT 174
Cdd:COG0410 154 RPKLLLLDEPS 164
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-226 |
1.67e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.94 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 3 TEKVLEVHQLTKQVGEGDSqisiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDD-----GSTGSVKLMGEDLTKM 77
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKA----LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 78 NEEErAKLRaQHVGFVFQSFMLIPtLNALENVQLPALLKGESEKHSYARAVDL-LKQLGLGE----RLYHMPAQLSGGEQ 152
Cdd:PRK14239 78 RTDT-VDLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKsLKGASIWDevkdRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 153 QRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYatTLILVTHDNELAAR-CQRRLRLVDGQLKE 226
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRiSDRTGFFLDGDLIE 227
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-227 |
1.71e-28 |
|
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: 107.07 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 27 QGVELVVESAQTIALIGESGSGKST----LLGIIAGLDDGSTGSVKLMGEDLTKMneeeraKLRAQHVGFVFQSFM--LI 100
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQNPRtaFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 101 PTLNALENVQLPALLKGESEKHSYARAVDLLKQLGL--GERLYHM-PAQLSGGEQQRVALARAFCTQPAILFADEPTGNL 177
Cdd:TIGR02770 77 PLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLpdPEEVLKKyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493580923 178 DRKTGDKIADLLFSLNRDYATTLILVTHDNELAARC-QRRLRLVDGQLKEE 227
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIaDEVAVMDDGRIVER 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-210 |
1.74e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 110.31 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVgegDSQISIlQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAkl 85
Cdd:PRK11607 19 LLEIRNLTKSF---DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 raqhVGFVFQSFMLIPTLNALENVQL----PALLKGESEkhsyARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAF 161
Cdd:PRK11607 93 ----INMMFQSYALFPHMTVEQNIAFglkqDKLPKAEIA----SRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493580923 162 CTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELA 210
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEA 213
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-228 |
1.98e-28 |
|
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: 106.48 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 30 ELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAklraqhVGFVFQSFMLIPTLNALENV 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 110 QL---PALLKGESEKHsyaRAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIA 186
Cdd:TIGR01277 92 GLglhPGLKLNAEQQE---KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493580923 187 DLLFSLNRDYATTLILVTHD-NELAARCQRRLRLVDGQLKEES 228
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQGKIKVVS 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-206 |
2.46e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.42 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEE 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ERaklraqHVGFVFQSFMLIPTLNALENVQ--LPALLKGESE-KHSYARAVDLLKQLGLGERLYHmpaQLSGGEQQRVAL 157
Cdd:PRK11432 77 QR------DICMVFQSYALFPHMSLGENVGygLKMLGVPKEErKQRVKEALELVDLAGFEDRYVD---QISGGQQQRVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493580923 158 ARAFCTQPAILFADEPTGNLD----RKTGDKIADLLFSLNrdyaTTLILVTHD 206
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDanlrRSMREKIRELQQQFN----ITSLYVTHD 196
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-224 |
2.82e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.59 E-value: 2.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 31 LVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAklraqhVGFVFQSFMLIPTLNALENVQ 110
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP------VSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 111 L---PALLKGESEKHSYAravDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIAD 187
Cdd:PRK10771 94 LglnPGLKLNAAQREKLH---AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 493580923 188 LLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRI 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-204 |
9.57e-28 |
|
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: 105.05 E-value: 9.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 18 EGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGStgsvKLMGEDLTKMNEEERAKLRAQHVGFVFQSF 97
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGG----GTTSGQILFNGQPRKPDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 98 MLIPTLNALENVQLPALLKGESEKHSYAR----AVDLLKQLGLgERLYHMP-AQLSGGEQQRVALARAFCTQPAILFADE 172
Cdd:cd03234 91 ILLPGLTVRETLTYTAILRLPRKSSDAIRkkrvEDVLLRDLAL-TRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|....
gi 493580923 173 PTGNLDRKTgdkiADLLFSLNRDYATT--LILVT 204
Cdd:cd03234 170 PTSGLDSFT----ALNLVSTLSQLARRnrIVILT 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
19-206 |
1.01e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 108.19 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 19 GDSQISilQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVkLMGEdlTKMNEEERAKlraQHVGFVFQSFM 98
Cdd:PRK11000 14 GDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGE--KRMNDVPPAE---RGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 99 LIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190
....*....|....*....|....*....|..
gi 493580923 179 R----KTGDKIADLLFSLNRdyatTLILVTHD 206
Cdd:PRK11000 166 AalrvQMRIEISRLHKRLGR----TMIYVTHD 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
26-206 |
1.24e-27 |
|
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: 109.39 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTL----LGIIAglddgSTGSVKLMGEDLTKMNEEERAKLRaQHVGFVFQ----Sf 97
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQdpfgS- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 98 mLIPTLNALENVQ--LPALLKGESEKHSYARAVDLLKQLGLGERLYH-MPAQLSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:COG4172 375 -LSPRMTVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
170 180 190
....*....|....*....|....*....|..
gi 493580923 175 GNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREHGLAYLFISHD 485
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-220 |
2.03e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.81 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVGFVFQSFMLIPTLNA 105
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKI 185
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190
....*....|....*....|....*....|....*
gi 493580923 186 ADLLFSLNRDYATTLILVTHDNELAARCQRRLRLV 220
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-212 |
2.85e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 104.54 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGL-----DDGSTGSVKLMGEDLtkMNEEERAKLRAQHVGFVFQSFML 99
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDVDPIEVRREVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 100 IPTLNALENV----QLPALLKGESEKHSYARAVdlLKQLGLGE----RLYHMPAQLSGGEQQRVALARAFCTQPAILFAD 171
Cdd:PRK14267 97 FPHLTIYDNVaigvKLNGLVKSKKELDERVEWA--LKKAALWDevkdRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493580923 172 EPTGNLDRKTGDKIADLLFSLNRDYatTLILVTHDNELAAR 212
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAAR 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-206 |
3.65e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.97 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTK--QVGEG-----DSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGED 73
Cdd:COG4608 2 AMAEPLLEVRDLKKhfPVRGGlfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 74 LTKMNEEERAKLRaQHVGFVFQ----SfmLIPTLNALENVQLPALLKGESEKHSY-ARAVDLLKQLGLgeRLYHM---PA 145
Cdd:COG4608 82 ITGLSGRELRPLR-RRMQMVFQdpyaS--LNPRMTVGDIIAEPLRIHGLASKAERrERVAELLELVGL--RPEHAdryPH 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 146 QLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-227 |
8.08e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.56 E-value: 8.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLRaQHVGFVFQSFMLIpTLN 104
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LR-RQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENVQLPAllkgesEKHSYARAVDLLKQLGLGERLYHMP-----------AQLSGGEQQRVALARAFCTQPAILFADEP 173
Cdd:COG1132 430 IRENIRYGR------PDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 174 TGNLDRKTGDKIADLLFSLNRDyATTL--------------ILV----------THDnELAARCQRRLRLVDGQLKEE 227
Cdd:COG1132 504 TSALDTETEALIQEALERLMKG-RTTIviahrlstirnadrILVlddgriveqgTHE-ELLARGGLYARLYRLQFGEE 579
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-205 |
9.67e-27 |
|
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: 101.47 E-value: 9.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGDSQIS--ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGS--TGSVKLMGEDLTKMNeee 81
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSGkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 rakLRAQhVGFVFQSFMLIPTLNALENVQLPALLKGesekhsyaravdllkqlglgerlyhmpaqLSGGEQQRVALARAF 161
Cdd:cd03213 80 ---FRKI-IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALEL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493580923 162 CTQPAILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTH 205
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-221 |
1.43e-26 |
|
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: 102.06 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSqisiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKlr 86
Cdd:cd03265 1 IEVENLVKKYGDFEA----VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqhVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03265 75 ---IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVD 221
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-206 |
1.75e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.33 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKS-TLLGIIAGLDDGS----TGSVKLMGEDLTK 76
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 77 MNEEERAKLRAQHVGFVFQSFMLipTLNALENV--QLPALL---KGESEKHSYARAVDLLKQLGL---GERLYHMPAQLS 148
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMV--SLNPLHTLekQLYEVLslhRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 149 GGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHN 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
25-223 |
1.99e-26 |
|
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: 102.08 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTG-SVKLMGEDLTKMNEEErakLRaQHVGFVFQSFML-IPT 102
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWE---LR-KRIGLVSPALQLrFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 103 LNALENVQLPAL-----LKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNL 177
Cdd:COG1119 94 DETVLDVVLSGFfdsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493580923 178 DRKTGDKIADLLFSLNRDYATTLILVTHDNELAARC-QRRLRLVDGQ 223
Cdd:COG1119 174 DLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-226 |
3.40e-26 |
|
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: 101.83 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTKQVGEGDSqisiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGED-----LTKMN 78
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 79 EEERAKLRAQHVGFVFQSFM--LIPTLNALENVQLPALLKGEseKHS---YARAVDLLKQLGLGE-RLYHMPAQLSGGEQ 152
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRdgLRMRVSAGANIGERLMAIGA--RHYgniRATAQDWLEEVEIDPtRIDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 153 QRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAA-RCQRRLRLVDGQLKE 226
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVVE 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-227 |
3.66e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.40 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 3 TEKVLEVHQLTKQVGEGDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGedlTKMNEEER 82
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYA--LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 83 AKLRAQhVGFVFQ---------------SFmliptlnALENVQLPALLKGEsekhsyaRAVDLLKQLGLGERLYHMPAQL 147
Cdd:PRK13635 77 WDVRRQ-VGMVFQnpdnqfvgatvqddvAF-------GLENIGVPREEMVE-------RVDQALRQVGMEDFLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 148 SGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-228 |
7.90e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 102.88 E-value: 7.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 29 VELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtkmnEEERAKL----RAQHVGFVFQSFMLIPTLN 104
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL----FDSRKGIflppEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENVQLP-ALLKGESEKHSYARAVDLLkqlGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGD 183
Cdd:TIGR02142 92 VRGNLRYGmKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493580923 184 KIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLV-DGQLKEES 228
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLeDGRVAAAG 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-206 |
8.60e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 102.35 E-value: 8.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTK--QVGEG----DSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLT 75
Cdd:PRK11308 1 SQQPLLQAIDLKKhyPVKRGlfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 76 KMNEEERAKLRaQHVGFVFQSfmliP--TLNA-------LE-----NVQLPAllkgeSEKHsyARAVDLLKQLGLGERLY 141
Cdd:PRK11308 81 KADPEAQKLLR-QKIQIVFQN----PygSLNPrkkvgqiLEeplliNTSLSA-----AERR--EKALAMMAKVGLRPEHY 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 142 ----HMpaqLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK11308 149 drypHM---FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-206 |
1.07e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.39 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTKQVGEGDSqisiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGE-----DLT 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 76 KMNEEERAKLRAQHVGFVFQSFM--LIPTLNALENVQLPalLKGESEKHsY----ARAVDLLKQLGLG-ERLYHMPAQLS 148
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQHPRdgLRMQVSAGGNIGER--LMAVGARH-YgdirATAGDWLERVEIDaARIDDLPTTFS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 149 GGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHD 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-224 |
1.32e-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: 99.36 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLr 86
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqhvGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03266 81 ----GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHD-NELAARCQRRLRLVDGQL 224
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHImQEVERLCDRVVVLHRGRV 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-227 |
3.83e-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: 97.00 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEeraklR 86
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQSFMLIPTlnalenvqlpallkgesekhsyaravDLLKQLGlgerlyhmpAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03247 74 SSLISVLNQRPYLFDT--------------------------TLRNNLG---------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-221 |
4.75e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.17 E-value: 4.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 22 QISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmneeERAKLRAQhVGFVF-QSFMLI 100
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK----RRKKFLRR-IGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 101 PTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRK 180
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493580923 181 TGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVD 221
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-212 |
4.84e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.32 E-value: 4.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVGFVFQsfmlIPTLNA 105
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQ----FPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVqlpaLLK---------GESEKHSYARAVDLLKQLGLGER-LYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTG 175
Cdd:PRK13634 99 FEET----VEKdicfgpmnfGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 493580923 176 NLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR 212
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-206 |
5.11e-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: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 9 VHQLTKQVGEGDsqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLmgedltkmneeeRAKLRaq 88
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------------PKGLR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 89 hVGFVFQSFMLIPTLNALENVQ--LPALLKGESEKH------------------------------SYARAVDLLKQLGL 136
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVLdgDAELRALEAELEeleaklaepdedlerlaelqeefealggweAEARAEEILSGLGF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 137 GERLYHMP-AQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLfslnRDYATTLILVTHD 206
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-224 |
6.77e-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: 97.66 E-value: 6.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 20 DSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMneeERAKLRaQHVGFVFQSFML 99
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADLR-RNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 100 IP-TLNalENVQLPALLKGESEKHSYARAVDLLK---------QLGLGERlyhmPAQLSGGEQQRVALARAFCTQPAILF 169
Cdd:cd03245 90 FYgTLR--DNITLGAPLADDERILRAAELAGVTDfvnkhpnglDLQIGER----GRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 170 ADEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLRLVDGQL 224
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-224 |
9.18e-25 |
|
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: 101.42 E-value: 9.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 23 ISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVK-LMGE---DLTKMNEEERAKLRaQHVGFVFQSFM 98
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDewvDMTKPGPDGRGRAK-RYIGILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 99 LIPTLNALEN------VQLPALLkgesekhSYARAVDLLKQLGLGER-----LYHMPAQLSGGEQQRVALARAFCTQPAI 167
Cdd:TIGR03269 376 LYPHRTVLDNlteaigLELPDEL-------ARMKAVITLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 168 LFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKI 506
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-206 |
2.11e-24 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 100.51 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 16 VGEGDSQIsILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLraqhVGFVFQ 95
Cdd:TIGR02868 342 AGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 96 SFMLIPTlNALENVQLPALLKGESEKHSYARAV---DLLKQL--GLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFA 170
Cdd:TIGR02868 417 DAHLFDT-TVRENLRLARPDATDEELWAALERVglaDWLRALpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 493580923 171 DEPTGNLDRKTGDKIADLLFSLNRDYATtlILVTHD 206
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAALSGRTV--VLITHH 529
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
25-224 |
2.65e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 96.98 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLRaQHVGFVFQS----FMLI 100
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE---IR-KKIGIIFQNpdnqFIGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 101 pTLNA-----LENVQLPallkgesEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTG 175
Cdd:PRK13632 100 -TVEDdiafgLENKKVP-------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493580923 176 NLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQL 224
Cdd:PRK13632 172 MLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-223 |
4.58e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.50 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTkqVGEGDSQIsILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLmgedltkmneee 81
Cdd:COG4178 358 SEDGALALEDLT--LRTPDGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR------------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 rakLRAQHVGFVFQ-SFMLIPTLnaLENVQLPAllkgESEKHSYARAVDLLKQLGLG---ERLY---HMPAQLSGGEQQR 154
Cdd:COG4178 423 ---PAGARVLFLPQrPYLPLGTL--REALLYPA----TAEAFSDAELREALEAVGLGhlaERLDeeaDWDQVLSLGEQQR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 155 VALARAFCTQPAILFADEPTGNLDRKTGDKIADLLfsLNRDYATTLILVTHDNELAARCQRRLRLVDGQ 223
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-226 |
5.53e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 5 KVLEVHQLTKqvGEGDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLmGEDLtkmneeerak 84
Cdd:COG0488 314 KVLELEGLSK--SYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 85 lraqHVGFVFQSF-MLIPTLNALENVQlpALLKGESEKHsyarAVDLLKQLGL-GERLYHMPAQLSGGEQQRVALARAFC 162
Cdd:COG0488 379 ----KIGYFDQHQeELDPDKTVLDELR--DGAPGGTEQE----VRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 163 TQPAILFADEPTGNLDRKTGDKIADLLfslnRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKE 226
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEAL----DDFPGTVLLVSHDRYFLDRvATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-217 |
6.05e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 6.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkmneEERAKLRA--QHVGFVFQsfmlIPTL 103
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT----DKKVKLSDirKKVGLVFQ----YPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 NALENVQL------PALLkGESEKHSYARAVDLLKQLGLGERLY--HMPAQLSGGEQQRVALARAFCTQPAILFADEPTG 175
Cdd:PRK13637 95 QLFEETIEkdiafgPINL-GLSEEEIENRVKRAMNIVGLDYEDYkdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493580923 176 NLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRL 217
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRI 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-205 |
1.27e-23 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 94.60 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLRaQHVGFVFQSFMLIPTlN 104
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR-RAIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENVQLPALLKGESEKHSYARAV---DLLKQLG------LGER-LYhmpaqLSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:cd03253 91 IGYNIRYGRPDATDEEVIEAAKAAqihDKIMRFPdgydtiVGERgLK-----LSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190
....*....|....*....|....*....|...
