|
Name |
Accession |
Description |
Interval |
E-value |
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-233 |
4.36e-160 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 442.33 E-value: 4.36e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAA 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RADLRNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAELTLMGAR 233
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAE 233
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-223 |
6.87e-141 |
|
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: 393.26 E-value: 6.87e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADL 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-226 |
2.37e-126 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 356.66 E-value: 2.37e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 3 KILLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARA 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 83 DLRNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVN 162
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 163 KPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAE 226
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-223 |
8.78e-119 |
|
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: 337.15 E-value: 8.78e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLR 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-226 |
4.62e-97 |
|
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: 282.79 E-value: 4.62e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAA 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RADLRNRELGFIYQFHHLLPDFTALENVAMPL-LIGkqkAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLeLAG---RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAE 226
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-223 |
1.44e-88 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 260.76 E-value: 1.44e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTvqtDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLR 85
Cdd:COG2884 2 IRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:COG2884 79 -RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRMN-RQLEMRDGHL 223
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPkRVLELEDGRL 215
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-221 |
1.95e-73 |
|
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: 222.12 E-value: 1.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTvqtDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADL 84
Cdd:TIGR02673 1 MIEFHNVSKAYPGGV---AALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRMN-RQLEMRDG 221
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDRVAhRVIILDDG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-223 |
3.66e-72 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 219.93 E-value: 3.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADL 84
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnRELGFIYQFHHLLPDFTALENV------AMPL---LIGKQKAADIERqAKAMLHAVGLEHRSNHRPSELSGGERQRVA 155
Cdd:COG3638 79 R-RRIGMIFQQFNLVPRLSVLTNVlagrlgRTSTwrsLLGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 156 IARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKR-MNRQLEMRDGHL 223
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-206 |
4.15e-69 |
|
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: 211.18 E-value: 4.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRlsaaaradlR 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL 206
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI 192
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
3.59e-68 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 210.33 E-value: 3.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaa 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 radlrnRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:COG1116 80 ------PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL 206
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-221 |
2.13e-66 |
|
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: 204.74 E-value: 2.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRnRE 88
Cdd:cd03258 5 KNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR-RR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVL 168
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 169 ADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRIcDRVAVMEKG 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-223 |
1.24e-65 |
|
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: 211.30 E-value: 1.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVQT-DVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAD 83
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 84 LRnRELGFIYQ--FHHLLPDFTALENVAMPLLI-GKQKAADIERQAKAMLHAVGLEHRSNHR-PSELSGGERQRVAIARA 159
Cdd:COG1123 340 LR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIaDRVAVMYDGRI 483
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-205 |
1.80e-64 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 203.79 E-value: 1.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAA 80
Cdd:COG3842 1 MAMPALELENVSKRY--GDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RadlrnrELGFIYQ----FHHLlpdfTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAI 156
Cdd:COG3842 77 R------NVGMVFQdyalFPHL----TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055389599 157 ARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHD 205
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-223 |
9.44e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 201.46 E-value: 9.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRnRE 88
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR-RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVL 168
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 169 ADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRIcDRVAVLENGRI 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-212 |
2.14e-63 |
|
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: 197.51 E-value: 2.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAA 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF--GDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RADLRnRELGFIYQFHHLLPDFTALENVAMPLLI-GKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:COG1127 77 LYELR-RRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM 212
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAI 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-223 |
4.64e-63 |
|
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: 196.19 E-value: 4.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADL 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnRELGFIYQ--FHHLLPDFTALENVAMPLLI--GKQKAADIERQAKAMLHAVGL-EHRSNHRPSELSGGERQRVAIARA 159
Cdd:cd03257 81 R-KEIQMVFQdpMSSLNPRMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIaDRVAVMYAGKI 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-226 |
9.57e-63 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 195.38 E-value: 9.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADL 84
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAE 226
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
10-224 |
2.06e-62 |
|
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: 194.08 E-value: 2.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRnREL 89
Cdd:TIGR02982 6 NLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR-RRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQFHHLLPDFTALENVAMPL-LIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVL 168
Cdd:TIGR02982 85 GYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 169 ADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLD 224
Cdd:TIGR02982 165 ADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-222 |
3.42e-62 |
|
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: 194.32 E-value: 3.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLR 85
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDFTALENVAMPLL---------IGKQKAADIERqAKAMLHAVGLEHRSNHRPSELSGGERQRVAI 156
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVLSGRLgrrstwrslFGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 157 ARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKR-MNRQLEMRDGH 222
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGR 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-223 |
4.84e-62 |
|
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: 193.01 E-value: 4.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRnREL 89
Cdd:cd03292 5 NVTKTYPNGTA---ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLA 169
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 170 DEPTGNLDARNADSIFQLLGELNVAQRTAfLVVTHDLQLAKRMN-RQLEMRDGHL 223
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTV-VVATHAKELVDTTRhRVIALERGKL 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-223 |
3.75e-61 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 202.26 E-value: 3.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADL 84
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RNRELGFIYQFHHLLPDFTALENVAMP-LLIGKQKAADIERqAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNK 163
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPaVYAGLERKQRLLR-AQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 164 PRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-229 |
6.18e-61 |
|
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: 191.55 E-value: 6.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrLSAAARADL 84
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP---VTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnRELGFIYQ-----FHhllPDFTALENVAMPLLIgkQKAADIERQAKAMLHAVGL--EHRSNhRPSELSGGERQRVAIA 157
Cdd:COG1124 78 R-RRVQMVFQdpyasLH---PRHTVDRILAEPLRI--HGLPDREERIAELLEQVGLppSFLDR-YPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 158 RALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAELTL 229
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTV 223
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
10-218 |
2.87e-60 |
|
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: 188.21 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRNREL 89
Cdd:TIGR03608 3 NISKKFGDKVI----LDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLA 169
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055389599 170 DEPTGNLDARNADSIFQLLGELNVAQRTaFLVVTHDLQLAKRMNRQLEM 218
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKT-IIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-223 |
3.54e-60 |
|
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: 188.11 E-value: 3.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEgtvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaaradlRNRE 88
Cdd:cd03259 4 KGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------ERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVL 168
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 169 ADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALaDRIAVMNEGRI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-226 |
4.37e-59 |
|
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: 186.00 E-value: 4.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLR 85
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFhhllPD---F--TALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:COG1122 75 -RKVGLVFQN----PDdqlFapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTaFLVVTHDLQLAKRM-NRQLEMRDGHLDAE 226
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKT-VIIVTHDLDLVAELaDRVIVLDDGRIVAD 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-211 |
1.05e-57 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 182.89 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrLSAAARADL 84
Cdd:COG1126 1 MIEIENLHKSF--GDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnRELGFIYQFHHLLPDFTALENVAM-PLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNK 163
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 164 PRLVLADEPTGNLDArnadsifQLLGE-LNV-----AQRTAFLVVTHDLQLAKR 211
Cdd:COG1126 155 PKVMLFDEPTSALDP-------ELVGEvLDVmrdlaKEGMTMVVVTHEMGFARE 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-223 |
1.64e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 182.60 E-value: 1.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrlsaAARADLRN--R 87
Cdd:PRK09493 6 NVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN----DPKVDERLirQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 88 ELGFIYQFHHLLPDFTALENVAM-PLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRL 166
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 167 VLADEPTGNLDArnadsifQLLGE-LNVAQRTA-----FLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:PRK09493 158 MLFDEPTSALDP-------ELRHEvLKVMQDLAeegmtMVIVTHEIGFAEKVaSRLIFIDKGRI 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
3.58e-57 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 184.89 E-value: 3.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLqcDNLCKRYQEgtvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaa 80
Cdd:COG3839 1 MASLEL--ENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 radlRNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:COG3839 73 ----KDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 161 VNKPRLVLADEPTGNLDA--RNA--DSIFQLLGELNvaqrTAFLVVTHD----LQLAKRMnrqLEMRDGHL 223
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAklRVEmrAEIKRLHRRLG----TTTIYVTHDqveaMTLADRI---AVMNDGRI 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-211 |
1.18e-56 |
|
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: 180.62 E-value: 1.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdl 84
Cdd:COG1120 1 MLEAENLSVGYG----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 rnRELGFIYQFHHLLPDFTALENVAM---PLL--IGKQKAADIERQAKAMlHAVGLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDREAVEEAL-ERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKR 211
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAAR 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-212 |
1.41e-56 |
|
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: 180.01 E-value: 1.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLR 85
Cdd:cd03261 1 IELRGLTKSFGGRTV----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NReLGFIYQFHHLLPDFTALENVAMPLLI-GKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM 212
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAI 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-223 |
2.79e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 178.09 E-value: 2.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAAradLR 85
Cdd:COG4619 1 LELEGLSFRVG----GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDfTALENVAMPLLIgKQKAADIERqAKAMLHAVGLEHRSNHRP-SELSGGERQRVAIARALVNKP 164
Cdd:COG4619 74 -RQVAYVPQEPALWGG-TVRDNLPFPFQL-RERKFDRER-ALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-224 |
2.61e-55 |
|
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: 176.66 E-value: 2.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAaradlrNRE 88
Cdd:cd03300 4 ENVSKFYGGFVA----LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH------KRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVL 168
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 169 ADEPTGNLDARNADSIfQLlgELNVAQR---TAFLVVTHDLQLAKRM-NRQLEMRDGHLD 224
Cdd:cd03300 154 LDEPLGALDLKLRKDM-QL--ELKRLQKelgITFVFVTHDQEEALTMsDRIAVMNKGKIQ 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-212 |