gi 493580923 175 GNLDRKTGDKIADLLFSL--NRdyatTLILVTH 205
Cdd:cd03253 166 SALDTHTEREIQAALRDVskGR----TTIVIAH 194
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-228 |
1.71e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.23 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLmgEDLTKMNEEERAKLRA--QHVGFVFQsfmlIPTL 103
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDKYIRPvrKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 NALENVQLPALLKGESE-----KHSYARAVDLLKQLGLGERLYHM-PAQLSGGEQQRVALARAFCTQPAILFADEPTGNL 177
Cdd:PRK13646 97 QLFEDTVEREIIFGPKNfkmnlDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493580923 178 DRKTGDKIADLLFSLNRDYATTLILVTHD-NELAARCQRRLRLVDGQLKEES 228
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQT 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-211 |
2.48e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.87 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 21 SQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLraqhVGFVFQS---F 97
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF----VGLVFQNpddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 98 MLIPTLNalENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNL 177
Cdd:PRK13652 91 IFSPTVE--QDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190
....*....|....*....|....*....|....
gi 493580923 178 DRKTGDKIADLLFSLNRDYATTLILVTHDNELAA 211
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVP 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-210 |
3.25e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.37 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtKMNEEERAKLRaQHVGFVFQS---FMLIPT 102
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQNpddQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 103 LnaLENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTG 182
Cdd:PRK13639 96 V--EEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180
....*....|....*....|....*...
gi 493580923 183 DKIADLLFSLNRDyATTLILVTHDNELA 210
Cdd:PRK13639 174 SQIMKLLYDLNKE-GITIIISTHDVDLV 200
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-223 |
3.67e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 92.73 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEdltKMNEEERaklr 86
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK---PLDIAAR---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03269 70 -NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHDNELAAR-CQRRLRLVDGQ 223
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGR 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-224 |
5.46e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 3 TEKVLEVHQLTK-----QVgegdsqisiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKM 77
Cdd:COG1129 1 AEPLLEMRGISKsfggvKA---------LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 78 NEEEraklrAQH--VGFVFQSFMLIPTLNALENVQLPALLKGE---SEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQ 152
Cdd:COG1129 72 SPRD-----AQAagIAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 153 QRVALARAFCTQPAILFADEPTGNLDRKTgdkiADLLFSLNRDYA---TTLILVTHD-NELAARCQRR--LRlvDGQL 224
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTERE----VERLFRIIRRLKaqgVAIIYISHRlDEVFEIADRVtvLR--DGRL 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-205 |
1.14e-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: 91.90 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 20 DSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeeRAKLRaQHVGFVFQSFML 99
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLR-SMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 100 IPTlNALENVQLPALLKGESEKHSYARAV---DLLKQL--GLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:cd03254 89 FSG-TIMENIRLGRPNATDEEVIEAAKEAgahDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190
....*....|....*....|....*....|.
gi 493580923 175 GNLDRKTGDKIADLLFSLNRDyaTTLILVTH 205
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMKG--RTSIIIAH 196
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-205 |
1.19e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.89 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVGFVFQ---SFMLIPT 102
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpeSQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 103 LnaLENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHM-PAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKT 181
Cdd:PRK13649 103 V--LKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180
....*....|....*....|....
gi 493580923 182 GDKIADLLFSLNRDyATTLILVTH 205
Cdd:PRK13649 181 RKELMTLFKKLHQS-GMTIVLVTH 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-206 |
2.41e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.37 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 23 ISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAklraqhVGFVFQSFMLIPT 102
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD------IAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 103 LNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDrktg 182
Cdd:PRK11650 91 MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD---- 166
|
170 180 190
....*....|....*....|....*....|.
gi 493580923 183 dkiADL-------LFSLNRDYATTLILVTHD 206
Cdd:PRK11650 167 ---AKLrvqmrleIQRLHRRLKTTSLYVTHD 194
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
25-227 |
3.66e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 90.28 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDltkmneeerAKLRAQHVGFVfqsfmliPTLN 104
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---------SSLLGLGGGFN-------PELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENVQLPALLKGESEKHSYARAVDLLKQLGLGERlYHMP-AQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGD 183
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDF-IDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493580923 184 KIADLLFSLNRDyATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:cd03220 180 KCQRRLRELLKQ-GKTVILVSHDPSSIKRlCDRALVLEKGKIRFD 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-211 |
3.72e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.34 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLRAQhVGFVFQSfmliP---- 101
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSK-VGLVFQD----Pddqv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 102 -TLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRK 180
Cdd:PRK13647 93 fSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190
....*....|....*....|....*....|.
gi 493580923 181 TGDKIADLLFSLNRDyATTLILVTHDNELAA 211
Cdd:PRK13647 173 GQETLMEILDRLHNQ-GKTVIVATHDVDLAA 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-209 |
4.42e-22 |
|
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: 87.89 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDsqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGlddgstgsvklmgedltkmneeeraklr 86
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG---------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqhvgfvfqsfMLIPTlnalenvqlpallKGESEKHSyaravdllkqlglGERLYHMPaQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03221 49 -----------ELEPD-------------EGIVTWGS-------------TVKIGYFE-QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLfslnRDYATTLILVTHDNEL 209
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYF 129
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-206 |
4.77e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.43 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVGFVFQ---SFMLIPT 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfpeAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 103 LnaLENVQLPALLKGESEKHSYARAVDLLKQLGLGERLY-HMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKT 181
Cdd:PRK13641 103 V--LKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLIsKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180
....*....|....*....|....*
gi 493580923 182 GDKIADLLFSLNRDyATTLILVTHD 206
Cdd:PRK13641 181 RKEMMQLFKDYQKA-GHTVILVTHN 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-226 |
6.57e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 6.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDD------GSTGSVKLMGEDLT 75
Cdd:PRK14246 6 SAEDVFNISRLYLYINDK----AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 76 KMNEeerAKLRaQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVD-LLKQLGLGERLY---HMPA-QLSGG 150
Cdd:PRK14246 82 QIDA---IKLR-KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEeCLRKVGLWKEVYdrlNSPAsQLSGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 151 EQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLR-LVDGQLKE 226
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAfLYNGELVE 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-224 |
7.08e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.01 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 20 DSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGL---DDGSTGSVKLMGedlTKMNEEERAKLRaQHVGFVFQS 96
Cdd:PRK13640 17 DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDG---ITLTAKTVWDIR-EKVGIVFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 97 ----FMLIPTLN----ALENVQLPallkgESEKHSYARavDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAIL 168
Cdd:PRK13640 93 pdnqFVGATVGDdvafGLENRAVP-----RPEMIKIVR--DVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493580923 169 FADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQL 224
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
28-206 |
9.88e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 91.31 E-value: 9.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 28 GVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRaQHVGFVFQSFM--LIPTLNA 105
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLasLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LE------NVQLPALLKGESEKhsyaRAVDLLKQLGLGERLYH-MPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:PRK15079 118 GEiiaeplRTYHPKLSRQEVKD----RVKAMMLKVGLLPNLINrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180
....*....|....*....|....*...
gi 493580923 179 RKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-205 |
1.14e-21 |
|
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: 88.81 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEeraklr 86
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKhsyaRAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTH 205
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSH 184
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-205 |
1.43e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.58 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 20 DSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLRAQhVGFVFQSFML 99
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQA-ISVVSQRVHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 100 IP-TLNalENVQLPAllkgesEKHSYARAVDLLKQLGLGERLYHMPA----------QLSGGEQQRVALARAFCTQPAIL 168
Cdd:PRK11160 426 FSaTLR--DNLLLAA------PNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190
....*....|....*....|....*....|....*..
gi 493580923 169 FADEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTH 205
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHAQN--KTVLMITH 532
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-224 |
2.10e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 21 SQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDL-----TKMNEEERAKLRAQ------- 88
Cdd:PRK13651 18 TELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkkTKEKEKVLEKLVIQktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 89 --------HVGFVFQ--SFMLIPTlNALENVQLPALLKGESEKHSYARAVDLLKQLGLGER-LYHMPAQLSGGEQQRVAL 157
Cdd:PRK13651 98 kkikeirrRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 158 ARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTH--DNELaARCQRRLRLVDGQL 224
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHdlDNVL-EWTKRTIFFKDGKI 243
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-219 |
2.10e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVklmgedltkmneeerAKLRAQHVGFVFQSFMLIPTLNA 105
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSEVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 --LENVQL----PALLKGESEKHSYARAVDLLKQLGLgERLYHMP-AQLSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:NF040873 73 tvRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQlGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493580923 179 RKTGDKIADLLFSLNRDYATTLIlVTHDNELAARCQRRLRL 219
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVV-VTHDLELVRRADPCVLL 191
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
7-206 |
2.74e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.96 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAG-LDDGSTGSVKLM---GEDLTKMNEEER 82
Cdd:COG4170 4 LDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGiTKDNWHVTADRFrwnGIDLLKLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 83 AKLRAQHVGFVFQ--SFMLIPTLNALEnvQL----PA-LLKG---ESEKHSYARAVDLLKQLGLGERLYHM---PAQLSG 149
Cdd:COG4170 84 RKIIGREIAMIFQepSSCLDPSAKIGD--QLieaiPSwTFKGkwwQRFKWRKKRAIELLHRVGIKDHKDIMnsyPHELTE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 150 GEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-227 |
3.30e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 24 SILQGVELVVESAQTIALIGESGSGKST----LLGIIAglddgSTGSVKLMGEDLTKMNEEERAKLRAQhVGFVFQ--SF 97
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 98 MLIPTLNALE------NVQLPALLKGESEkhsyARAVDLLKQLGLG-ERLYHMPAQLSGGEQQRVALARAFCTQPAILFA 170
Cdd:PRK15134 374 SLNPRLNVLQiieeglRVHQPTLSAAQRE----QQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 171 DEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELA-ARCQRRLRLVDGQLKEE 227
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVrALCHQVIVLRQGEVVEQ 507
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-227 |
9.55e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 90.18 E-value: 9.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMneeERAKLR 86
Cdd:TIGR01193 474 IVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQS-FMLIPTLnaLENVQLPALLKGESEKhsYARAVDLLK--------QLGLGERLYHMPAQLSGGEQQRVAL 157
Cdd:TIGR01193 548 -QFINYLPQEpYIFSGSI--LENLLLGAKENVSQDE--IWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 158 ARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRdyaTTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
7-225 |
1.02e-20 |
|
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: 89.81 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTkqVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAklr 86
Cdd:COG4618 331 LSVENLT--VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aQHVGFVFQSFMLIP-TLNalENVqlpA-LLKGESEK-HSYARAV---DLLKQLGLGerlYHMP-----AQLSGGEQQRV 155
Cdd:COG4618 406 -RHIGYLPQDVELFDgTIA--ENI---ArFGDADPEKvVAAAKLAgvhEMILRLPDG---YDTRigeggARLSGGQRQRI 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 156 ALARAFCTQPAILFADEPTGNLDRkTGDK-----IADLlfslnRDYATTLILVTHDNELAARCQRRLRLVDGQLK 225
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDD-EGEAalaaaIRAL-----KARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-178 |
1.34e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.72 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 24 SILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGST---GSVKLMGEdltKMNEEERAKLRAqhvgFVFQSFMLI 100
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGM---PIDAKEMRAISA----YVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 101 PTLNALENVQLPALLK---GESEKHSYARAVDLLKQLGLGerlyhmPAQ------------LSGGEQQRVALARAFCTQP 165
Cdd:TIGR00955 112 PTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLR------KCAntrigvpgrvkgLSGGERKRLAFASELLTDP 185
|
170
....*....|...
gi 493580923 166 AILFADEPTGNLD 178
Cdd:TIGR00955 186 PLLFCDEPTSGLD 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-178 |
2.19e-20 |
|
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: 85.67 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLr 86
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLgERLYHMPA-QLSGGEQQRVALARAFCTQP 165
Cdd:cd03218 76 --GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKAsSLSGGERRRVEIARALATNP 152
|
170
....*....|...
gi 493580923 166 AILFADEPTGNLD 178
Cdd:cd03218 153 KFLLLDEPFAGVD 165
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-209 |
3.88e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.81 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEE 81
Cdd:PRK11300 1 MSQPLLSVSGLMMRFG----GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 RAKLraqhvGFV--FQSFMLIPTLNALENVQ-----------LPALLKG----ESEKHSYARAVDLLKQLGLGERLYHMP 144
Cdd:PRK11300 77 IARM-----GVVrtFQHVRLFREMTVIENLLvaqhqqlktglFSGLLKTpafrRAESEALDRAATWLERVGLLEHANRQA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 145 AQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNEL 209
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-205 |
4.65e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.77 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQVGegdsqiSI--LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkMNE 79
Cdd:COG3845 1 MMPPALELRGITKRFG------GVvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 80 EERAklRAQHVGFVFQSFMLIPTLNALENVQL---PALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVA 156
Cdd:COG3845 74 PRDA--IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493580923 157 LARAFCTQPAILFADEPTGNLdrkTGDKIADLLFSLNR--DYATTLILVTH 205
Cdd:COG3845 152 ILKALYRGARILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITH 199
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-228 |
5.24e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.94 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 3 TEKVLEVHQLTKQVGEgDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkmnEEER 82
Cdd:PRK13650 1 MSNIIEVKNLTFKYKE-DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 83 AKLRaQHVGFVFQS----FMLIPTLN----ALENvqlpallKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQR 154
Cdd:PRK13650 77 WDIR-HKIGMVFQNpdnqFVGATVEDdvafGLEN-------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493580923 155 VALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKEES 228
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTS 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-210 |
6.84e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.38 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 14 KQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAklraQHVGFV 93
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR----QQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 94 FQSfmliPTL---NALENVQLPALLKGESEKHsyARAVDLLKQLGLGERLYHMP-AQLSGGEQQRVALARAFCTQPAILF 169
Cdd:PRK10247 87 AQT----PTLfgdTVYDNLIFPWQIRNQQPDP--AIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493580923 170 ADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD-NELA 210
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDkDEIN 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-204 |
1.34e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.46 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTK----QVGEGDSQ-ISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMN 78
Cdd:PRK15112 2 ETLLEVRNLSKtfryRTGWFRRQtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 79 eeerAKLRAQHVGFVFQ--SFMLIPTLNALENVQLPALLKGESEKHSYARAVDL-LKQLGL-GERLYHMPAQLSGGEQQR 154
Cdd:PRK15112 82 ----YSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIEtLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493580923 155 VALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVT 204
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-181 |
1.63e-19 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 83.74 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 22 QISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLRaQHVGFVFQSFMLIP 101
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW---LR-SQIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 102 TlNALENVQL---PALLKGESEKHSYARAVDLLKQLG------LGERlyhmPAQLSGGEQQRVALARAFCTQPAILFADE 172
Cdd:cd03249 91 G-TIAENIRYgkpDATDEEVEEAAKKANIHDFIMSLPdgydtlVGER----GSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
....*....
gi 493580923 173 PTGNLDRKT 181
Cdd:cd03249 166 ATSALDAES 174
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-212 |
1.93e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDD-----GSTGSVKLMGEDLTKmNEEERAKLRaQHVGFVFQSFMLI 100
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA-PDVDPVEVR-RRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 101 PTlNALENVQLPALLKG------ESEKHSYARAV------DLLKQLGLGerlyhmpaqLSGGEQQRVALARAFCTQPAIL 168
Cdd:PRK14243 104 PK-SIYDNIAYGARINGykgdmdELVERSLRQAAlwdevkDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493580923 169 FADEPTGNLDRKTGDKIADLLFSLNRDYatTLILVTHDNELAAR 212
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAAR 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-178 |
2.09e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.35 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGStGSVKLMGEDLTKMNEEERAKLRA---QHV--GF---VFQSF 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHRAylsQQQspPFampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 98 MLiptlnalenvQLPAllkGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCT-------QPAILFA 170
Cdd:COG4138 91 AL----------HQPA---GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLL 157
|
....*...
gi 493580923 171 DEPTGNLD 178
Cdd:COG4138 158 DEPMNSLD 165
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-228 |
2.73e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.99 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 5 KVLEVHQLTKQVgEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmneEERAK 84
Cdd:PRK13642 3 KILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 85 LRaQHVGFVFQS----FMlipTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARA 160
Cdd:PRK13642 79 LR-RKIGMVFQNpdnqFV---GATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 161 FCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKEES 228
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-206 |
2.80e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 84.47 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDG----STGSVKLMGEDLTKMNEEE 81
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 RAKLRAQHVGFVFQSfmliPT--LNALENV--QLPALLKGESEKHSY--------ARAVDLLKQLGLGERLYHM---PAQ 146
Cdd:PRK15093 83 RRKLVGHNVSMIFQE----PQscLDPSERVgrQLMQNIPGWTYKGRWwqrfgwrkRRAIELLHRVGIKDHKDAMrsfPYE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 147 LSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHD 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-227 |
3.08e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.60 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 17 GEGDSQISiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLmgEDLTKMNEEERAKLRaQHVGFVFQS 96
Cdd:PRK13633 18 EESTEKLA-LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTSDEENLWDIR-NKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 97 --FMLIPTLnALENVQL-PALLkGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEP 173
Cdd:PRK13633 94 pdNQIVATI-VEEDVAFgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493580923 174 TGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-225 |
3.25e-19 |
|
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: 85.48 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTkqVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERA 83
Cdd:TIGR01842 314 EGHLSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 84 KlraqHVGFVFQSFMLIP-TLNA-----LENVQLPALLkgesEKHSYARAVDLLKQLGLGERLYHMP--AQLSGGEQQRV 155
Cdd:TIGR01842 392 K----HIGYLPQDVELFPgTVAEniarfGENADPEKII----EAAKLAGVHELILRLPDGYDTVIGPggATLSGGQRQRI 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 156 ALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTlILVTHDNELAARCQRRLRLVDGQLK 225
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITV-VVITHRPSLLGCVDKILVLQDGRIA 532
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-210 |
3.89e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.80 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDsqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDG--STGSVKLMGEDLTKMNEEERAK 84
Cdd:cd03217 1 LEIKDLHVSVGGKE----ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 85 LraqhvGfVFQSFmliptlnalenvQLPALLKGesekhsyARAVDLLKQLGLGerlyhmpaqLSGGEQQRVALARAFCTQ 164
Cdd:cd03217 77 L-----G-IFLAF------------QYPPEIPG-------VKNADFLRYVNEG---------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHDNELA 210
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLL 167
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-206 |
6.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.13 E-value: 6.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVkLMGE-----DLTKMNEEERAKlraQHVGFVFQsfmlI 100
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDyaipaNLKKIKEVKRLR---KEIGLVFQ----F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 101 PTLNALE-----NVQLPALLKGESEKHSYARAVDLLKQLGLGER-LYHMPAQLSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:PRK13645 99 PEYQLFQetiekDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190
....*....|....*....|....*....|..
gi 493580923 175 GNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHN 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-206 |
7.05e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGE-------- 72
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 73 --DLTKMNEEERAKLRAQHVGFVFQSFM--LIPTLNALENV-QLPALLKGESEKHSYARAVDLLKQLGLGER---LYHMP 144
Cdd:PRK10261 87 viELSEQSAAQMRHVRGADMAMIFQEPMtsLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 145 AQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHD 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-205 |
7.22e-19 |
|
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: 81.89 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 19 GDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtkmNEEERAKLRAQhVGFVFQSFM 98
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLRRQ-IGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 99 LIPTlNALENVQLPALLKGESEKHSYARAV---DLLKQLGLGerlYHMP-----AQLSGGEQQRVALARAFCTQPAILFA 170
Cdd:cd03251 87 LFND-TVAENIAYGRPGATREEVEEAARAAnahEFIMELPEG---YDTVigergVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 493580923 171 DEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTH 205
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKN--RTTFVIAH 195
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-225 |
1.04e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTeKVLEVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkmnee 80
Cdd:PRK13537 3 MSV-APIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ERAKLRAQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARA 160
Cdd:PRK13537 73 SRARHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 161 FCTQPAILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHDNELAARCQRRLRLVDGQLK 225
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRK 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-226 |
1.13e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.83 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmneeERAKLrAQHVGFVF-QSFMLIPTLN 104
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK----RRKEF-ARRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENVQLPALLKGESEKhSYARAVDLL-KQLGLGErLYHMPA-QLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTG 182
Cdd:COG4586 113 AIDSFRLLKAIYRIPDA-EYKKRLDELvELLDLGE-LLDTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493580923 183 DKIADLLFSLNRDYATTLILVTHD-NELAARCQRRL-----RLV-DGQLKE 226
Cdd:COG4586 191 EAIREFLKEYNRERGTTILLTSHDmDDIEALCDRVIvidhgRIIyDGSLEE 241
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-201 |
1.37e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeeRAKLRaQHVGFVFQSFMLiptLNA 105
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQDAGL---FNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 L--ENVQLPALLKGESEKH---SYARAVDLL--KQLGL----GERlyhmPAQLSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:PRK13657 424 SieDNIRVGRPDATDEEMRaaaERAQAHDFIerKPDGYdtvvGER----GRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180
....*....|....*....|....*..
gi 493580923 175 GNLDRKTGDKIADLLFSLNRDYATTLI 201
Cdd:PRK13657 500 SALDVETEAKVKAALDELMKGRTTFII 526
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-213 |
1.59e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.28 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 5 KVLEVHQLTKQvgegdSQISILQGVELVVESAQTIALIGESGSGKStlLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAK 84
Cdd:PRK10418 3 QQIELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 85 LRAQHVGFVFQ----SFMLIPTLNALENVQLPALLKGESEkhsyARAVDLLKQLGLGE-----RLYhmPAQLSGGEQQRV 155
Cdd:PRK10418 76 LRGRKIATIMQnprsAFNPLHTMHTHARETCLALGKPADD----ATLTAALEAVGLENaarvlKLY--PFEMSGGMLQRM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 156 ALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARC 213
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARL 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-205 |
2.07e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.70 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 29 VELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVGFVFQ---SFMLIPTLna 105
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpeSQLFEETV-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHM-PAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDK 184
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180
....*....|....*....|.