1.00e-54 |
|
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: 177.55 E-value: 1.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQ--EGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTP---TSGDVIFSGQSMNRLSAA 79
Cdd:COG0444 1 LLEVRNLKVYFPtrRGVVK--AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 80 ARADLRNRELGFIYQ--FHHLLPDFTALENVAMPLLI-GKQKAADIERQAKAMLHAVGL---EHRSNHRPSELSGGERQR 153
Cdd:COG0444 79 ELRKIRGREIQMIFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 154 VAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM 212
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEI 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-223 |
2.58e-54 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 173.91 E-value: 2.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRnRELGFIYQFHHLLPDFTA 104
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 105 LENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSI 184
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2055389599 185 FQLLGELNVAQRTAfLVVTHDLQLAKRMN-RQLEMRDGHL 223
Cdd:PRK10908 177 LRLFEEFNRVGVTV-LMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-222 |
3.33e-54 |
|
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: 173.04 E-value: 3.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 7 QCDNLCKRYQEGtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlrn 86
Cdd:cd03225 1 ELKNLSFSYPDG--ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 87 RELGFIYQFhhllPD--F---TALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALV 161
Cdd:cd03225 75 RKVGLVFQN----PDdqFfgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 162 NKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKR-MNRQLEMRDGH 222
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-216 |
5.85e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 173.35 E-value: 5.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEgtvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRlsaaa 80
Cdd:COG1121 2 MMMPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 radlRNRELGFIYQFHHLLPDF--TALENVAMPL-----LIGKQKAADIERqAKAMLHAVGLEHRSNHRPSELSGGERQR 153
Cdd:COG1121 73 ----ARRRIGYVPQRAEVDWDFpiTVRDVVLMGRygrrgLFRRPSRADREA-VDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 154 VAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKR-------MNRQL 216
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREyfdrvllLNRGL 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-214 |
1.65e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 173.02 E-value: 1.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrlsAAARADLR 85
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-----LFTNLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQfHHLL-PDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:COG1118 74 ERRVGFVFQ-HYALfPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHD----LQLAKR---MNR 214
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDqeeaLELADRvvvMNQ 209
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-223 |
2.00e-52 |
|
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: 169.40 E-value: 2.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADL 84
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnRELGFIYQFHHLLPDFTALENVAMPLL---------IGKQKAADIERqAKAMLHAVGLEHRSNHRPSELSGGERQRVA 155
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGRLgykptwrslLGRFSEEDKER-ALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 156 IARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYaDRIVGLKAGEI 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-229 |
4.15e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.32 E-value: 4.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadlr 85
Cdd:COG1131 1 IEVRGLTKRY--GDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAELTL 229
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTP 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-228 |
6.72e-52 |
|
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: 175.48 E-value: 6.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVqtDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPT---SGDVIFSGQSMNRLSAAar 81
Cdd:COG1123 4 LLEVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 82 adLRNRELGFIYQ--FHHLLPdFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:COG1123 80 --LRGRRIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAELT 228
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGP 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-222 |
1.21e-51 |
|
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: 165.44 E-value: 1.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlR 85
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQFHHLLPDFTALENVAMPlligkqkaadierqakamlhavglehrsnhrpseLSGGERQRVAIARALVNKPR 165
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGH 222
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-223 |
1.34e-51 |
|
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: 166.55 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdLR 85
Cdd:cd03262 1 IEIKNLHKSF--GDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINE-LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDFTALENVAM-PLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 165 RLVLADEPTGNLDArnadsifQLLGE-LNVAQRTA-----FLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03262 155 KVMLFDEPTSALDP-------ELVGEvLDVMKDLAeegmtMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-211 |
1.66e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 169.98 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRnREL 89
Cdd:PRK11153 6 NISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR-RQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLA 169
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2055389599 170 DEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKR 211
Cdd:PRK11153 165 DEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKR 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-221 |
3.21e-51 |
|
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: 165.51 E-value: 3.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAaradlr 85
Cdd:cd03301 1 VELENVTKRFGNVTA----LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 166 LVLADEPTGNLDARNAdsiFQLLGELNVAQR---TAFLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:cd03301 151 VFLMDEPLSNLDAKLR---VQMRAELKRLQQrlgTTTIYVTHDQVEAMTMaDRIAVMNDG 207
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-223 |
5.28e-50 |
|
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: 163.97 E-value: 5.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 17 EGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRNRELGFIYQFH 96
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 97 HLLPDFTALENVAMPLLIGKQKAAdiERQAKAM--LHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTG 174
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGVPRA--EREERAAeaLELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 175 NLDA--RN--ADSIFQLLGELnvaQRTaFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03294 190 ALDPliRRemQDELLRLQAEL---QKT-IVFITHDLDEALRLgDRIAIMKDGRL 239
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-173 |
4.49e-49 |
|
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: 157.81 E-value: 4.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAAradlRNRELGFIYQFHHLLPDFTA 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS----LRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 105 LENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHR----PSELSGGERQRVAIARALVNKPRLVLADEPT 173
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-209 |
2.16e-48 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 159.64 E-value: 2.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaaradlr 85
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nrELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:COG4525 77 --DRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLgeLNVAQRTA--FLVVTHDLQLA 209
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELL--LDVWQRTGkgVFLITHSVEEA 198
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-223 |
6.09e-48 |
|
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: 157.88 E-value: 6.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGtvqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaaradlR 85
Cdd:cd03299 1 LKVENLSKDWKEF-----KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP------E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALaDKVAIMLNGKL 208
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-223 |
8.42e-48 |
|
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: 158.77 E-value: 8.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGT-VQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRnR 87
Cdd:TIGR04521 4 KNVSYIYQPGTpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 88 ELGFIYQF--HHLLPDfTALENVAM-PLLIGKQKAaDIERQAKAMLHAVGLE----HRSnhrPSELSGGERQRVAIARAL 160
Cdd:TIGR04521 83 KVGLVFQFpeHQLFEE-TVYKDIAFgPKNLGLSEE-EAEERVKEALELVGLDeeylERS---PFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL-QLAKRMNRQLEMRDGHL 223
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMeDVAEYADRVIVMHKGKI 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-208 |
1.55e-47 |
|
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: 156.15 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 7 QCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrlsaaarADLRN 86
Cdd:cd03235 1 EVEDLTVSYGGHPV----LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP---------LEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 87 RELGFIYQFHHLLPDF--TALENVAMPL-----LIGKQKAADIERqAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:cd03235 68 KRIGYVPQRRSIDRDFpiSVRDVVLMGLyghkgLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAfLVVTHDLQL 208
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTI-LVVTHDLGL 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-222 |
3.48e-47 |
|
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: 153.69 E-value: 3.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLR 85
Cdd:cd03228 1 IEFKNVSFSYPGRPKP--VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NReLGFIYQFHHLLPDfTALENVamplligkqkaadierqakamlhavglehrsnhrpseLSGGERQRVAIARALVNKPR 165
Cdd:cd03228 76 KN-IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELnvAQRTAFLVVTHDLQLAKRMNRQLEMRDGH 222
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-222 |
7.41e-47 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 158.96 E-value: 7.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEgtvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaa 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDG----KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 radlRNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:PRK09452 84 ----ENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADsifQLLGELNVAQRT---AFLVVTHDLQLAKRM-NRQLEMRDGH 222
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRK---QMQNELKALQRKlgiTFVFVTHDQEEALTMsDRIVVMRDGR 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-208 |
1.32e-46 |
|
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: 154.81 E-value: 1.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 4 ILLQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAD 83
Cdd:COG0411 3 PLLEVRGLTKRF--GGLV--AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 84 LRnreLGFIYQFHHLLPDFTALENVAMPLLIG---------------KQKAADIERQAKAMLHAVGLEHRSNHRPSELSG 148
Cdd:COG0411 79 LG---IARTFQNPRLFPELTVLENVLVAAHARlgrgllaallrlpraRREEREARERAEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 149 GERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQL 208
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDL 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-223 |
2.55e-46 |
|
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: 151.40 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadlr 85
Cdd:cd03230 1 IEVRNLSKRYGKKTA----LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDFTALENVamplligkqkaadierqakamlhavglehrsnhrpsELSGGERQRVAIARALVNKPR 165
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
10-214 |
3.43e-46 |
|
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: 153.26 E-value: 3.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrlsaAARADLRNREL 89
Cdd:cd03296 7 NVSKRFGDFVA----LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED------ATDVPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQFHHLLPDFTALENVAMPLLIGKQK----AADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHD----LQLAKR---MNR 214
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDqeeaLEVADRvvvMNK 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-226 |
1.58e-45 |
|
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: 149.89 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 7 QCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlrn 86
Cdd:cd03214 1 EVENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 87 RELGFIYQfhhllpdftalenvamplligkqkaadierqakaMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRL 166
Cdd:cd03214 73 RKIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 167 VLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAE 226
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQ 179
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-206 |
2.15e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 153.73 E-value: 2.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRY---------QEGTVQTdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQ 71
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrTVGVVKA--VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 72 SMNRLSAAARADLRnRELGFIYQ--FHHLLPDFTALENVAMPLLI-GKQKAADIERQAKAMLHAVGL--EHRsnHR-PSE 145
Cdd:COG4608 81 DITGLSGRELRPLR-RRMQMVFQdpYASLNPRMTVGDIIAEPLRIhGLASKAERRERVAELLELVGLrpEHA--DRyPHE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 146 LSGGERQRVAIARALVNKPRLVLADEPTGNLDArnadSIfQ-----LLGELnvaQRT---AFLVVTHDL 206
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDV----SI-QaqvlnLLEDL---QDElglTYLFISHDL 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-223 |
3.37e-45 |
|
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: 158.39 E-value: 3.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLR 85
Cdd:COG4987 334 LELEDVSFRYPGA--GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD---EDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NReLGFIYQFHHLLPDfTALENvampLLIGKQKAADieRQAKAMLHAVGLEHRSNHRP-----------SELSGGERQRV 154
Cdd:COG4987 409 RR-IAVVPQRPHLFDT-TLREN----LRLARPDATD--EELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 155 AIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTaFLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRT-VLLITHRLAGLERMDRILVLEDGRI 547
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-223 |
6.08e-45 |
|
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: 157.15 E-value: 6.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKS----TLLHLLGGLDTPTSGDVIFSGQSMNRL 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 77 SAAARADLRNRELGFIYQfhhlLPdFTALeNvamPLL-IGKQ-----------KAADIERQAKAMLHAVGL---EHRSNH 141
Cdd:COG4172 82 SERELRRIRGNRIAMIFQ----EP-MTSL-N---PLHtIGKQiaevlrlhrglSGAAARARALELLERVGIpdpERRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 142 RPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRD 220
Cdd:COG4172 153 YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFaDRVAVMRQ 232
|
...
gi 2055389599 221 GHL 223
Cdd:COG4172 233 GEI 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-223 |
9.28e-45 |
|
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: 158.84 E-value: 9.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLR 85
Cdd:COG2274 474 IELENVSFRYPGDS--PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NReLGFIYQFHHLLPDfTALENVAMplliGKQKA--ADIERQAK-AMLHAV------GLEHRSNHRPSELSGGERQRVAI 156
Cdd:COG2274 549 RQ-IGVVLQDVFLFSG-TIRENITL----GDPDAtdEEIIEAARlAGLHDFiealpmGYDTVVGEGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 157 ARALVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAfLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTV-IIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-223 |
1.53e-44 |
|
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: 156.46 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrLSAAARADLR 85
Cdd:COG4988 337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD---LSDLDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NReLGFIYQFHHLLPDfTALENvampLLIGKQKAADIE-RQA--KAMLHAV------GLEHRSNHRPSELSGGERQRVAI 156
Cdd:COG4988 411 RQ-IAWVPQNPYLFAG-TIREN----LRLGRPDASDEElEAAleAAGLDEFvaalpdGLDTPLGEGGRGLSGGQAQRLAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 157 ARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAfLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTV-ILITHRLALLAQADRILVLDDGRI 549
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-221 |
1.70e-44 |
|
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: 148.74 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNkILLQCDNLCKR---YQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIF--SGQSMNR 75
Cdd:COG4778 1 MT-TLLEVENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 76 LSAAARA--DLRNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGL-EHRSNHRPSELSGGERQ 152
Cdd:COG4778 80 AQASPREilALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 153 RVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEEVREAVaDRVVDVTPF 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-221 |
3.90e-44 |
|
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: 148.80 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTV-----QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAA 79
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLfgakqRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 80 ARADLRnRELGFIYQ--FHHLLPDFTALENVAMPLL-IGKQKAADIERQAKAMLHAVGLehRSNH---RPSELSGGERQR 153
Cdd:TIGR02769 82 QRRAFR-RDVQLVFQdsPSAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGL--RSEDadkLPRQLSGGQLQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 154 VAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDG 221
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-205 |
8.01e-44 |
|
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: 146.08 E-value: 8.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadl 84
Cdd:COG4133 2 MLEAENLSCRRGERLL----FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 rnRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADieRQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:COG4133 75 --RRLAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHD 205
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQ 190
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-224 |
9.56e-44 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 150.23 E-value: 9.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 22 TDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaaradlRNRELGFIYQFHHLLPD 101
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDRKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENVAMPLLI----GKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLD 177
Cdd:PRK10851 89 MTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2055389599 178 ARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLD 224
Cdd:PRK10851 169 AQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVaDRVVVMSQGNIE 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-211 |
1.30e-43 |
|
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: 146.81 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlr 85
Cdd:cd03219 1 LEVRGLTKRF--GGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nrELGFIYQFHH--LLPDFTALENVAMPLLIGK----------QKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQR 153
Cdd:cd03219 74 --RLGIGRTFQIprLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 154 VAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTaFLVVTHDLQLAKR 211
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGIT-VLLVEHDMDVVMS 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-223 |
6.10e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 145.99 E-value: 6.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 4 ILLQCDNLCKRYQEGTV------QTdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLS 77
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLsgkhqhQT-VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 78 AAARADLRnRELGFIYQ--FHHLLPDFTALENVAMPL--LIGKQKAADIERqAKAMLHAVGL-EHRSNHRPSELSGGERQ 152
Cdd:PRK10419 81 RAQRKAFR-RDIQMVFQdsISAVNPRKTVREIIREPLrhLLSLDKAERLAR-ASEMLRAVDLdDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 153 RVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFcQRVMVMDNGQI 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-221 |
1.48e-42 |
|
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: 150.61 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 3 KILLQCDNLCKRY-------QEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLdTPTSGDVIFSGQSMNR 75
Cdd:COG4172 273 PPLLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 76 LSAAARADLRnRELGFIYQ--FHHLLPDFTALENVAMPLLI--GKQKAADIERQAKAMLHAVGLEHRSNHR-PSELSGGE 150
Cdd:COG4172 352 LSRRALRPLR-RRMQVVFQdpFGSLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQ 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 151 RQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALaHRVMVMKDG 502
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-226 |
1.55e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 144.49 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdl 84
Cdd:COG4559 1 MLEAENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 rnRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALV--- 161
Cdd:COG4559 75 --RRRAVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 162 ----NKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAE 226
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYaDRILLLHQGRLVAQ 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-223 |
1.44e-41 |
|
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: 141.67 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAAradLRnRE 88
Cdd:cd03295 4 ENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LR-RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQFHHLLPDFTALENVAM-PLLIGKQKAAdIERQAKAMLHAVGLEHRS--NHRPSELSGGERQRVAIARALVNKPR 165
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALvPKLLKWPKEK-IRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLaDRIAIMKNGEI 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
24-212 |
1.50e-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: 1.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGL-----DTPTSGDVIFSGQsmNRLSAAARADLRNRELGFIYQFHHL 98
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGK--DIYDLDVDVLELRRRVGMVFQKPNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 99 LPdFTALENVAMPL-LIGKQKAADIERQAKAMLHAVGL--EHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGN 175
Cdd:cd03260 93 FP-GSIYDNVAYGLrLHGIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 2055389599 176 LDARNADSIFQLLGELnvAQRTAFLVVTHDLQLAKRM 212
Cdd:cd03260 172 LDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARV 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-223 |
1.82e-41 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 141.30 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMN---RLSAAARA 82
Cdd:COG4161 3 IQLKNINCFY--GSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 83 DLRnRELGFIYQFHHLLPDFTALEN-VAMPL-LIGKQKAADIERqAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:COG4161 79 LLR-QKVGMVFQQYNLWPHLTVMENlIEAPCkVLGLSKEQAREK-AMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 161 VNKPRLVLADEPTGNLD---ARNADSIFQLLGELNVAQrtafLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:COG4161 157 MMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQTGITQ----VIVTHEVEFARKVaSQVVYMEKGRI 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-226 |
1.92e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 141.83 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 4 ILLQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAD 83
Cdd:PRK13548 1 AMLEARNLSVRLG----GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 84 LRnrelGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALV-- 161
Cdd:PRK13548 77 RR----AVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 162 ----NKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAE 226
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYaDRIVLLHQGRLVAD 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-223 |
4.45e-41 |
|
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: 142.63 E-value: 4.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 40 IVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaaradlRNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKA 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP------HLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 120 ADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADsifQLLGELNVAQR--- 196
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRD---QMQLELKTIQEqlg 151
|
170 180
....*....|....*....|....*...