gi 493580923 185 IADLLFSLNRDyATTLILVTH 205
Cdd:PRK13643 183 MMQLFESIHQS-GQTVVLVTH 202
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-206 |
2.13e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.24 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 20 DSQiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDgSTGSVKLMGE-DLTKMNEEERA----KLRAQhVGFVF 94
Cdd:PRK14258 18 DTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFFNQNIYERRvnlnRLRRQ-VSMVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 95 QSFMLIPtLNALENVQLPALLKGESEK-------HSYARAVDLLKQLGlgERLYHMPAQLSGGEQQRVALARAFCTQPAI 167
Cdd:PRK14258 95 PKPNLFP-MSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDEIK--HKIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 493580923 168 LFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-206 |
4.38e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.13 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 8 EVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAK--- 84
Cdd:COG4604 3 EIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 85 -LRaqhvgfvfQSfmliPTLNALENV-QLPAL---------LKGESEKHsYARAVDLLKQLGLGERLYHmpaQLSGGEQQ 153
Cdd:COG4604 79 iLR--------QE----NHINSRLTVrELVAFgrfpyskgrLTAEDREI-IDEAIAYLDLEDLADRYLD---ELSGGQRQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493580923 154 RVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-219 |
4.51e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtkmnEEERAKL 85
Cdd:PRK13539 2 MLEGEDLACVRGG----RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI----DDPDVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RAQHVGfvFQSFMLiPTLNALENVQLPALLKGESEkhsyARAVDLLKQLGLGeRLYHMPAQ-LSGGEQQRVALARAFCTQ 164
Cdd:PRK13539 74 ACHYLG--HRNAMK-PALTVAENLEFWAAFLGGEE----LDIAAALEAVGLA-PLAHLPFGyLSAGQKRRVALARLLVSN 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFS-LNRDyaTTLILVTHdNELAARCQRRLRL 219
Cdd:PRK13539 146 RPIWILDEPTAALDAAAVALFAELIRAhLAQG--GIVIAATH-IPLGLPGARELDL 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-227 |
5.47e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.14 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 24 SILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTG-----SVKLMGEDLtkMNEEERAKLRaQHVGFVFQS-- 96
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFR-RRVGMLFQRpn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 97 -FMLIPTLNALENVQLPALL-KGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:PRK14271 112 pFPMSIMDNVLAGVRAHKLVpRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493580923 175 GNLDRKTGDKIADLLFSLNRdyATTLILVTHDNELAARCQRRLRL-VDGQLKEE 227
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALfFDGRLVEE 243
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-219 |
5.61e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.55 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEeraklR 86
Cdd:TIGR01189 1 LAARNLACSRGE----RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQSFMLIPTLNALENVQ-LPALLKGESEKhsyarAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQP 165
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSALENLHfWAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 166 AILFADEPTGNLDRKTGDKIADLLfslnRDYATT---LILVTHdNELAARCQRRLRL 219
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLL----RAHLARggiVLLTTH-QDLGLVEARELRL 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-223 |
7.47e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.51 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 3 TEKVLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGL-DDGS-TGSVKLMGEDLTKMN-- 78
Cdd:PRK13549 2 MEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyPHGTyEGEIIFEGEELQASNir 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 79 EEERAKLRAQHvgfvfQSFMLIPTLNALENVqlpaLLKGESEKHS-------YARAVDLLKQLGLGERLYHMPAQLSGGE 151
Cdd:PRK13549 78 DTERAGIAIIH-----QELALVKELSVLENI----FLGNEITPGGimdydamYLRAQKLLAQLKLDINPATPVGNLGLGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493580923 152 QQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHD-NELAARCQRRLRLVDGQ 223
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-221 |
1.46e-17 |
|
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: 76.81 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKlmgedltkmneeeraKLR 86
Cdd:cd03223 1 IELENLSLATPDGRV---LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---------------MPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQsfmliptlnalenvqlpallkgesekHSYARAVDLLKQLglgerLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03223 63 GEDLLFLPQ--------------------------RPYLPLGTLREQL-----IYPWDDVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLfslnRDYATTLILVTHDNELAARCQRRLRLVD 221
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-206 |
1.82e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 78.65 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 24 SILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRaQHVGFVFQSFMLIPTL 103
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 NALENVQLPaLLKGESEKHSYARAVDLLKQLGLGER--LYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKT 181
Cdd:PRK11831 100 NVFDNVAYP-LREHTQLPAPLLHSTVMMKLEAVGLRgaAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180
....*....|....*....|....*
gi 493580923 182 GDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK11831 179 MGVLVKLISELNSALGVTCVVVSHD 203
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
25-227 |
2.21e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGE-----DLTkmneeeraklraqhVGFVfqsfml 99
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallELG--------------AGFH------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 100 iPTLNALENVQLPALLKGESeKHSYARAVDLLKQL-GLGERLyHMPAQ-LSGGEQQRVALARAFCTQPAILFADE--PTG 175
Cdd:COG1134 101 -PELTGRENIYLNGRLLGLS-RKEIDEKFDEIVEFaELGDFI-DQPVKtYSSGMRARLAFAVATAVDPDILLVDEvlAVG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 176 NLD--RKTGDKIADLlfslnRDYATTLILVTHDNELAAR-CQRRLRLVDGQLKEE 227
Cdd:COG1134 178 DAAfqKKCLARIREL-----RESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMD 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-217 |
2.49e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 37 QTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRaQHVGFVFQS--FMLIPTLNA----LENVQ 110
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLDPRQTVgdsiMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 111 LPALLKGESEKhsyARAVDLLKQLGL-GERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLL 189
Cdd:PRK10261 430 VHGLLPGKAAA---ARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
170 180
....*....|....*....|....*...
gi 493580923 190 FSLNRDYATTLILVTHDNELAARCQRRL 217
Cdd:PRK10261 507 LDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-206 |
3.48e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.35 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtKMNEEERAKLRaQHVGFVFQSfmliP---- 101
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLR-ESVGMVFQD----Pdnql 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 102 -TLNALENVQLPALLKGESEKHSYARAVDLLKQLGLgERLYHMPAQ-LSGGEQQRVALARAFCTQPAILFADEPTGNLDR 179
Cdd:PRK13636 96 fSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180
....*....|....*....|....*..
gi 493580923 180 KTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-223 |
3.50e-17 |
|
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: 79.48 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGST--GSVKLMGEDLTKMN--EEE 81
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNirDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 RAKLRAQHvgfvfQSFMLIPTLNALENVQLPALLKGESEKHSYA----RAVDLLKQLGLGERLYHMP-AQLSGGEQQRVA 156
Cdd:TIGR02633 77 RAGIVIIH-----QELTLVPELSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 157 LARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRdYATTLILVTHD-NELAARCQRRLRLVDGQ 223
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-224 |
3.57e-17 |
|
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: 75.54 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtkmneeeraklr 86
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqhvgfvfqsfmliptlnalenvqlpallkgesEKHSYARAvdllKQLGLGerlyhMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:cd03216 65 ---------------------------------SFASPRDA----RRAGIA-----MVYQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 167 ILFADEPTGNLDRKTgdkiADLLFSLNRDYA---TTLILVTHD-NELAARCQRRLRLVDGQL 224
Cdd:cd03216 103 LLILDEPTAALTPAE----VERLFKVIRRLRaqgVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-209 |
4.64e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 3 TEKVLEVHQLTKqVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGlddgstgsvklmgedltkmneeer 82
Cdd:COG2401 24 SERVAIVLEAFG-VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG------------------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 83 aklraQHVGFVFQSFMLIPTLNALENVqlpALLKGESEKHSYARAVDLLKQLGLGE-----RLYHmpaQLSGGEQQRVAL 157
Cdd:COG2401 79 -----ALKGTPVAGCVDVPDNQFGREA---SLIDAIGRKGDFKDAVELLNAVGLSDavlwlRRFK---ELSTGQKFRFRL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493580923 158 ARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNEL 209
Cdd:COG2401 148 ALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDV 199
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
25-178 |
4.74e-17 |
|
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: 76.93 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLraqHVGFVFQSFMLIPTLN 104
Cdd:TIGR04406 16 VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL---GIGYLPQEASIFRKLT 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 105 ALENVQlpALL---KGESEKHSYARAVDLLKQLGLGeRLYHMPAQ-LSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:TIGR04406 93 VEENIM--AVLeirKDLDRAEREERLEALLEEFQIS-HLRDNKAMsLSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-215 |
5.38e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.84 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNE------ 79
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrrigyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 80 -EERAklraqhvgfvfqsfmLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALA 158
Cdd:COG4152 77 pEERG---------------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLI 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 159 RAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHDNELAAR-CQR 215
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEElCDR 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-173 |
7.38e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.61 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERA 83
Cdd:COG1137 1 MMTLEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 84 KLraqHVGF------VFQSfmliptLNALENVQLPALLKGESEKHSYARAVDLLKQLGLgERLYHMPA-QLSGGEQQRVA 156
Cdd:COG1137 77 RL---GIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGI-THLRKSKAySLSGGERRRVE 146
|
170
....*....|....*..
gi 493580923 157 LARAFCTQPAILFADEP 173
Cdd:COG1137 147 IARALATNPKFILLDEP 163
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-222 |
8.48e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 8.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtkmnEEERAKLR 86
Cdd:PRK09536 4 IDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV----EALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQSFMLIPTLNALENVQL---PALLKGESEKHSYARAVD-LLKQLGLGERLYHMPAQLSGGEQQRVALARAFC 162
Cdd:PRK09536 76 SRRVASVPQDTSLSFEFDVRQVVEMgrtPHRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 163 TQPAILFADEPTGNLD----RKTGDKIADLLfslnrDYATTLILVTHDNELAAR-CQRRLRLVDG 222
Cdd:PRK09536 156 QATPVLLLDEPTASLDinhqVRTLELVRRLV-----DDGKTAVAAIHDLDLAARyCDELVLLADG 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-224 |
8.93e-17 |
|
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: 75.16 E-value: 8.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLtkqvgegdSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERa 83
Cdd:cd03215 2 EPVLEVRGL--------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 84 klRAQHVGFV---FQSFMLIPTLNALENVQLPALLkgesekhsyaravdllkqlglgerlyhmpaqlSGGEQQRVALARA 160
Cdd:cd03215 73 --IRAGIAYVpedRKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 161 FCTQPAILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHDN-ELAARCQRRLRLVDGQL 224
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELdELLGLCDRILVMYEGRI 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
11-180 |
9.83e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.61 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 11 QLTKQVGEGDSQISI---LQGVElvvesaqtiALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNE------EE 81
Cdd:PRK11144 5 NFKQQLGDLCLTVNLtlpAQGIT---------AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiclppEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 RaklraqHVGFVFQSFMLIPTLNALENvqlpaLLKG--ESEKHSYARAVDLLkqlGLGERLYHMPAQLSGGEQQRVALAR 159
Cdd:PRK11144 76 R------RIGYVFQDARLFPHYKVRGN-----LRYGmaKSMVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGR 141
|
170 180
....*....|....*....|...
gi 493580923 160 AFCTQPAILFADEPTGNLD--RK 180
Cdd:PRK11144 142 ALLTAPELLLMDEPLASLDlpRK 164
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-224 |
1.24e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTkqVGEGDSqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeerAKLR 86
Cdd:PRK11231 3 LRTENLT--VGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLS----SRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 AQHVGFVFQSfMLIPtlnalENVQLPALLK-------------GESEKHSYARAVDLLKQLGLGERLYhmpAQLSGGEQQ 153
Cdd:PRK11231 75 ARRLALLPQH-HLTP-----EGITVRELVAygrspwlslwgrlSAEDNARVNQAMEQTRINHLADRRL---TDLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 154 RVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNrDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRyCDHLVVLANGHV 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-222 |
1.80e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.52 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 3 TEKVLEVHQLTKQVGegdsQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEER 82
Cdd:PRK09700 2 ATPYISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 83 AKLraqHVGFVFQSFMLIPTLNALENVQLPALLKGE-------SEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRV 155
Cdd:PRK09700 78 AQL---GIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 156 ALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHD-NELAARCQRRLRLVDG 222
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-178 |
2.32e-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: 75.22 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMneeERAKLRAQhVGFVFQSFMLIpTLN 104
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQ-VGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 105 ALENVQL--PAL-LKGESEKHSYARAVDLLKQL--GLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:cd03252 92 IRDNIALadPGMsMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
25-226 |
2.71e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 74.45 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeeRAKLRaQHVGFVFQsfmlIPTL- 103
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR-SRISIIPQ----DPVLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 --------------------NALENVQLPALLKGESEkhsyaravdllkqlGLGERLYHMPAQLSGGEQQRVALARAFCT 163
Cdd:cd03244 91 sgtirsnldpfgeysdeelwQALERVGLKEFVESLPG--------------GLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493580923 164 QPAILFADEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLRLVDGQLKE 226
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-178 |
2.78e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 33 VESAQTIALIGESGSGKSTLLGIIAGLDDGStGSVKLMGEDLTKMNEEERAKLRA-----QHVGF---VFQSFML-IPTL 103
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELARHRAylsqqQTPPFampVFQYLTLhQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 NALENVQlpallkgesekhsyARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALArAFCTQ--PAI------LFADEPTG 175
Cdd:PRK03695 98 TRTEAVA--------------SALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLA-AVVLQvwPDInpagqlLLLDEPMN 162
|
...
gi 493580923 176 NLD 178
Cdd:PRK03695 163 SLD 165
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-201 |
3.25e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 76.78 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEeerAKLRAqHVGFVFQSFMLiptLN 104
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ---ASLRA-AIGIVPQDTVL---FN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 A--LENVQLPALLKGESEKHSYARAV---DLLKQL--GL----GER-LyhmpaQLSGGEQQRVALARAFCTQPAILFADE 172
Cdd:COG5265 446 DtiAYNIAYGRPDASEEEVEAAARAAqihDFIESLpdGYdtrvGERgL-----KLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180
....*....|....*....|....*....
gi 493580923 173 PTGNLDRKTGDKIADLLFSLNRDyATTLI 201
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARG-RTTLV 548
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-226 |
3.79e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.68 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEeeraKLRAQHVGFVFQSFMLIpTLN 104
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH----HYLHRQVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMP-----AQLSGGEQQRVALARAFCTQPAILFADEPTGNLDR 179
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493580923 180 ktgdKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKE 226
Cdd:TIGR00958 651 ----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-206 |
5.52e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLRaQHVGFVFQ--------SF 97
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK---LR-KHIGIVFQnpdnqfvgSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 98 MLIPTLNALENVQLPallkgESEKHSYARAVdlLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNL 177
Cdd:PRK13648 101 VKYDVAFGLENHAVP-----YDEMHRRVSEA--LKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180
....*....|....*....|....*....