gi 2055389599 197 TAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMsDRIAIMRKGKI 179
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-223 |
8.01e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 146.85 E-value: 8.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGTvqtDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLRNRe 88
Cdd:COG1132 343 ENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQ- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQFHHLLPDfTALENVAMplliGKQKA--ADIERQAK-AMLHAV------GLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:COG1132 416 IGVVPQDTFLFSG-TIRENIRY----GRPDAtdEEVEEAAKaAQAHEFiealpdGYDTVVGERGVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFlVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTI-VIAHRLSTIRNADRILVLDDGRI 552
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-222 |
9.26e-41 |
|
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: 136.99 E-value: 9.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlrnREL 89
Cdd:cd00267 4 NLSFRYGGRTA----LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQfhhllpdftalenvamplligkqkaadierqakamlhavglehrsnhrpseLSGGERQRVAIARALVNKPRLVLA 169
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 170 DEPTGNLDARNADSIFQLLGELNVAQRTaFLVVTHDLQLAKR-MNRQLEMRDGH 222
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELaADRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-229 |
4.74e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 137.68 E-value: 4.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadl 84
Cdd:COG4555 1 MIEVENLSKKYGKVPA----LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 rnRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:COG4555 74 --RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAELTL 229
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSL 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-211 |
1.46e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 136.04 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVQTDvlhnvsFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlr 85
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD------LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nreLGFIYQFHHLLPDFTALENVAMPL-----LIGKQKAadierQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:COG3840 73 ---VSMLFQENNLFPHLTVAQNIGLGLrpglkLTAEQRA-----QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKR 211
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAAR 195
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-228 |
5.38e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 135.58 E-value: 5.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIfsgqSMNRLSAAARADLR 85
Cdd:PRK11247 13 LLLNAVSKRYGERTV----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL----AGTAPLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nrelgFIYQFHHLLPDFTALENVAMPLLiGKQKAAdierqAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:PRK11247 85 -----LMFQDARLLPWKKVIDNVGLGLK-GQWRDA-----ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAELT 228
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMaDRVLLIEEGKIGLDLT 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-226 |
5.43e-39 |
|
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: 135.64 E-value: 5.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGqsMNRLSAAARADLR 85
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NReLGFIYQFhhllPD--FTA----------LENVAMPlligkqkAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQR 153
Cdd:TIGR04520 77 KK-VGMVFQN----PDnqFVGatveddvafgLENLGVP-------REEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 154 VAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAE 226
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-222 |
8.83e-39 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 134.67 E-value: 8.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQS-----MNR 75
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 76 LSAAARADLRNRELGFIYQfhH----LLPDFTALENVAMPLL-IGKQKAADIERQAKAMLHAVGLE-HRSNHRPSELSGG 149
Cdd:PRK11701 78 LSEAERRRLLRTEWGFVHQ--HprdgLRMQVSAGGNIGERLMaVGARHYGDIRATAGDWLERVEIDaARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 150 ERQRVAIARALVNKPRLVLADEPTGNLD----ARNADSIFQLLGELNVaqrtAFLVVTHDLQLAKRM-NRQLEMRDGH 222
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVRELGL----AVVIVTHDLAVARLLaHRLLVMKQGR 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
10-221 |
1.55e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 134.11 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDV------IFSGQSMNRLSAAARAd 83
Cdd:PRK11264 8 NLVKKFHGQTV----LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQKGLIRQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 84 LRnRELGFIYQFHHLLPDFTALENVAM-PLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVN 162
Cdd:PRK11264 83 LR-QHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 163 KPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTaFLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVaDRAIFMDQG 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-223 |
1.79e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 139.00 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 2 NKILLQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAAR 81
Cdd:COG1129 1 AEPLLEMRGISKSF--GGVK--ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 82 ADLRnreLGFIYQFHHLLPDFTALENVAMPLLIGKQKAAD---IERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIAR 158
Cdd:COG1129 77 QAAG---IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDwraMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 159 ALVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHdlqlakRMNRQLE-------MRDGHL 223
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISH------RLDEVFEiadrvtvLRDGRL 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-216 |
4.06e-38 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 132.90 E-value: 4.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaaradl 84
Cdd:PRK11248 1 MLQISHLYADYG----GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 rnrELGFIYQFHHLLPDFTALENVAMPL-LIGKQKAADIERqAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNK 163
Cdd:PRK11248 71 ---ERGVVFQNEGLLPWRNVQDNVAFGLqLAGVEKMQRLEI-AHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 164 PRLVLADEPTGNLDARNADSIFQLLgeLNVAQRTA--FLVVTHDLQLAKRMNRQL 216
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLL--LKLWQETGkqVLLITHDIEEAVFMATEL 199
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-206 |
6.42e-37 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 132.01 E-value: 6.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRY--------QEGTVQTdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQS 72
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrglfkPERLVKA--LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 73 MNRLSAAARADLRnRELGFIYQ--FHHLLPDFTALENVAMPLLIGKQ-KAADIERQAKAMLHAVGL--EHrSNHRPSELS 147
Cdd:PRK11308 79 LLKADPEAQKLLR-QKIQIVFQnpYGSLNPRKKVGQILEEPLLINTSlSAAERREKALAMMAKVGLrpEH-YDRYPHMFS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 148 GGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL 206
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-178 |
7.03e-37 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 132.85 E-value: 7.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEgtvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAaradlrNREL 89
Cdd:PRK11000 8 NVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA------ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLA 169
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
....*....
gi 2055389599 170 DEPTGNLDA 178
Cdd:PRK11000 158 DEPLSNLDA 166
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-209 |
7.59e-37 |
|
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: 128.78 E-value: 7.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYqeGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadlr 85
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDFTALENVA-MPLLIGKQKaADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRfYARLKGLPK-SEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLgeLNVAQRTAFLVVTHDLQLA 209
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLI--LEVRKGRSIILTTHSMDEA 195
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-223 |
8.16e-37 |
|
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: 128.57 E-value: 8.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 27 NVSFSIEEgEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRNRELGFIYQFHHLLPDFTALE 106
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 107 NVAMPLLIGKQKAADIerQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQ 186
Cdd:cd03297 95 NLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 2055389599 187 LLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRL 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-221 |
1.33e-36 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 127.76 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGTvqtDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGqsmNRLSAAARAdlrnRE 88
Cdd:cd03226 3 ENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERR----KS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFI-----YQFhhllpdFTalENVAMPLLIG-KQKAADIERQAKAM----LHAVGLEHrsnhrPSELSGGERQRVAIAR 158
Cdd:cd03226 73 IGYVmqdvdYQL------FT--DSVREELLLGlKELDAGNEQAETVLkdldLYALKERH-----PLSLSGGQKQRLAIAA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 159 ALVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVcDRVLLLANG 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-223 |
2.81e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 127.82 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMN---RLSAAARA 82
Cdd:PRK11124 3 IQLNGINCFY--GAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 83 DLRnRELGFIYQFHHLLPDFTALEN-VAMPL-LIGKQKAADIERqAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:PRK11124 79 ELR-RNVGMVFQQYNLWPHLTVQQNlIEAPCrVLGLSKDQALAR-AEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 161 VNKPRLVLADEPTGNLDAR---NADSIFQLLGELNVAQrtafLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEitaQIVSIIRELAETGITQ----VIVTHEVEVARKTaSRVVYMENGHI 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-212 |
3.62e-36 |
|
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: 127.41 E-value: 3.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADL 84
Cdd:COG0410 3 MLEVENLHAGY--GGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnreLGFIYQFHHLLPDFTALENvampLLIGKQKAADIERQAKAMLHAVG----LEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:COG0410 79 G---IGYVPEGRRIFPSLTVEEN----LLLGAYARRDRAEVRADLERVYElfprLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM 212
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEI 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-212 |
1.30e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 129.57 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYqEGTVQTDvlhNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaaradl 84
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2055389599 165 RLVLADEPTGNLDARNADSIfqLLGELNVAQRTAF--LVVTHDLQLAKRM 212
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRM--QLEVVDILERVGVtcVMVTHDQEEAMTM 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-225 |
3.36e-35 |
|
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: 125.20 E-value: 3.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEgtvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSG-DVIFSGQSMNRLSAAaraD 83
Cdd:COG1119 3 LLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVW---E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 84 LRNReLGFIYQFHHLlpDFTALENVAMPLLIGK-------QKAADIERQ-AKAMLHAVGLEHRSNHRPSELSGGERQRVA 155
Cdd:COG1119 76 LRKR-IGLVSPALQL--RFPRDETVLDVVLSGFfdsiglyREPTDEQRErARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 156 IARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQ-LAKRMNRQLEMRDGHLDA 225
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVA 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-212 |
4.83e-35 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 124.08 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlr 85
Cdd:cd03224 1 LEVENLNAGY--GKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQFHHLLPDFTALENVAMPLLIGKQK--AADIERqAKAMLHAvgLEHRSNHRPSELSGGERQRVAIARALVNK 163
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLLGAYARRRAkrKARLER-VYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055389599 164 PRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM 212
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEI 198
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-228 |
1.15e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.74 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVQTdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrLSAAA 80
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYA--LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RADLRnRELGFIYQFhhllPD--FT----------ALENVAMPlligkqKAADIERQAKAmLHAVGLEHRSNHRPSELSG 148
Cdd:PRK13635 76 VWDVR-RQVGMVFQN----PDnqFVgatvqddvafGLENIGVP------REEMVERVDQA-LRQVGMEDFLNREPHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 149 GERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAELT 228
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-209 |
1.47e-34 |
|
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: 123.34 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaaradlrnrELGFIYQFHHLLPDFTA 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---------DRMVVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 105 LENVAMPLLIGKQKAADIERQA--KAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNAD 182
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRAivEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|....*..