gi 493580923 178 DRKTGDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHD 202
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-208 |
1.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTKQVGEGDS-QISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSV---------KLM 70
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDEKQEnELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 71 GEDLTKMNEEERAK----LRaQHVGFVFQ--SFMLIPTLNALENVQLPALLkGESEKHSYARAVDLLKQLGLGER-LYHM 143
Cdd:PRK13631 96 NHELITNPYSKKIKnfkeLR-RRVSMVFQfpEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493580923 144 PAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHDNE 208
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTME 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-177 |
1.35e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTKQVgegdSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNee 80
Cdd:PRK15439 6 TTAPPLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 eraKLRAQHVG--FVFQSFMLIPTLNALENVqlpaLLKGESEKHSYARAVDLLKQLGLGERLyHMPA-QLSGGEQQRVAL 157
Cdd:PRK15439 80 ---PAKAHQLGiyLVPQEPLLFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGCQLDL-DSSAgSLEVADRQIVEI 151
|
170 180
....*....|....*....|
gi 493580923 158 ARAFCTQPAILFADEPTGNL 177
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASL 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-205 |
1.50e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.44 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 37 QTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtkmneEERAKLRAQHVGFVFQSFMLIPTLNALENVQLPALLK 116
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 117 GESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLfsLNRDY 196
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRS 1109
|
....*....
gi 493580923 197 ATTLILVTH 205
Cdd:TIGR01257 1110 GRTIIMSTH 1118
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-219 |
1.75e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.14 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEE-ERAKL 85
Cdd:cd03231 1 LEADELTCERDG----RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RAQHVGfvfqsfMLIPTLNALENVQLPALLkgesekHSYARAVDLLKQLGLGErLYHMP-AQLSGGEQQRVALARAFCTQ 164
Cdd:cd03231 77 YLGHAP------GIKTTLSVLENLRFWHAD------HSDEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFSlNRDYATTLILVTH-DNELAARCQRRLRL 219
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMAG-HCARGGMVVLTTHqDLGLSEAGARELDL 198
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-216 |
1.88e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkmnEEERAKL 85
Cdd:PRK11614 5 MLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---DWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 RAQHVGFVFQSFMLIPTLNALENVQLPALLKGESE-KHSYARAVDLLKQlgLGERLYHMPAQLSGGEQQRVALARAFCTQ 164
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHDNELAARCQRR 216
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADR 206
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-205 |
4.22e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.60 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEeerAKLRaQHVGFVFQ-------SF 97
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLR-QGVAMVQQdpvvladTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 98 MLIPTL----------NALENVQLPALLKGESEkhsyaravdllkqlGLGERLYHMPAQLSGGEQQRVALARAFCTQPAI 167
Cdd:PRK10790 432 LANVTLgrdiseeqvwQALETVQLAELARSLPD--------------GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190
....*....|....*....|....*....|....*...
gi 493580923 168 LFADEPTGNLDRKTGDKIADLLfSLNRDYaTTLILVTH 205
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQAL-AAVREH-TTLVVIAH 533
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-206 |
5.18e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.43 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEGDSqisILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMgEDLTkmneeerakl 85
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 raqhVGFVFQSFMLIPTLNALENVQ-----LPALLK-----------------------GE-SEKHSYARAVDLLKQLGL 136
Cdd:TIGR03719 70 ----VGYLPQEPQLDPTKTVRENVEegvaeIKDALDrfneisakyaepdadfdklaaeqAElQEIIDAADAWDLDSQLEI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493580923 137 GERLYHMP------AQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLfslnRDYATTLILVTHD 206
Cdd:TIGR03719 146 AMDALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-225 |
9.48e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.79 E-value: 9.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDltkmnEEERAKLRAQHVGFVFQSFMLIPTLN 104
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP-----VPARARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDK 184
Cdd:PRK13536 131 VRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493580923 185 IADLLFSLnRDYATTLILVTHDNELAARCQRRLRLVDGQLK 225
Cdd:PRK13536 211 IWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRK 250
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-224 |
2.08e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKlraQHVGFVFQSFMLIPTLN 104
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR---RGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENvqLPALL---KGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKT 181
Cdd:PRK10895 95 VYDN--LMAVLqirDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493580923 182 GDKIADLLFSLnRDYATTLILVTHD-NELAARCQRRLRLVDGQL 224
Cdd:PRK10895 173 VIDIKRIIEHL-RDSGLGVLITDHNvRETLAVCERAYIVSQGHL 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-224 |
2.40e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.41 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 33 VESAQTIALIGESGSGKSTLLGIIAGLDDgSTGSVKLMGEDLTKMNEEE-RaklraQHVGFVFQSFMLI-PTLnaLENVQ 110
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESwR-----KHLSWVGQNPQLPhGTL--RDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 111 LPALLKGESEKHSyaravdLLKQLGLGERLYHMP-----------AQLSGGEQQRVALARAFCTQPAILFADEPTGNLDR 179
Cdd:PRK11174 445 LGNPDASDEQLQQ------ALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493580923 180 KTGDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLRLVDGQL 224
Cdd:PRK11174 519 HSEQLVMQALNAASRR--QTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-227 |
3.68e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.63 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNE-EERAKLraqhVGFVFQS----FMLI 100
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL----VGIVFQNpetqFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 101 PTLNAL----ENVQLPALlkgesekhSYARAVDL-LKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTG 175
Cdd:PRK13644 94 TVEEDLafgpENLCLPPI--------EIRKRVDRaLAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493580923 176 NLDRKTGDKIADLLFSLNRDyATTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-192 |
3.74e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 24 SILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGS--TGSVKLMGEDLTKMNeeeraklrAQHVGFVFQSFMLIP 101
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQI--------LKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 102 TLNALENVQLPALLK-----GESEKHSYARAVdlLKQLGLGERLYHMPAQ-----LSGGEQQRVALARAFCTQPAILFAD 171
Cdd:PLN03211 154 HLTVRETLVFCSLLRlpkslTKQEKILVAESV--ISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180
....*....|....*....|.
gi 493580923 172 EPTGNLDRKTGDKIADLLFSL 192
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSL 252
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-206 |
4.96e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAG---LDDGS--------------------TGSV-KLMGEDLtkmnEE 80
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDGRiiyeqdlivarlqqdpprnvEGTVyDFVAEGI----EE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 ERAKLRAQHVgfVFQSFMLIPT---LNALENVQlpALLKGESEKHSYARAVDLLKQLGLGErlyHMP-AQLSGGEQQRVA 156
Cdd:PRK11147 94 QAEYLKRYHD--ISHLVETDPSeknLNELAKLQ--EQLDHHNLWQLENRINEVLAQLGLDP---DAAlSSLSGGWLRKAA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493580923 157 LARAFCTQPAILFADEPTGNLDRKTGDKIADLLfslnRDYATTLILVTHD 206
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHD 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-205 |
5.22e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeERAKLRAQhVGFVFQSFMLIPTLNA 105
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS--TTAALAAG-VAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENV---QLPALLKGESEKHSYARAVDLLKQLGL----GERLYHmpaqLSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:PRK11288 97 AENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVdidpDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190
....*....|....*....|....*....|.
gi 493580923 179 -RKTgdkiaDLLFSLN---RDYATTLILVTH 205
Cdd:PRK11288 173 aREI-----EQLFRVIrelRAEGRVILYVSH 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-206 |
8.92e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.76 E-value: 8.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 39 IALIGESGSGKSTLLGIIAGLDDGSTGSVKLMgEDLTkmneeeraklraqhVGFVFQSFMLIPTLNALENVQ-----LPA 113
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK--------------VGYLPQEPQLDPEKTVRENVEegvaeVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 114 LLK--GE-SEKhsYARAVD----LLKQLG-LGERLYH-------------MPA-----------QLSGGEQQRVALARAF 161
Cdd:PRK11819 101 ALDrfNEiYAA--YAEPDAdfdaLAAEQGeLQEIIDAadawdldsqleiaMDAlrcppwdakvtKLSGGERRRVALCRLL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493580923 162 CTQPAILFADEPTGNLDRKTgdkIADLLFSLnRDYATTLILVTHD 206
Cdd:PRK11819 179 LEKPDMLLLDEPTNHLDAES---VAWLEQFL-HDYPGTVVAVTHD 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-206 |
1.11e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVklmgedltkmneEERAKLRaqhVGFVFQSFMLIPTLn 104
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR---IGYVPQKLYLDTTL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 alenvqlPALLKGESEKHSYARAVDLLKQLGL--GERLYHMPAQ-LSGGEQQRVALARAFCTQPAILFADEPTGNLDRKT 181
Cdd:PRK09544 83 -------PLTVNRFLRLRPGTKKEDILPALKRvqAGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*
gi 493580923 182 GDKIADLLFSLNRDYATTLILVTHD 206
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-219 |
1.15e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKQVGEgdsqiSIL-QGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAK 84
Cdd:PRK13538 1 MLEARNLACERDE-----RILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 85 LR--AQHVGfvfqsfmLIPTLNALENVQLPALLKGESEKhsyARAVDLLKQLGLGERLyHMPA-QLSGGEQQRVALARAF 161
Cdd:PRK13538 76 LLylGHQPG-------IKTELTALENLRFYQRLHGPGDD---EALWEALAQVGLAGFE-DVPVrQLSAGQQRRVALARLW 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 162 CTQPAILFADEPTGNLDRKTgdkIADL--LFSLNRDYATTLILVTH-DNELAARCQRRLRL 219
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQG---VARLeaLLAQHAEQGGMVILTTHqDLPVASDKVRKLRL 202
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-224 |
1.30e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGS--------TGSVKLMGEDLTKMNEEERAKLRA-----QHVG 91
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAvlpqaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 92 FVFqsfmliptlNALENVQLP----ALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFC----- 162
Cdd:PRK13547 96 FAF---------SAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 163 ----TQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRL-RLVDGQL 224
Cdd:PRK13547 167 hdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIaMLADGAI 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
42-215 |
3.36e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 42 IGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERaklraQHVGFVFQSFMLIPTLNALENVQLPALLKGESEK 121
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR-----RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 122 HSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLI 201
Cdd:NF033858 373 EIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIF 452
|
170
....*....|....*
gi 493580923 202 LVTH-DNElAARCQR 215
Cdd:NF033858 453 ISTHfMNE-AERCDR 466
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-224 |
4.62e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 65.96 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtkmNEEERAKLRAQhVGFVFQSfmliPTLN 104
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHSK-VSLVGQE----PVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 A----------LENVQLPALLKGESEKHSYARAVDLLK--QLGLGERlyhmPAQLSGGEQQRVALARAFCTQPAILFADE 172
Cdd:cd03248 101 ArslqdniaygLQSCSFECVKEAAQKAHAHSFISELASgyDTEVGEK----GSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493580923 173 PTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLRLVDGQL 224
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-181 |
6.45e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLT----KMNEEeraklraQHVGFVFQSFMLIP 101
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQE-------AGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 102 TLNALENVQLPALLKGE----SEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNL 177
Cdd:PRK10762 93 QLTIAENIFLGREFVNRfgriDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
....*
gi 493580923 178 -DRKT 181
Cdd:PRK10762 173 tDTET 177
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-206 |
1.28e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmneeeraKLRAQHVGFVFQSFML---IPT 102
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQSEEVdwsFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 103 LnaLENVQLPA------LLKgESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGN 176
Cdd:PRK15056 96 L--VEDVVMMGryghmgWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190
....*....|....*....|....*....|
gi 493580923 177 LDRKTGDKIADLLFSLnRDYATTLILVTHD 206
Cdd:PRK15056 173 VDVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-226 |
1.32e-12 |
|
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: 64.36 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 24 SILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEeraKLRaqhvgfvfQSFMLIPtl 103
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE---DLR--------SSLTIIP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 nalenvQLPALLKG--ESEKHSYARAVDllKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKT 181
Cdd:cd03369 89 ------QDPTLFSGtiRSNLDPFDEYSD--EEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493580923 182 GDKIADLLFSLNRDyaTTLILVTHDNELAARCQRRLRLVDGQLKE 226
Cdd:cd03369 161 DALIQKTIREEFTN--STILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
25-223 |
2.22e-12 |
|
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: 63.64 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGedltkmneeeraklraqHVGFVFQSFMLiptLN 104
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------------SIAYVSQEPWI---QN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 A--LENVqlpalLKGESEKHS-YARAVDL------LKQLG------LGERlyhmPAQLSGGEQQRVALARAFCTQPAILF 169
Cdd:cd03250 80 GtiRENI-----LFGKPFDEErYEKVIKAcalepdLEILPdgdlteIGEK----GINLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 170 ADEPTGNLDRKTGDKIADLLF----SLNRdyatTLILVTHDNELAARCQRRLRLVDGQ 223
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFENCIlgllLNNK----TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-178 |
2.53e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTkqVgEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeeRA 83
Cdd:COG3845 255 EVVLEVENLS--V-RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 84 KLRAQHVGFV---FQSFMLIPTLNALENVQL-----PALLKGESEKHSYAR--AVDLLKQLGLGERLYHMPA-QLSGGEQ 152
Cdd:COG3845 329 ERRRLGVAYIpedRLGRGLVPDMSVAENLILgryrrPPFSRGGFLDRKAIRafAEELIEEFDVRTPGPDTPArSLSGGNQ 408
|
170 180
....*....|....*....|....*.
gi 493580923 153 QRVALARAFCTQPAILFADEPTGNLD 178
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-174 |
2.87e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkmNEEERAKLRAQhvgfvfQSFM------- 98
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPR------IAYMpqglgkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 99 LIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLG---ERlyhmPA-QLSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:NF033858 89 LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLApfaDR----PAgKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-224 |
3.57e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 24 SILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNeeerAKLRAQHVGFVFQSfmlIPTL 103
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS----SKAFARKVAYLPQQ---LPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 NALENVQLPALLK----------GESEKHSYARAVDLLKQLGLGERLYHmpaQLSGGEQQRVALARAFCTQPAILFADEP 173
Cdd:PRK10575 98 EGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD---SLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493580923 174 TGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAAR-CQRRLRLVDGQL 224
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEM 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-205 |
3.75e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtkmNEEERAKLRaQHVGFVFQSFMLIPTLNA 105
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLR-NQVALVSQNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 lENVQLPA---LLKGESEKHSY-ARAVDLLKQL--GLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDR 179
Cdd:PRK11176 435 -NNIAYARteqYSREQIEEAARmAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180
....*....|....*....|....*.
gi 493580923 180 KTGDKIADLLFSLNRDyaTTLILVTH 205
Cdd:PRK11176 514 ESERAIQAALDELQKN--RTSLVIAH 537
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-221 |
4.57e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.37 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 102 TLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKT 181
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 493580923 182 GDKIADLLFSLNRDYATTLiLVTHDNELAARCQRRLRLVD 221
Cdd:NF000106 180 RNEVWDEVRSMVRDGATVL-LTTQYMEEAEQLAHELTVID 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-174 |
8.58e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTkqVGEGdsqisiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERA 83
Cdd:COG1129 254 EVVLEVEGLS--VGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 84 KLraqhvGFVF-----QSFMLIPTLNALENVQLPALLKGE-----SEKHSYARAVDLLKQLGL-GERLYHMPAQLSGGEQ 152
Cdd:COG1129 326 RA-----GIAYvpedrKGEGLVLDLSIRENITLASLDRLSrggllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQ 400
|
170 180
....*....|....*....|..
gi 493580923 153 QRVALARAFCTQPAILFADEPT 174
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPT 422
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-85 |
9.97e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.35 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGS--TGSVKLMGEDLTKMN 78
Cdd:CHL00131 2 NKNKPILEIKNLHASVNE----NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLE 77
|
....*..
gi 493580923 79 EEERAKL 85
Cdd:CHL00131 78 PEERAHL 84
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-211 |
1.90e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGL-DDGS-TGSVKLMGEdltkmnEEERAKLRA-QHVGFVF--QSFMLI 100
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyPHGSyEGEILFDGE------VCRFKDIRDsEALGIVIihQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 101 PTLNALENVqlpaLLKGESEKH-------SYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEP 173
Cdd:NF040905 91 PYLSIAENI----FLGNERAKRgvidwneTNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 493580923 174 TGNLDRKTGDKIADLLFSLnRDYATTLILVTHD-NELAA 211
Cdd:NF040905 167 TAALNEEDSAALLDLLLEL-KAQGITSIIISHKlNEIRR 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-178 |
1.92e-11 |
|
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: 61.12 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 11 QLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGS---TGSVKLMGEDLTKMNEEERAklra 87
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 88 qHVGFVFQSFMLIPTLNALENVQLPALLKGesekHSYARAVdllkqlglgerlyhmpaqlSGGEQQRVALARAFCTQPAI 167
Cdd:cd03233 84 -EIIYVSEEDVHFPTLTVRETLDFALRCKG----NEFVRGI-------------------SGGERKRVSIAEALVSRASV 139
|
170
....*....|.
gi 493580923 168 LFADEPTGNLD 178
Cdd:cd03233 140 LCWDNSTRGLD 150
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-178 |
2.26e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLTKQVGEgdsqISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNee 80
Cdd:PRK13543 6 HTAPPLLAAHALAFSRNE----EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 81 eraklRAQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLkqlGLGERLYHMPAQLSGGEQQRVALARA 160
Cdd:PRK13543 80 -----RSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARL 151
|
170
....*....|....*...
gi 493580923 161 FCTQPAILFADEPTGNLD 178
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLD 169
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-189 |
2.80e-11 |
|
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: 60.33 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGS--TGSVKLMGEDLTKMNEEEraklraqhVGFVFQSFMLIPT 102
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQRS--------TGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 103 LNALENVQLPALLKGesekhsyaravdllkqLGLGERlyhmpaqlsggeqQRVALARAFCTQPAILFADEPTGNLDRKTG 182
Cdd:cd03232 94 LTVREALRFSALLRG----------------LSVEQR-------------KRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
....*..
gi 493580923 183 DKIADLL 189
Cdd:cd03232 145 YNIVRFL 151
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-227 |
4.93e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.77 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 14 KQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKlraqHVGFV 93
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 94 FQSFMLIPTLNALENV------QLPALLKGESE-KHSYARAvdlLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:PRK10253 87 AQNATTPGDITVQELVargrypHQPLFTRWRKEdEEAVTKA---MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRL-RLVDGQLKEE 227
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLiALREGKIVAQ 225
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
140-212 |
6.22e-11 |
|
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: 59.54 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 140 LYHMPAQLSGGEQQ------RVALARAFCTQPAILFADEPTGNLDR-KTGDKIADLLFSLNRDYATTLILVTHDNELAAR 212
Cdd:cd03240 109 LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDA 188
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-205 |
9.68e-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: 59.27 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 21 SQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKLRAQHVGFVFQSFMLi 100
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 101 ptLNAL--ENVQLPALL-----KGESEKHSYARAVDLL---KQLGLGERlyhmPAQLSGGEQQRVALARAFCTQPAILFA 170
Cdd:cd03290 91 --LNATveENITFGSPFnkqryKAVTDACSLQPDIDLLpfgDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 493580923 171 DEPTGNLDRKTGDKI-ADLLFSLNRDYATTLILVTH 205
Cdd:cd03290 165 DDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTH 200
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-189 |
2.43e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLddgSTGSVKLMGEDLtkMNEEE 81
Cdd:TIGR00956 755 SGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAER---VTTGVITGGDRL--VNGRP 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 82 RAKLRAQHVGFVFQSFMLIPTLNALENVQLPALLK-----GESEKHSYARAV-DLLKQLGLGERLYHMPAQ-LSGGEQQR 154
Cdd:TIGR00956 830 LDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpksvSKSEKMEYVEEViKLLEMESYADAVVGVPGEgLNVEQRKR 909
|
170 180 190
....*....|....*....|....*....|....*.
gi 493580923 155 VALARAFCTQPA-ILFADEPTGNLDRKTGDKIADLL 189
Cdd:TIGR00956 910 LTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLM 945
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-206 |
2.73e-10 |
|
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: 58.53 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 32 VVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGsvKLMGED-----------------LTKMNEEE-RAKLRAQHVGfv 93
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPdwdeildefrgselqnyFTKLLEGDvKVIVKPQYVD-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 94 fqsfmLIPTL---NALEnvqlpaLLKGESEKHSYAravDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFA 170
Cdd:cd03236 98 -----LIPKAvkgKVGE------LLKKKDERGKLD---ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 493580923 171 DEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHD 206
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHD 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-178 |
3.92e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.09 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLtkmNEEERAKLR-AQHVGFVFQ---SFMLI 100
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKRGLLAlRQQVATVFQdpeQQIFY 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 101 PTLNALENVQLPALLKGESEkhsYARAVDLLKQLGLGERLYHMPAQ-LSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAE---ITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-205 |
8.53e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 8.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDG--STGSVKLMGEDLTKMNEEERAklrAQHVGFVFQ------- 95
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQypveipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 96 ---SFMLIPTLNALENV-QLPALLKGESEkhsyaravDLLKQlglGERLYHMPAQL---------SGGEQQRVALARAFC 162
Cdd:PRK09580 93 vsnQFFLQTALNAVRSYrGQEPLDRFDFQ--------DLMEE---KIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493580923 163 TQPAILFADEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTH 205
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
41-206 |
2.44e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 41 LIGESGSGKSTLLGIIAGLDDGSTGSVKL-MGEDLTKMNEEEraklraqhvgFVFQSFMLIPTL----NALENVQ----- 110
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQ----------FAFEEFTVLDTVimghTELWEVKqerdr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 111 ---LP----------ALLKGE-SEKHSY---ARAVDLLKQLGLGERLYHMP-AQLSGGEQQRVALARAFCTQPAILFADE 172
Cdd:PRK15064 102 iyaLPemseedgmkvADLEVKfAEMDGYtaeARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDE 181
|
170 180 190
....*....|....*....|....*....|....
gi 493580923 173 PTGNLDRKTGDKIADLLfslnRDYATTLILVTHD 206
Cdd:PRK15064 182 PTNNLDINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-225 |
2.50e-09 |
|
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: 56.95 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTKqVGEGDSQISIlQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGED-LTKMNEEErak 84
Cdd:TIGR01257 1937 ILRLNELTK-VYSGTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVH--- 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 85 lraQHVGFVFQSFMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQ 164
Cdd:TIGR01257 2012 ---QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILVTHD-NELAARCQRRLRLVDGQLK 225
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSmEECEALCTRLAIMVKGAFQ 2149
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-226 |
3.76e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 29 VELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkmnEEERAKLRaQHVGFVFQSFMLiptlnalen 108
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR-KLFSAVFTDFHL--------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 109 vqLPALLKGESEKHSYARAVDLLKQLGLGERLYH-----MPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGD 183
Cdd:PRK10522 409 --FDQLLGPEGKPANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493580923 184 KIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKE 226
Cdd:PRK10522 487 EFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-227 |
5.24e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 1 MSTEKVLEVHQLT----KQVgegdsqisilQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTK 76
Cdd:PRK09700 260 LAHETVFEVRNVTsrdrKKV----------RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 77 MNEEERAKlraQHVGFVFQSFM---LIPTLNALENVQLPALLK-----------GESEKHSYARAVDLLKQLGLGErLYH 142
Cdd:PRK09700 330 RSPLDAVK---KGMAYITESRRdngFFPNFSIAQNMAISRSLKdggykgamglfHEVDEQRTAENQRELLALKCHS-VNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 143 MPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDG 222
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
....*
gi 493580923 223 QLKEE 227
Cdd:PRK09700 486 RLTQI 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-206 |
1.94e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 39 IALIGESGSGKSTLLGIIAGLDDGSTGSVKLmGedlTKMN----EEERAKLRaqhvgfvfqsfmliPTLNALENVqlpAL 114
Cdd:PRK11147 348 IALIGPNGCGKTTLLKLMLGQLQADSGRIHC-G---TKLEvayfDQHRAELD--------------PEKTVMDNL---AE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 115 LKGESEKHSYARAVdllkqLG-LGERLYH-MPAQ-----LSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTgdkiAD 187
Cdd:PRK11147 407 GKQEVMVNGRPRHV-----LGyLQDFLFHpKRAMtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET----LE 477
|
170
....*....|....*....