gi 2055389599 183 SIFQLLGELNVAQRTAFLVVTHDLQLA 209
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEA 178
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-207 |
1.97e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 122.21 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGG-LDTP--TSGDVIFSGQSMNRLSAAARAdlrnreLGFIYQFHHLLPD 101
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRR------IGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENV--AMPLLIGKQkaadiERQAKAM--LHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLD 177
Cdd:COG4136 91 LSVGENLafALPPTIGRA-----QRRARVEqaLEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190
....*....|....*....|....*....|
gi 2055389599 178 ARNADSIFQLLGELNVAQRTAFLVVTHDLQ 207
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-218 |
3.04e-34 |
|
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: 128.17 E-value: 3.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 22 TDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMnrlsAAARADLRNRELGFIYQFHHLLPD 101
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL----ADADADSWRDQIAWVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 fTALENVAMPLliGKQKAADIERQA-KAMLHAV------GLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTG 174
Cdd:TIGR02857 411 -TIAENIRLAR--PDASDAEIREALeRAGLDEFvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2055389599 175 NLDARNADSIFQLLGELnvAQRTAFLVVTHDLQLAKRMNRQLEM 218
Cdd:TIGR02857 488 HLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-221 |
3.29e-34 |
|
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: 121.93 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 21 QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLRnRELGFIYQFHHLlp 100
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQDVTL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 101 dF--TALENVAMplliGKQKAADIERQAKAML---------HAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLA 169
Cdd:cd03245 90 -FygTLRDNITL----GAPLADDERILRAAELagvtdfvnkHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 170 DEPTGNLDARNADSIFQLLGELnVAQRTAfLVVTHDLQLAKRMNRQLEMRDG 221
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQL-LGDKTL-IIITHRPSLLDLVDRIIVMDSG 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-205 |
9.02e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.06 E-value: 9.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaa 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTV----IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 radLRNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:PRK11432 75 ---IQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055389599 161 VNKPRLVLADEPTGNLDA---RNA-DSIFQLLGELNVAQrtafLVVTHD 205
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDAnlrRSMrEKIRELQQQFNITS----LYVTHD 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-221 |
9.97e-34 |
|
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: 119.24 E-value: 9.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLsaaARADLR 85
Cdd:cd03246 1 LEVENVSFRYPGA--EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDfTALENVamplligkqkaadierqakamlhavglehrsnhrpseLSGGERQRVAIARALVNKPR 165
Cdd:cd03246 76 -DHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNVAQRTAfLVVTHDLQLAKRMNRQLEMRDG 221
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATR-IVIAHRPETLASADRILVLEDG 171
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-222 |
1.00e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 121.87 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGT-----VQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAA 79
Cdd:COG4167 4 LLEVRNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 80 ARAdlrnRELGFIYQ--FHHLLPDFTALENVAMPLLIGKQKAAdIERQAK--AMLHAVGL--EHrSNHRPSELSGGERQR 153
Cdd:COG4167 84 YRC----KHIRMIFQdpNTSLNPRLNIGQILEEPLRLNTDLTA-EEREERifATLRLVGLlpEH-ANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 154 VAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQ-LEMRDGH 222
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKvLVMHQGE 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-216 |
1.03e-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: 120.29 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 29 SFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMnrlsaaARADLRNRELGFIYQFHHLLPDFTALENV 108
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV------TAAPPADRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 109 AMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLL 188
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180
....*....|....*....|....*...
gi 2055389599 189 GELNVAQRTAFLVVTHDLQLAKRMNRQL 216
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRV 199
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-228 |
1.46e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.72 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrLSAAARADL 84
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP---IKYDKKSLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RNRE-LGFIYQFhhllPD---F--TALENVAM-PLLIGKQKAaDIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIA 157
Cdd:PRK13639 75 EVRKtVGIVFQN----PDdqlFapTVEEDVAFgPLNLGLSKE-EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 158 RALVNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLA-KRMNRQLEMRDGHLDAELT 228
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-204 |
4.05e-33 |
|
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: 124.91 E-value: 4.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEgtvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDT--PTSGDVIFS-------------- 69
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 70 ---------GQSMN-------RLSAAARADLRNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAV 133
Cdd:TIGR03269 77 kvgepcpvcGGTLEpeevdfwNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 134 GLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTH 204
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-212 |
6.04e-33 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 121.87 E-value: 6.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQcdNLCKRYQEGTvqtDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAa 80
Cdd:PRK11650 1 MAGLKLQ--AVRKSYDGKT---QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 radlrNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:PRK11650 75 -----DRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 161 VNKPRLVLADEPTGNLDARnadsifqllgeLNVAQR-----------TAFLVVTHD----LQLAKRM 212
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAK-----------LRVQMRleiqrlhrrlkTTSLYVTHDqveaMTLADRV 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-221 |
6.38e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.54 E-value: 6.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGT-VQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARaDL 84
Cdd:PRK13637 3 IKIENLTHIYMEGTpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLS-DI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnRELGFIYQF-HHLLPDFTALENVAM-PLLIGKQKaADIERQAKAMLHAVGL--EHRSNHRPSELSGGERQRVAIARAL 160
Cdd:PRK13637 82 R-KKVGLVFQYpEYQLFEETIEKDIAFgPINLGLSE-EEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQ-LAKRMNRQLEMRDG 221
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKG 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-205 |
8.35e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 124.02 E-value: 8.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 8 CDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGqsmnrlsaaaraDLRnr 87
Cdd:COG0488 1 LENLSKSFGGRPL----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 88 eLGFIYQFHHLLPDFTALENVAM---PLL-IGKQKAA----------------------------DIERQAKAMLHAVGL 135
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVLDgdaELRaLEAELEEleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 136 EHRSNHRP-SELSGGERQRVAIARALVNKPRLVLADEPTGNLDarnADSIFQLLGELNvAQRTAFLVVTHD 205
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWLEEFLK-NYPGTVLVVSHD 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-229 |
1.64e-32 |
|
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: 120.99 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 28 VSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrlSAAARADL--RNRELGFIYQFHHLLPDFTAL 105
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLppEKRRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 106 ENvampLLIGKQKAADIERQAK--AMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADS 183
Cdd:TIGR02142 94 GN----LRYGMKRARPSERRISfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2055389599 184 IFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAELTL 229
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPI 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-223 |
2.09e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.16 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 15 YQEGT-VQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMN-RLSAAARADLRnRELGFI 92
Cdd:PRK13641 12 YSPGTpMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLR-KKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 93 YQFHHL-LPDFTALENVAM-PLLIG--KQKAadiERQAKAMLHAVGL-EHRSNHRPSELSGGERQRVAIARALVNKPRLV 167
Cdd:PRK13641 91 FQFPEAqLFENTVLKDVEFgPKNFGfsEDEA---KEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 168 LADEPTGNLDARNADSIFQLLGELNVAQRTAFLvVTHDL-QLAKRMNRQLEMRDGHL 223
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVIL-VTHNMdDVAEYADDVLVLEHGKL 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-206 |
2.27e-32 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 116.91 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGtvqtDVLHNVSFSIEEGeMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadlr 85
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELnvAQRTAFLVVTHDL 206
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIV 189
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-221 |
3.00e-32 |
|
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: 117.62 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVQTDVlhnvSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQS-----MNRLSAA 79
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDV----SFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 80 ARADLRNRELGFIYQ--FHHLLPDFTALENVAMPLL-IGKQKAADIERQAKAMLHAVGLEH-RSNHRPSELSGGERQRVA 155
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQnpRDGLRMRVSAGANIGERLMaIGARHYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 156 IARALVNKPRLVLADEPTGNLD----ARNADSIFQLLGELNVaqrtAFLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDvsvqARLLDLLRGLVRDLGL----AVIIVTHDLGVARLLaQRLLVMQQG 225
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-213 |
4.54e-32 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 119.24 E-value: 4.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 16 QEGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTP----TSGDVIFSGQSMNRLSAAARADLRNRELGF 91
Cdd:COG4170 16 PQGRVK--AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 92 IYQ--FHHLLPDFTALENV--AMP--LLIGK--QKAADIERQAKAMLHAVGL-EHRS--NHRPSELSGGERQRVAIARAL 160