gi 493580923 188 LLFSLNRDYATTLILVTHD 206
Cdd:PRK11147 478 LLEELLDSYQGTVLLVSHD 496
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-178 |
2.05e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 14 KQVGEGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGS--TGSVKLMGedLTKmNEEERAKLRaqhvG 91
Cdd:PLN03140 884 KEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISG--FPK-KQETFARIS----G 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 92 FVFQSFMLIPTLNALENVQLPALLK-----GESEKHSYARAVDLLKQL-GLGERLYHMPA--QLSGGEQQRVALARAFCT 163
Cdd:PLN03140 957 YCEQNDIHSPQVTVRESLIYSAFLRlpkevSKEEKMMFVDEVMELVELdNLKDAIVGLPGvtGLSTEQRKRLTIAVELVA 1036
|
170
....*....|....*
gi 493580923 164 QPAILFADEPTGNLD 178
Cdd:PLN03140 1037 NPSIIFMDEPTSGLD 1051
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-226 |
2.78e-08 |
|
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: 52.93 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDgSTGSVKLMGEDLTKMNEEERAKLr 86
Cdd:cd03289 3 MTVKDLTAKYTEGGN--AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqhVGFVFQS-FMLIPTLNalENVQlpallkgESEKHSYARAVDLLKQLGLGERLYHMPAQL-----------SGGEQQR 154
Cdd:cd03289 79 ---FGVIPQKvFIFSGTFR--KNLD-------PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493580923 155 VALARAFCTQPAILFADEPTGNLDRKTGDKIADllfSLNRDYAT-TLILVTHDNELAARCQRRLRLVDGQLKE 226
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRK---TLKQAFADcTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-212 |
4.37e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGdsqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLmgedltkmneEERAKL- 85
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----------SENANIg 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 -RAQHVGFVFQSfmlipTLNALENVqlpALLKGESEKHSYARAVdllkqlgLGERLY-----HMPAQ-LSGGEQQRVALA 158
Cdd:PRK15064 386 yYAQDHAYDFEN-----DLTLFDWM---SQWRQEGDDEQAVRGT-------LGRLLFsqddiKKSVKvLSGGEKGRMLFG 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 159 RAFCTQPAILFADEPTGNLDRKTgdkIADLLFSLnRDYATTLILVTHDNE----LAAR 212
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMES---IESLNMAL-EKYEGTLIFVSHDREfvssLATR 504
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-220 |
6.15e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGlD--DGSTGSVKLMGEdltKMNEEERAKLRAQHVGFVFQSFMLIPT 102
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DhpQGYSNDLTLFGR---RRGSGETIWDIKKHIGYVSSSLHLDYR 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 103 LNA-LENVqlpaLLKGESEKHSYARAV-DLLKQ--------LGLGERLYHMPAQ-LSGGeQQRVAL-ARAFCTQPAILFA 170
Cdd:PRK10938 351 VSTsVRNV----ILSGFFDSIGIYQAVsDRQQKlaqqwldiLGIDKRTADAPFHsLSWG-QQRLALiVRALVKHPTLLIL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493580923 171 DEPTGNLD---RKTGDKIADLLFSlnrDYATTLILVTHDNELAARC-QRRLRLV 220
Cdd:PRK10938 426 DEPLQGLDplnRQLVRRFVDVLIS---EGETQLLFVSHHAEDAPACiTHRLEFV 476
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-227 |
7.52e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 20 DSQIS--ILQGVELVVESAQTIALIGESGSGKSTLLGIIAG-LDDGSTGSVKLMGEdltkmneeeraklraqhVGFVFQ- 95
Cdd:PLN03232 625 DSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-----------------VAYVPQv 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 96 SFMLIPTLNalENVqlpaLLKGESEKHSYARAVD---LLKQLGL---------GERlyhmPAQLSGGEQQRVALARAFCT 163
Cdd:PLN03232 688 SWIFNATVR--ENI----LFGSDFESERYWRAIDvtaLQHDLDLlpgrdlteiGER----GVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493580923 164 QPAILFADEPTGNLDRKTGDKIADllfSLNRD--YATTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFD---SCMKDelKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-226 |
8.24e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 7 LEVHQLTKQVGEGDSqiSILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDgSTGSVKLMGEDLTKMNEEERAKlr 86
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRK-- 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 87 aqhvgfvfqSFMLIPtlnalenvQLPALLKGESEKH--SYARAVD-----LLKQLGLGERLYHMPAQ-----------LS 148
Cdd:TIGR01271 1293 ---------AFGVIP--------QKVFIFSGTFRKNldPYEQWSDeeiwkVAEEVGLKSVIEQFPDKldfvlvdggyvLS 1355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 149 GGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADllfSLNRDYAT-TLILVTHDNELAARCQRRLRLVDGQLKE 226
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRK---TLKQSFSNcTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
26-226 |
1.12e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGE-DLTKMNeeerAKLRAQhvgfvfqsfmliptLN 104
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAIS----AGLSGQ--------------LT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDK 184
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493580923 185 IADLLFSLnRDYATTLILVTHD-NELAARCQRRLRLVDGQLKE 226
Cdd:PRK13546 182 CLDKIYEF-KEQNKTIFFVSHNlGQVRQFCTKIAWIEGGKLKD 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-212 |
1.14e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 49.67 E-value: 1.14e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 146 QLSGGEQQRVALARAFC---TQPAILFA-DEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHDNELAAR 212
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQALAEAILEH-LVKGAQVIVITHLPELAEL 146
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-206 |
1.15e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 21 SQISILQGVELVVESA-------QTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGE-DLTKMNEEERAklraqhvgf 92
Cdd:PRK10636 5 SSLQIRRGVRVLLDNAtatinpgQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPA--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 93 vfqsfMLIPTLNAL-----ENVQLPALLKGESEK---HSYA----------------RAVDLLKQLGLG-ERLYHMPAQL 147
Cdd:PRK10636 76 -----LPQPALEYVidgdrEYRQLEAQLHDANERndgHAIAtihgkldaidawtirsRAASLLHGLGFSnEQLERPVSDF 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 148 SGGEQQRVALARAFCTQPAILFADEPTGNLDrktgdkiADLLFSLNR---DYATTLILVTHD 206
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKwlkSYQGTLILISHD 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-206 |
1.21e-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: 51.47 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTKqvGEGDSQIsiLQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLmGEDLtkmneeera 83
Cdd:TIGR03719 320 DKVIEAENLTK--AFGDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 84 klraqHVGFVFQSF-MLIPTLNALENVQ--LPALLKGESEKHSYA-------RAVDLLKQLGlgerlyhmpaQLSGGEQQ 153
Cdd:TIGR03719 386 -----KLAYVDQSRdALDPNKTVWEEISggLDIIKLGKREIPSRAyvgrfnfKGSDQQKKVG----------QLSGGERN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493580923 154 RVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFslnrDYATTLILVTHD 206
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL----NFAGCAVVISHD 499
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-205 |
2.34e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 23 ISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTK--MNEEERAKLRAQHVGF-------- 92
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNdmTNEQDYQGDEEQNVGMknvnefsl 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 93 -----------VFQS----------------------FMLIPTLNALENVQLPALLKGESEKHSYARAVDLLKQLGLGER 139
Cdd:PTZ00265 1261 tkeggsgedstVFKNsgkilldgvdicdynlkdlrnlFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEF 1340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 140 LYHMPAQ-----------LSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTH 205
Cdd:PTZ00265 1341 IESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-226 |
2.75e-07 |
|
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: 50.71 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEdltkmneeeraklraqhVGFVFQSfMLIPTLNA 105
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------------VAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVQLPALLKgESEKHSYARAVDLLKQLGL---GER--LYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRK 180
Cdd:TIGR00957 716 RENILFGKALN-EKYYQQVLEACALLPDLEIlpsGDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493580923 181 TGDKIADLLFSLNRDYAT-TLILVTHDNELAARCQRRLRLVDGQLKE 226
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLKNkTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-227 |
2.80e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.43 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 6 VLEVHQLTkqvGEGDSQISilqgveLVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKL 85
Cdd:PRK15439 268 VLTVEDLT---GEGFRNIS------LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 86 raqhvGFVF-----QS---FMLIP-TLN--ALENVQLPALLKGESEK---HSYARAvdllkqlgLGERLYHM--PAQ-LS 148
Cdd:PRK15439 339 -----GLVYlpedrQSsglYLDAPlAWNvcALTHNRRGFWIKPARENavlERYRRA--------LNIKFNHAeqAARtLS 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 149 GGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:PRK15439 406 GGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
124-209 |
3.33e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 124 YARA-----VDLLKQLGLGE-RLYHMPAQLSGGEQQRVALARAFCTQ-PAILFA-DEPTGNLDRKTGDKIADLLFSLnRD 195
Cdd:cd03270 109 FARVgirerLGFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIGSGlTGVLYVlDEPSIGLHPRDNDRLIETLKRL-RD 187
|
90
....*....|....
gi 493580923 196 YATTLILVTHDNEL 209
Cdd:cd03270 188 LGNTVLVVEHDEDT 201
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-223 |
3.46e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEERAKlraQHVGFVFQSFMLIPTLNA 105
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVQLPAL-LKGE--SEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTG 182
Cdd:PRK10982 91 MDNMWLGRYpTKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493580923 183 DKIADLLFSLnRDYATTLILVTHD-NELAARCQRRLRLVDGQ 223
Cdd:PRK10982 171 NHLFTIIRKL-KERGCGIVYISHKmEEIFQLCDEITILRDGQ 211
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-185 |
3.85e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.10 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 20 DSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMN-EEERAKLraqhvGFVFQSFM 98
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRL-----AVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 99 LIPTLNAlENVQL--PALLKGESEKHSYARAV--DLLK-----QLGLGERlyhmPAQLSGGEQQRVALARAFCTQPAILF 169
Cdd:PRK10789 400 LFSDTVA-NNIALgrPDATQQEIEHVARLASVhdDILRlpqgyDTEVGER----GVMLSGGQKQRISIARALLLNAEILI 474
|
170
....*....|....*.
gi 493580923 170 ADEPTGNLDRKTGDKI 185
Cdd:PRK10789 475 LDDALSAVDGRTEHQI 490
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-228 |
6.10e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEErakLRaqhvgfvfQSFMLIPtln 104
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LR--------RVLSIIP--- 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 alenvQLPALLKGES----EKHSYARAVDLLKQL--------------GLGERLYHMPAQLSGGEQQRVALARAFCTQPA 166
Cdd:PLN03232 1317 -----QSPVLFSGTVrfniDPFSEHNDADLWEALerahikdvidrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493580923 167 ILFADEPTGNLDRKTGDKIADLLFSLNRdyATTLILVTHDNELAARCQRRLRLVDGQLKEES 228
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFK--SCTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-225 |
7.91e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVklmgedltkmneeerakLRAQHVGFVFQSFMLiptLN 104
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------------WAERSIAYVPQQAWI---MN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 AleNVQLPALLKGESEKHSYARAVDL------LKQL--GLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGN 176
Cdd:PTZ00243 735 A--TVRGNILFFDEEDAARLADAVRVsqleadLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493580923 177 LDRKTGDKIADLLFsLNRDYATTLILVTHDNELAARCQRRLRLVDGQLK 225
Cdd:PTZ00243 813 LDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-178 |
8.03e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTkqvGEGDSQISilqgveLVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMNEEEra 83
Cdd:PRK10762 255 EVRLKVDNLS---GPGVNDVS------FTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 84 KLRAqhvGFVFQSF-----MLIPTLNALENVQLPAL---------LKGESEKHSYARAVDLL--------KQLGLgerly 141
Cdd:PRK10762 324 GLAN---GIVYISEdrkrdGLVLGMSVKENMSLTALryfsraggsLKHADEQQAVSDFIRLFniktpsmeQAIGL----- 395
|
170 180 190
....*....|....*....|....*....|....*..
gi 493580923 142 hmpaqLSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:PRK10762 396 -----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-205 |
8.25e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 23 ISILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKL-----------------MG-------------- 71
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndshnlkdinlkwwrskIGvvsqdpllfsnsik 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 72 ----------EDLTKMNEE-------------ERAKLRAQHVGFVFqsfMLIPTLNALENVQLpallKGESEKHSYARAV 128
Cdd:PTZ00265 478 nnikyslyslKDLEALSNYynedgndsqenknKRNSCRAKCAGDLN---DMSNTTDSNELIEM----RKNYQTIKDSEVV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 129 DLLKQLGLGERLYHMP-----------AQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYA 197
Cdd:PTZ00265 551 DVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 630
|
....*...
gi 493580923 198 TTLILVTH 205
Cdd:PTZ00265 631 RITIIIAH 638
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-203 |
1.64e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 21 SQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAG---LDDGSTGS-----VKLMGEDLTKMNEEEraklraqhvgf 92
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGelpLLSGERQSqfshiTRLSFEQLQKLVSDE----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 93 vFQ---SFMLIPT-----LNALENVQLpallkgesEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQ 164
Cdd:PRK10938 83 -WQrnnTDMLSPGeddtgRTTAEIIQD--------EVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSE 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 493580923 165 PAILFADEPTGNLDRKTGDKIADLLFSLNRDyATTLILV 203
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-223 |
1.81e-06 |
|
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: 47.40 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 37 QTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkmneeerakLRAQHVGFVFQSfmlipTLNALenvqLPALLK 116
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQYIKADYEG-----TVRDL----LSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 117 GESEkHSYARaVDLLKQLGLgERLY--HMPaQLSGGEQQRVALArAFCTQPA-ILFADEPTGNLDRKTGDKIADLL--FS 191
Cdd:cd03237 88 DFYT-HPYFK-TEIAKPLQI-EQILdrEVP-ELSGGELQRVAIA-ACLSKDAdIYLLDEPSAYLDVEQRLMASKVIrrFA 162
|
170 180 190
....*....|....*....|....*....|..
gi 493580923 192 LNRDyaTTLILVTHDNELAARCQRRLRLVDGQ 223
Cdd:cd03237 163 ENNE--KTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
33-205 |
1.82e-06 |
|
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: 48.21 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 33 VESAQTIALIGESGSGKSTLLGIIAGLddgstgsVKLMGEDLTKMNEEE-----------RAKLRAQHV----------- 90
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGEL-------WPVYGGRLTKPAKGKlfyvpqrpymtLGTLRDQIIypdssedmkrr 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 91 GFVFQSFMLIptlnaLENVQLPALLKGESEKHSYARAVDLLkqlglgerlyhmpaqlSGGEQQRVALARAFCTQPAILFA 170
Cdd:TIGR00954 548 GLSDKDLEQI-----LDNVQLTHILEREGGWSAVQDWMDVL----------------SGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 493580923 171 DEPTGNLDRKTGDKIadllFSLNRDYATTLILVTH 205
Cdd:TIGR00954 607 DECTSAVSVDVEGYM----YRLCREFGITLFSVSH 637
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-226 |
2.27e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEdltkmneeerAKLRAQHVGFVFQsfmliptLNA 105
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAISSGLNGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVQLPALLKGESEKHSYARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKI 185
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493580923 186 ADLLFSLnRDYATTLILVTHD-NELAARCQRRLRLVDGQLKE 226
Cdd:PRK13545 183 LDKMNEF-KEQGKTIFFISHSlSQVKSFCTKALWLHYGQVKE 223
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-224 |
3.65e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLM-GEDLTKMNEEERAKLRA-----QHvgfvfqsfm 98
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRAdesplQH--------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 99 liptlnalenvqLPALLKGESEKhsyaRAVDLLKQLGL-GERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNL 177
Cdd:PRK10636 398 ------------LARLAPQELEQ----KLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493580923 178 DRKTGDKIADLLFslnrDYATTLILVTHDNELAARCQRRLRLV-DGQL 224
Cdd:PRK10636 462 DLDMRQALTEALI----DFEGALVVVSHDRHLLRSTTDDLYLVhDGKV 505
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-181 |
4.29e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmneeERAKLRAQhVGFVFQSFMLIPTLN 104
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQKQ-LCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 105 ALENVQLpallkgesEKHSYARAV---DLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKT 181
Cdd:PRK13540 91 LRENCLY--------DIHFSPGAVgitELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
129-206 |
8.11e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 8.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 129 DLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHD 206
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEG--KYVLVVEHD 270
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
27-206 |
1.17e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 27 QGVELVVESAQTIALIGESGSGKSTLL-GIIAGLDdGSTGSVKLMGEDLTKMNEEE-RAKLRAQHVGFV---------FQ 95
Cdd:COG0419 14 RDTETIDFDDGLNLIVGPNGAGKSTILeAIRYALY-GKARSRSKLRSDLINVGSEEaSVELEFEHGGKRyrierrqgeFA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 96 SFMLIPT------------LNALENVQ--LPALLKGESEKHSYARAVDLLKQlglgERLYHM-----PAQLSGGEQQRVA 156
Cdd:COG0419 93 EFLEAKPserkealkrllgLEIYEELKerLKELEEALESALEELAELQKLKQ----EILAQLsgldpIETLSGGERLRLA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493580923 157 LARAFctqpaILFADepTGNLDRKTGDKIADLLFSLNrdyattliLVTHD 206
Cdd:COG0419 169 LADLL-----SLILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-215 |
1.70e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 130 LLKQLGLGerlYHMP----AQLSGGEQQRVALARAFctqPAILFA-----DEPTGNLDRKTGDKIADLLFSLnRDYATTL 200
Cdd:PRK00635 459 ILIDLGLP---YLTPeralATLSGGEQERTALAKHL---GAELIGityilDEPSIGLHPQDTHKLINVIKKL-RDQGNTV 531
|
90
....*....|....*
gi 493580923 201 ILVTHDNELAARCQR 215
Cdd:PRK00635 532 LLVEHDEQMISLADR 546
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-206 |
2.35e-05 |
|
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: 44.78 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 32 VVESAQTIALIGESGSGKSTLLGIIAGL---------DDGSTGSV------KLMGEDLTKM-NEEERAKLRAQHVGFVFQ 95
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGElkpnlgdydEEPSWDEVlkrfrgTELQDYFKKLaNGEIKVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 96 SFmlipTLNALEnvqlpaLLKGESEKhsyARAVDLLKQLGLGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTG 175
Cdd:COG1245 175 VF----KGTVRE------LLEKVDER---GKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|.
gi 493580923 176 NLDRKTGDKIADLLFSLNRDYATTLIlVTHD 206
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVLV-VEHD 271
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-222 |
2.51e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.90 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 25 ILQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEdltkmneeeraklraqhVGFVFQSFMLIP-TL 103
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWIMPgTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 104 NalENVqLPALLKGESEKHSYARAVDLLKQLGLGERLYHMP-----AQLSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:TIGR01271 504 K--DNI-IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493580923 179 RKTGDKIAD-----LLFSLNRdyattlILVTHDNELAARCQRRLRLVDG 222
Cdd:TIGR01271 581 VVTEKEIFEsclckLMSNKTR------ILVTSKLEHLKKADKILLLHEG 623
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-178 |
3.48e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 28 GVELVVESAQTIA------LIGESGSGKSTLLGIIA-GLDDGSTGSVKLM-------GEDLTKMN-----EEERAKLRAQ 88
Cdd:PLN03073 189 GRDLIVDASVTLAfgrhygLVGRNGTGKTTFLRYMAmHAIDGIPKNCQILhveqevvGDDTTALQcvlntDIERTQLLEE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 89 HVGFVFQSFMLiPTLNALENVQLPalLKGESEKHSY--------------------ARAVDLLKQLGLGERLYHMPA-QL 147
Cdd:PLN03073 269 EAQLVAQQREL-EFETETGKGKGA--NKDGVDKDAVsqrleeiykrlelidaytaeARAASILAGLSFTPEMQVKATkTF 345
|
170 180 190
....*....|....*....|....*....|.
gi 493580923 148 SGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-206 |
3.66e-05 |
|
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: 42.36 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 37 QTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMgeDLTKMNEEERAKLRaqhvgfvfqsfmliptlnalenvqlpallk 116
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYI--DGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 117 gesekhsyaravdllkqlglGERLYHMPAQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKI-----ADLLFS 191
Cdd:smart00382 51 --------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLLL 110
|
170
....*....|....*
gi 493580923 192 LNRDYATTLILVTHD 206
Cdd:smart00382 111 LKSEKNLTVILTTND 125
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
145-225 |
4.51e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 43.66 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 145 AQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQL 224
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
.
gi 493580923 225 K 225
Cdd:TIGR02633 482 K 482
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
145-178 |
4.54e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 4.54e-05
10 20 30
....*....|....*....|....*....|....
gi 493580923 145 AQLSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-224 |
5.39e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 4 EKVLEVHQLTKQvgegdSQISIlQGVELVVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKMN----- 78
Cdd:PRK10982 248 EVILEVRNLTSL-----RQPSI-RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneai 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 79 --------EEERAKLRAQHVGFVFQSfmLIPTLNALENVQlpALLKGESEKHSYARAVDLLKQLGLGERLyhMPAQLSGG 150
Cdd:PRK10982 322 nhgfalvtEERRSTGIYAYLDIGFNS--LISNIRNYKNKV--GLLDNSRMKSDTQWVIDSMRVKTPGHRT--QIGSLSGG 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493580923 151 EQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQL 224
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-209 |
7.72e-05 |
|
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: 41.92 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 26 LQGVELVVESAQTIALIGESGSGKSTLLgiiaglDDGSTGSVKLMGEDLTKMNEEERAklraqhvgfVFqsfmlIPTLNA 105
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV------NEGLYASGKARLISFLPKFSRNKL---------IF-----IDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 106 LENVQLpallkgesekhSYaravdllkqLGLGERLyhmpAQLSGGEQQRVALAR--AFCTQPAILFADEPTGNLDRKTGD 183
Cdd:cd03238 71 LIDVGL-----------GY---------LTLGQKL----STLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDIN 126
|
170 180
....*....|....*....|....*.
gi 493580923 184 KIADLLFSLnRDYATTLILVTHDNEL 209
Cdd:cd03238 127 QLLEVIKGL-IDLGNTVILIEHNLDV 151
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
147-223 |
7.94e-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: 41.79 E-value: 7.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 147 LSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAARCQRRLRLVDGQ 223
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-209 |
1.33e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 39 IALIGESGSGKSTLLGIIAGLDDGSTGSVklmgedlTKMNEEERAKLRAQHV-GFVFQSFMLIPTLNALenvqlPALLKG 117
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV-------FRSAKVRMAVFSQHHVdGLDLSSNPLLYMMRCF-----PGVPEQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 118 ESEKHsyaravdlLKQLGLGERLYHMPA-QLSGGEQQRVALARAFCTQPAILFADEPTGNLDRktgDKIADLLFSLNRdY 196
Cdd:PLN03073 606 KLRAH--------LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL---DAVEALIQGLVL-F 673
|
170
....*....|...
gi 493580923 197 ATTLILVTHDNEL 209
Cdd:PLN03073 674 QGGVLMVSHDEHL 686
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-227 |
1.49e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.42 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 18 EGDSQISILQGVELVVESAQTIALIGESGSGKSTLLGIIAG-LDDGSTGSVKLMGEdltkmneeeraklraqhVGFVFQ- 95
Cdd:PLN03130 625 DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-----------------VAYVPQv 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 96 SFMLIPTLNalENVqlpaLLKGESEKHSYARAVD---LLKQLGL---------GERlyhmPAQLSGGEQQRVALARAFCT 163
Cdd:PLN03130 688 SWIFNATVR--DNI----LFGSPFDPERYERAIDvtaLQHDLDLlpggdlteiGER----GVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493580923 164 QPAILFADEPTGNLDRKTGDKIAD--LLFSLNRdyaTTLILVTHDNELAARCQRRLRLVDGQLKEE 227
Cdd:PLN03130 758 NSDVYIFDDPLSALDAHVGRQVFDkcIKDELRG---KTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
154-218 |
1.66e-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: 42.34 E-value: 1.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493580923 154 RVALARAFCTQPAILFADEPTGNLDRKTGDKIA----DLLFSLNRDYATTLILVTHDNELAARCQRRLR 218
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESLAhalvEIIKSRSQQRNFQLLVITHDEDFVELLGRSEY 1281
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
41-228 |
2.58e-04 |
|
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: 41.32 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 41 LIGESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTkmnEEERAKLRaQHVGFVFQSFMLIPTLNALENVQLPallkgese 120
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYR-QLFSAVFSDFHLFDRLLGLDGEADP-------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 121 khsyARAVDLLKQLGLGERLyhmpA---------QLSGGEQQRVALARAFCTQPAILFADEPTgnldrktgdkiAD---- 187
Cdd:COG4615 431 ----ARARELLERLELDHKV----SvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWA-----------ADqdpe 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493580923 188 --------LLFSLnRDYATTLILVTHDNELAARCQRRLRLVDGQLKEES 228
Cdd:COG4615 492 frrvfyteLLPEL-KARGKTVIAISHDDRYFDLADRVLKMDYGKLVELT 539
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-189 |
2.88e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 38 TIALI-GESGSGKSTLLGIIAGLDDGSTGSVKLMGEDLTKmneeerakLRAQHVGFVFQSFMLIPTLNALENVQLPALLK 116
Cdd:PRK13541 27 AITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN--------IAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493580923 117 GESE----KHSYARAVDLLKqlglgERLYhmpaQLSGGEQQRVALARAFCTQPAILFADEPTGNLDRKTGDKIADLL 189
Cdd:PRK13541 99 NSAEtlyaAIHYFKLHDLLD-----EKCY----SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-205 |
4.35e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 125 ARAVDLLKQLGLGE-RLYHMPAQLSGGEQQRVALARAF---CTQPAILFADEPTgnldrkTG---DKIADLLFSLNR--D 195
Cdd:TIGR00630 807 SRKLQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPT------TGlhfDDIKKLLEVLQRlvD 880
|
90
....*....|
gi 493580923 196 YATTLILVTH 205
Cdd:TIGR00630 881 KGNTVVVIEH 890
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-178 |
5.22e-04 |
|
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: 40.54 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 2 STEKVLEVHQLTKQVGegdsqisilqGVELVVESAQ-----TIALIGESGSGKSTLLGIIAGLDDGSTGSVKlmgEDLT- 75
Cdd:COG1245 337 EEETLVEYPDLTKSYG----------GFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLKi 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 76 ---------KMNEEERAKLRaQHVGFVFQSfmliptlnalenvqlpallkgesekhSYARAvDLLKQLGLgERLYHMP-A 145
Cdd:COG1245 404 sykpqyispDYDGTVEEFLR-SANTDDFGS--------------------------SYYKT-EIIKPLGL-EKLLDKNvK 454
|
170 180 190
....*....|....*....|....*....|...
gi 493580923 146 QLSGGEQQRVALARAFCTQPAILFADEPTGNLD 178
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
7-67 |
1.08e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 1.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 7 LEVHQLTKQVGEGdsqISILQGVelvVESAQTIALIGESGSGKSTLLGIIAGLDDGSTGSV 67
Cdd:PRK01889 172 VPVLAVSALDGEG---LDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-208 |
1.19e-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: 39.61 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 147 LSGGEQQRVALArafcTQ-----PAILFA-DEPTGNLDRKTGDKIADLLFSLnRDYATTLILVTHDNE 208
Cdd:TIGR00630 489 LSGGEAQRIRLA----TQigsglTGVLYVlDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDED 551
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
147-174 |
1.92e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 1.92e-03
10 20
....*....|....*....|....*...
gi 493580923 147 LSGGEQQRVALARAFCTQPAILFADEPT 174
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
125-213 |
2.40e-03 |
|
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: 37.98 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 125 ARAVDLLKQLGLGERLYHMPA-QLSGGEQQRVALARAF---CTQPAILFADEPTgnldrkTG---DKIADLLFSLNR--D 195
Cdd:cd03271 147 ARKLQTLCDVGLGYIKLGQPAtTLSGGEAQRIKLAKELskrSTGKTLYILDEPT------TGlhfHDVKKLLEVLQRlvD 220
|
90
....*....|....*...
gi 493580923 196 YATTLILVTHDNELAARC 213
Cdd:cd03271 221 KGNTVVVIEHNLDVIKCA 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
128-178 |
2.84e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 38.25 E-value: 2.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 493580923 128 VDLLKQLGLgERLYHMP-AQLSGGEQQRVALARAFcTQPAILFA-DEPTGNLD 178
Cdd:PRK13409 435 SEIIKPLQL-ERLLDKNvKDLSGGELQRVAIAACL-SRDADLYLlDEPSAHLD 485
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
30-57 |
5.91e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 36.67 E-value: 5.91e-03
10 20
....*....|....*....|....*...
gi 493580923 30 ELVVESAQTIaLIGESGSGKSTLLGIIA 57
Cdd:COG3910 32 GLEFHPPVTF-FVGENGSGKSTLLEAIA 58
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
146-211 |
8.18e-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: 36.47 E-value: 8.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493580923 146 QLSGGEQQRVALARAFCTQ-----PAILFaDEPTGNLDRKTGDKIADLLFSLNRDyaTTLILVTHDNELAA 211
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdpaPFYLF-DEIDAALDAQYRTAVANMIKELSDG--AQFITTTFRPELLE 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
72-211 |
8.71e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 36.94 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493580923 72 EDLTKMNEEERAKLRAQHVG----FVFQSFMLIPTLNALENVQLpallKGESEKHSYARAvdllkqlglGERLyhMPAQL 147
Cdd:PRK02224 718 EELESMYGDLRAELRQRNVEtlerMLNETFDLVYQNDAYSHIEL----DGEYELTVYQKD---------GEPL--EPEQL 782
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493580923 148 SGGEQQ------RVALAR--------AFCTQPAILfaDEPTGNLDRKTGDKIADLLFSLNRDYATTLILVTHDNELAA 211
Cdd:PRK02224 783 SGGERAlfnlslRCAIYRllaegiegDAPLPPLIL--DEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDELVG 858
|
|
| |