Cdd:COG4170 94 IFQepSSCLDPSAKIGDQLieAIPswTFKGKwwQRFKWRKKRAIELLHRVGIkDHKDimNSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL----QLAKRMN 213
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLesisQWADTIT 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-223 |
5.19e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 117.42 E-value: 5.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 3 KILLQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGL---DTPTSGDVIFSGQSMNRLSAA 79
Cdd:PRK09984 2 QTIIRVEKLAKTFN----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 80 ARADLRNR-ELGFIYQFHHLLPDFTALENVamplLIGKQKAADIER------------QAKAMLHAVGLEHRSNHRPSEL 146
Cdd:PRK09984 78 ARDIRKSRaNTGYIFQQFNLVNRLSVLENV----LIGALGSTPFWRtcfswftreqkqRALQALTRVGMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 147 SGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-221 |
5.43e-32 |
|
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: 116.82 E-value: 5.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 23 DVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGqsmNRLSAAARADLRnRELGFIYQ----FHHL 98
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLR-RQVGVVLQenvlFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 99 LPDFTALENVAMPLligkQKAADIERQAKAmlHAVGLEHRSNH------RPSELSGGERQRVAIARALVNKPRLVLADEP 172
Cdd:cd03252 92 IRDNIALADPGMSM----ERVIEAAKLAGA--HDFISELPEGYdtivgeQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055389599 173 TGNLDARNADSIFQLLGELnVAQRTAfLVVTHDLQLAKRMNRQLEMRDG 221
Cdd:cd03252 166 TSALDYESEHAIMRNMHDI-CAGRTV-IIIAHRLSTVKNADRIIVMEKG 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-226 |
6.35e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 117.04 E-value: 6.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlr 85
Cdd:PRK11231 3 LRTENLTVGYGTKRI----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQfHHLLP-DFTALENVAM---PLL--IGKQKAADIERQAKAMlHAVGLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:PRK11231 76 -RRLALLPQ-HHLTPeGITVRELVAYgrsPWLslWGRLSAEDNARVNQAM-EQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAfLVVTHDLQLAKRMNRQLE-MRDGHLDAE 226
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTV-VTVLHDLNQASRYCDHLVvLANGHVMAQ 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
28-222 |
7.48e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 118.66 E-value: 7.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 28 VSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRNrELGFIYQ--FHHLLPDFTAL 105
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS-DIQMIFQdpLASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 106 ENVAMPLLI--GKQKAADIERQAKAMLHAVGL-EHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNAD 182
Cdd:PRK15079 119 EIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2055389599 183 SIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGH 222
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDLAVVKHIsDRVLVMYLGH 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-216 |
8.36e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 121.35 E-value: 8.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKST----LLHLLggldtPTSGDVIFSGQSMNRLSAAARADLRNR-ELGFIYQFHHL 98
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRiQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 99 LPDFTALENVAMPLLIGKQK--AADIERQAKAMLHAVGLEHRSNHR-PSELSGGERQRVAIARALVNKPRLVLADEPTGN 175
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQPTlsAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2055389599 176 LDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQL 216
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQV 496
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-202 |
9.84e-32 |
|
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: 115.83 E-value: 9.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 11 LCKRYQEGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTP---TSGDVIFSGQSMNRlsaaaraDLRNR 87
Cdd:cd03234 11 LKAKNWNKYAR--ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP-------DQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 88 ELGFIYQFHHLLPDFTALENVA-MPLLIGKQKAADIERQAKA---MLHAVGLEHRSNHRPSELSGGERQRVAIARALVNK 163
Cdd:cd03234 82 CVAYVRQDDILLPGLTVRETLTyTAILRLPRKSSDAIRKKRVedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 2055389599 164 PRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVV 202
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI 200
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-223 |
1.33e-31 |
|
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: 113.29 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaarADLR 85
Cdd:cd03216 1 LELRGITKRF--GGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP---RDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQfhhllpdftalenvamplligkqkaadierqakamlhavglehrsnhrpseLSGGERQRVAIARALVNKPR 165
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-223 |
1.37e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 117.49 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGT-VQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARA------ 82
Cdd:PRK13651 7 NIVKIFNKKLpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 83 ---------------DLRnRELGFIYQF-HHLLPDFTALENVAM-PLLIGKQKAADIERqAKAMLHAVGLE----HRSnh 141
Cdd:PRK13651 87 lviqktrfkkikkikEIR-RRVGVVFQFaEYQLFEQTIEKDIIFgPVSMGVSKEEAKKR-AAKYIELVGLDesylQRS-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 142 rPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLvVTHDLQLA-KRMNRQLEMRD 220
Cdd:PRK13651 163 -PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL-VTHDLDNVlEWTKRTIFFKD 240
|
...
gi 2055389599 221 GHL 223
Cdd:PRK13651 241 GKI 243
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-221 |
2.41e-31 |
|
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: 115.02 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAaraDLRnRE 88
Cdd:cd03251 4 KNVTFRYPGD--GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLA---SLR-RQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQFHHLLPDfTALENVAmpllIGKQKA--ADIERQAK-AMLHAV------GLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIA----YGRPGAtrEEVEEAARaANAHEFimelpeGYDTVIGERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFlVVTHDLQLAKRMNRQLEMRDG 221
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTF-VIAHRLSTIENADRIVVLEDG 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-221 |
2.70e-31 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 114.63 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLRNReLGFIYQFHHLLPDfT 103
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSM-IGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMPLLIGKQKAADIERQAKAMLHAV-----GLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDA 178
Cdd:cd03254 93 IMENIRLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2055389599 179 RNADSIFQLLGELNVaQRTAFlVVTHDLQLAKRMNRQLEMRDG 221
Cdd:cd03254 173 ETEKLIQEALEKLMK-GRTSI-IIAHRLSTIKNADKILVLDDG 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-223 |
2.74e-31 |
|
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: 119.91 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRY---QEGTVQTdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFS-GQS---MNRLs 77
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGVVKA--VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdMTKP- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 78 aaaRADLRNRE---LGFIYQFHHLLPDFTALENV--AMPLLIGKQKAadiERQAKAMLHAVGLEHRS-----NHRPSELS 147
Cdd:TIGR03269 356 ---GPDGRGRAkryIGILHQEYDLYPHRTVLDNLteAIGLELPDELA---RMKAVITLKMVGFDEEKaeeilDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 148 GGERQRVAIARALVNKPRLVLADEPTGNLD--ARN--ADSIFQLLGELNvaqrTAFLVVTHDLQLAKRM-NRQLEMRDGH 222
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDpiTKVdvTHSILKAREEME----QTFIIVSHDMDFVLDVcDRAALMRDGK 505
|
.
gi 2055389599 223 L 223
Cdd:TIGR03269 506 I 506
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-218 |
2.92e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.48 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 23 DVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVifsgqsmnrlsaaARAdlRNRELGFIYQfHHLLPD- 101
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------------RRA--GGARVAYVPQ-RSEVPDs 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 --FTALENVAMPL-----LIGKQKAADiERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTG 174
Cdd:NF040873 70 lpLTVRDLVAMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2055389599 175 NLDARNADSIFQLLGELnVAQRTAFLVVTHDLQLAKRMNRQLEM 218
Cdd:NF040873 149 GLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-211 |
9.00e-31 |
|
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: 112.85 E-value: 9.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadlr 85
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL----QLAKR 211
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMeeaeQLCDR 201
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-225 |
9.34e-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: 115.97 E-value: 9.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 27 NVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMnrLSAAARADL--RNRELGFIYQFHHLLPDFTA 104
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLppHRRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 105 LENvampLLIGKQKAADIERQAK-----AMLhavGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDAR 179
Cdd:COG4148 95 RGN----LLYGRKRAPRAERRISfdevvELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2055389599 180 NADSIFQLLGELNVAQRTAFLVVTHDL----QLAKRMnrqLEMRDGHLDA 225
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLdevaRLADHV---VLLEQGRVVA 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-211 |
1.54e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 114.35 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 14 RYQEGT-VQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSG------DVIFSGQSMNRLSaaaraDLRn 86
Cdd:PRK13634 11 RYQYKTpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigeRVITAGKKNKKLK-----PLR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 87 RELGFIYQF-HHLLPDFTALENVAM-PLLIGKQKaADIERQAKAMLHAVGLEHRSNHR-PSELSGGERQRVAIARALVNK 163
Cdd:PRK13634 85 KKVGIVFQFpEHQLFEETVEKDICFgPMNFGVSE-EDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2055389599 164 PRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKR 211
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-204 |
1.66e-30 |
|
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: 111.49 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 18 GTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTP--TSGDVIFSGQSMnrlsaaaRADLRNRELGFIYQF 95
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL-------DKRSFRKIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 96 HHLLPDFTALEnvamplligkqkaadierqakAMLHAVGLehRSnhrpseLSGGERQRVAIARALVNKPRLVLADEPTGN 175
Cdd:cd03213 91 DILHPTLTVRE---------------------TLMFAAKL--RG------LSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180
....*....|....*....|....*....
gi 2055389599 176 LDARNADSIFQLLGELNVAQRTaFLVVTH 204
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTGRT-IICSIH 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-221 |
1.90e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.50 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKS-TLLHLLGGLDTP----TSGDVIFSGQSMNR 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 76 LSAAARADLRNRELGFIYQ--FHHLLPDFTALENVAMPLLIGK---QKAADIErqAKAMLHAVGLEH---RSNHRPSELS 147
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQepMVSLNPLHTLEKQLYEVLSLHRgmrREAARGE--ILNCLDRVGIRQaakRLTDYPHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 148 GGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLaDRVAVMQNG 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-209 |
1.94e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.68 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILlQCDNLCKRYQEGTvqtDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrlsAAA 80
Cdd:PRK13647 1 MDNII-EVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RADLRNReLGFIYQFhhllPD-----FTALENVAM-PLLIGKQKAaDIERQAKAMLHAVGLEHRSNHRPSELSGGERQRV 154
Cdd:PRK13647 74 EKWVRSK-VGLVFQD----PDdqvfsSTVWDDVAFgPVNMGLDKD-EVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 155 AIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLA 209
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLA 201
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-223 |
2.91e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.52 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 27 NVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRNRELGFIYQFHHLLPDFTALE 106
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 107 NVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQ 186
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190
....*....|....*....|....*....|....*...
gi 2055389599 187 LLGELNVAQRTAFLVVTHDLQLAKRMNRQLE-MRDGHL 223
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAiMQNGEV 243
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-221 |
3.25e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.49 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTV-QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdl 84
Cdd:COG1101 2 LELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 rnRELGFIYQfHHLL---PDFTALENVAMPLLIGK-------QKAADIE--RQAKAMLHaVGLEHRSNHRPSELSGGERQ 152
Cdd:COG1101 80 --KYIGRVFQ-DPMMgtaPSMTIEENLALAYRRGKrrglrrgLTKKRRElfRELLATLG-LGLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 153 RVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQR--TAfLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEENnlTT-LMVTHNMEQALDYgNRLIMMHEG 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-206 |
3.83e-30 |
|
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: 111.15 E-value: 3.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAaradlr 85
Cdd:cd03268 1 LKTNDLTKTYGKKRV----LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQFHHLLPDFTALENvamplLIGKQKAADIERQA-KAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTAREN-----LRLLARLLGIRKKRiDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDL 206
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLL 186
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-206 |
3.92e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 112.55 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRNReLGFIYQFHHLLPDFT 103
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMPLLIGKQKAADIERQAKAM-LHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNAD 182
Cdd:PRK11831 101 VFDNVAYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180
....*....|....*....|....
gi 2055389599 183 SIFQLLGELNVAQRTAFLVVTHDL 206
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHDV 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-223 |
6.40e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 111.21 E-value: 6.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 29 SFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAaradlrNRELGFIYQFHHLLPDFTALENV 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 109 AMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLL 188
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 2055389599 189 GELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIaPRSLVVADGRI 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-192 |
6.87e-30 |
|
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: 111.10 E-value: 6.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLr 85
Cdd:cd03218 1 LRAENLSKRYGKRKV----VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nrELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:cd03218 76 --GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180
....*....|....*....|....*..
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELN 192
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILK 180
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-213 |
1.29e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.21 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEgtvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMN------ 74
Cdd:PRK10619 1 MSENKLNVIDLHKRYGE----HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 75 -RLSAAARADLR--NRELGFIYQFHHLLPDFTALENV--AMPLLIGKQKAADIERQAKaMLHAVGLEHRSNHR-PSELSG 148
Cdd:PRK10619 77 gQLKVADKNQLRllRTRLTMVFQHFNLWSHMTVLENVmeAPIQVLGLSKQEARERAVK-YLAKVGIDERAQGKyPVHLSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 149 GERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTaFLVVTHDLQLAKRMN 213
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVS 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-206 |
1.32e-29 |
|
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: 115.15 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMnrlsAAARADLRNRELGFIYQFHHLLpDFT 103
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV----SSLDQDEVRRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENvampLLIGKQKAADIErqAKAMLHAVGLEHRSNHRP-----------SELSGGERQRVAIARALVNKPRLVLADEP 172
Cdd:TIGR02868 425 VREN----LRLARPDATDEE--LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....
gi 2055389599 173 TGNLDARNADSIFQLLgeLNVAQRTAFLVVTHDL 206
Cdd:TIGR02868 499 TEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-230 |
1.67e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 110.15 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 26 HNVSFSIEEGEMMAIVGTSGSGKST----LLHLLGGLDTPTSGDVIFSGQSMNRLSaaaradLRNRELGFIYQfhHLLPD 101
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQ--NPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENVAMPLLIGKQKAADIERQAKAM----LHAVGLEHRS---NHRPSELSGGERQRVAIARALVNKPRLVLADEPTG 174
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLSKQARALileaLEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 175 NLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLE-MRDGHLDAELTLM 230
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAvMDDGRIVERGTVK 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
1.84e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 2 NKILLQCDNLCKRYQEGtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaar 81
Cdd:PRK13632 4 KSVMIKVENVSFSYPNS--ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 82 ADLRNReLGFIYQFhhllPD--F---TALENVAMPL---LIGKQKAAD-IERQAKamlhAVGLEHRSNHRPSELSGGERQ 152
Cdd:PRK13632 79 KEIRKK-IGIIFQN----PDnqFigaTVEDDIAFGLenkKVPPKKMKDiIDDLAK----KVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 153 RVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLV-VTHDLQLAKRMNRQLEMRDGHL 223
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLR-KTRKKTLIsITHDMDEAILADKVIVFSEGKL 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-205 |
2.68e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.42 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 2 NKILLQCDNLckRYQEGTvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAAr 81
Cdd:PRK10247 4 NSPLLQLQNV--GYLAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 82 adlRNRELGFIYQFHHLLPDfTALENVAMPLLIGKQK------AADIERqakamlhaVGL-EHRSNHRPSELSGGERQRV 154
Cdd:PRK10247 79 ---YRQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQpdpaifLDDLER--------FALpDTILTKNIAELSGGEKQRI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 155 AIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHD 205
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-216 |
2.71e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 111.44 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAA 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLV----VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RAdlrnrELGFIYQFHHLLPDFTALENVampLLIGKQ---KAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIA 157
Cdd:PRK13537 79 RQ-----RVGVVPQFDNLDPDFTVRENL---LVFGRYfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 158 RALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTaFLVVTHDLQLAKRMNRQL 216
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRL 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-212 |
3.40e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.97 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRlsaaaraDLR 85
Cdd:COG4152 2 LELKGLTKRF--GDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-------EDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NR------ELGfiyqfhhLLPDFTALENVA-------MPlligkqkAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQ 152
Cdd:COG4152 71 RRigylpeERG-------LYPKMKVGEQLVylarlkgLS-------KAEAKRRADEWLERLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 153 RVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM 212
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELA-AKGTTVIFSSHQMELVEEL 195
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-206 |
4.45e-29 |
|
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: 108.86 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 23 DVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAAradLRnRELGFIYQFHHLLPDf 102
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR-RAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 103 TALENVAMplliGKQKAAD--IERQAK-AMLHAV------GLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPT 173
Cdd:cd03253 90 TIGYNIRY----GRPDATDeeVIEAAKaAQIHDKimrfpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190
....*....|....*....|....*....|...
gi 2055389599 174 GNLDARNADSIFQLLGELnVAQRTAfLVVTHDL 206
Cdd:cd03253 166 SALDTHTEREIQAALRDV-SKGRTT-IVIAHRL 196
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-173 |
9.22e-29 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 108.00 E-value: 9.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlr 85
Cdd:TIGR03410 1 LEVSNLNVYYG----QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQFHHLLPDFTALENvampLLIGKQKAADIERQAKAMLHAV--GLEHRSNHRPSELSGGERQRVAIARALVNK 163
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEEN----LLTGLAALPRRSRKIPDEIYELfpVLKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170
....*....|
gi 2055389599 164 PRLVLADEPT 173
Cdd:TIGR03410 150 PKLLLLDEPT 159
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-223 |
1.42e-28 |
|
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: 105.98 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 23 DVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadlRNRELGFI---YQFHHLL 99
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYVpedRKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 100 PDFTALENVAMPLLigkqkaadierqakamlhavglehrsnhrpseLSGGERQRVAIARALVNKPRLVLADEPTGNLDAR 179
Cdd:cd03215 91 LDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2055389599 180 NADSIFQLLGELnVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03215 139 AKAEIYRLIREL-ADAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-233 |
1.96e-28 |
|
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: 112.15 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 21 QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVifsgqsmnRLSAAARADLRNRELGfiyqfHHL-- 98
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV--------RLDGADLSQWDREELG-----RHIgy 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 99 LPDFTAL------ENVAMpllIGKQKAADIERQAK-AMLHAV------GLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:COG4618 411 LPQDVELfdgtiaENIAR---FGDADPEKVVAAAKlAGVHEMilrlpdGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAeltlMGAR 233
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSLLAAVDKLLVLRDGRVQA----FGPR 550
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-223 |
2.25e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 112.23 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 2 NKILLQCDNLCKRYQEGtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAAr 81
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQ--PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 82 adLRNReLGFIYQFHHLLPDfTALENvampLLIGKQKAADieRQAKAMLHAVGLEHRSNH------------RPseLSGG 149
Cdd:PRK11160 412 --LRQA-ISVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGLEKLLEDdkglnawlgeggRQ--LSGG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 150 ERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLgeLNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-204 |
4.91e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.52 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 15 YQEGT-VQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrlSAAARADLRN--RELGF 91
Cdd:PRK13649 12 YQAGTpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT--STSKNKDIKQirKKVGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 92 IYQF-HHLLPDFTALENVAM-PLLIGKQKaADIERQAKAMLHAVGL-EHRSNHRPSELSGGERQRVAIARALVNKPRLVL 168
Cdd:PRK13649 90 VFQFpESQLFEETVLKDVAFgPQNFGVSQ-EEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 2055389599 169 ADEPTGNLDARNADSIFQLLGELNVAQRTAFLvVTH 204
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVL-VTH 203
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-215 |
5.31e-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: 105.71 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 29 SFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAaradlrNRELGFIYQFHHLLPDFTALENV 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY------QRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 109 AMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLL 188
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180
....*....|....*....|....*..
gi 2055389599 189 GELNVAQRTAFLVVTHDLQLAKRMNRQ 215
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQ 198
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-212 |
6.57e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 105.44 E-value: 6.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMnrlSAAARadlr 85
Cdd:cd03269 1 LEVENVTKRF--GRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL---DIAAR---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDFTALEN-VAMPLLIGKQKaADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:cd03269 70 -NRIGYLPEERGLYPKMKVIDQlVYLAQLKGLKK-EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLvVTHDLQLAKRM 212
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVIL-STHQMELVEEL 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-206 |
6.77e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.12 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMN-RLSAA 79
Cdd:COG3845 1 MMPPALELRGITKRF--GGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 80 ARAdlrnRELGFIYQfhH--LLPDFTALENVAM---PLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRV 154
Cdd:COG3845 77 AIA----LGIGMVHQ--HfmLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 155 AIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHDL 206
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKL 201
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-213 |
7.72e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 7.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 21 QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGL-----DTPTSGDVIFSGQSMNRLSAAaraDLRNReLGFIYQF 95
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVI---ELRRR-VQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 96 HHLLPDFTALENVAMPLLIGK--QKAADIERQAKAMLHAVGL----EHRSNHRPSELSGGERQRVAIARALVNKPRLVLA 169
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2055389599 170 DEPTGNLDARNADSIFQLLGELNvaQRTAFLVVTHDLQLAKRMN 213
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELK--KDMTIVLVTHFPQQAARIS 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-211 |
1.12e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.89 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 3 KILLQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGL-----DTPTSGDVIFSGQSMNrls 77
Cdd:COG1117 9 EPKIEVRNLNVYY--GDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIY--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 78 aAARAD---LRnRELGFIYQFHHLLPdFTALENVAMPL-LIGKQKAADIERQAKAMLHAVGL----EHRSNHRPSELSGG 149
Cdd:COG1117 82 -DPDVDvveLR-RRVGMVFQKPNPFP-KSIYDNVAYGLrLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 150 ERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELnvAQRTAFLVVTHDLQLAKR 211
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAAR 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-226 |
1.18e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 106.22 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVQtdvlHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlr 85
Cdd:PRK10253 8 LRGEQLTLGYGKYTVA----ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQFHHLLPDFTALENVA------MPLLIgKQKAADIERQAKAMlHAVGLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:PRK10253 81 -RRIGLLAQNATTPGDITVQELVArgryphQPLFT-RWRKEDEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQL-EMRDGHLDAE 226
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLiALREGKIVAQ 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-222 |
1.83e-27 |
|
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: 104.93 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAaraDLRNReLGFIYQFHHLLpDFT 103
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR---WLRSQ-IGLVSQEPVLF-DGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMplliGKQKAADIERQA---KAMLHAV------GLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTG 174
Cdd:cd03249 93 IAENIRY----GKPDATDEEVEEaakKANIHDFimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2055389599 175 NLDARNADSIFQLLGELnVAQRTAfLVVTHDLQLAKRMNRQLEMRDGH 222
Cdd:cd03249 169 ALDAESEKLVQEALDRA-MKGRTT-IVIAHRLSTIRNADLIAVLQNGQ 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-212 |
2.19e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.84 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMnrlsaAARADLRNRELGFIYQFHHLLPDFT 103
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-----PARARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVampLLIGK---QKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARN 180
Cdd:PRK13536 131 VRENL---LVFGRyfgMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190
....*....|....*....|....*....|..
gi 2055389599 181 ADSIFQLLGELnVAQRTAFLVVTHDLQLAKRM 212
Cdd:PRK13536 208 RHLIWERLRSL-LARGKTILLTTHFMEEAERL 238
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-206 |
3.11e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 106.35 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRY--QEGTVqTDVlHNVSFSIEEGEMMAIVGTSGSGKS-TLLHLLGGL--DTPTSGDVIFSGQSMNRLSAA 79
Cdd:PRK09473 12 LLDVKDLRVTFstPDGDV-TAV-NDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLaaNGRIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 80 ARADLRNRELGFIYQ--FHHLLPDFTALENVAMPLLIGK--QKAADIERQAKaMLHAVGL---EHRSNHRPSELSGGERQ 152
Cdd:PRK09473 90 ELNKLRAEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKgmSKAEAFEESVR-MLDAVKMpeaRKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 153 RVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL 206
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
3.37e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.83 E-value: 3.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVQTdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQsmnRLSAAA 80
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RADLRnRELGFIYQFhhllPD--FTA----------LENVAMPlligkqkAADIERQAKAMLHAVGLEHRSNHRPSELSG 148
Cdd:PRK13648 78 FEKLR-KHIGIVFQN----PDnqFVGsivkydvafgLENHAVP-------YDEMHRRVSEALKQVDMLERADYEPNALSG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 149 GERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDG 221
Cdd:PRK13648 146 GQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-202 |
7.79e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 107.83 E-value: 7.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTP---TSGDVIFSGQSMNRLSAAARAdlrnrelGFIYQFHHLLPD 101
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS-------AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENV---AMpLLIGKQKAADIERQA-KAMLHAVGLEHRSN------HRPSELSGGERQRVAIARALVNKPRLVLADE 171
Cdd:TIGR00955 114 LTVREHLmfqAH-LRMPRRVTKKEKRERvDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190
....*....|....*....|....*....|.
gi 2055389599 172 PTGNLDARNADSIFQLLGELNVAQRTAFLVV 202
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTI 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-221 |
9.39e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.01 E-value: 9.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 2 NKILLQCDNLCKRYQEG--TVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGqsMNRLSAA 79
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 80 ARADLRNRElGFIYQFhhllPDFTAL-----ENVAM-PLLIGKQkAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQR 153
Cdd:PRK13633 79 NLWDIRNKA-GMVFQN----PDNQIVativeEDVAFgPENLGIP-PEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 154 VAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDG 221
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSG 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-226 |
1.48e-26 |
|
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: 100.85 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadlrnRELGFIYQFHHLLpDFT 103
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS-----SLISVLNQRPYLF-DTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENvampllIGKQkaadierqakamlhavglehrsnhrpseLSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADS 183
Cdd:cd03247 91 LRNN------LGRR----------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2055389599 184 IFQLLGElnVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAE 226
Cdd:cd03247 137 LLSLIFE--VLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-212 |
2.01e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.82 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGL------DTPTSGDVIFSGQSMNRLSAAaraDLRnRELGFIYQFHH 97
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAI---KLR-KEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 98 LLPDFTALENVAMPLLI-GKQKAADIERQAKAMLHAVGL----EHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEP 172
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKShGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2055389599 173 TGNLDARNADSIFQLLGELNvaQRTAFLVVTHDLQLAKRM 212
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELK--NEIAIVIVSHNPQQVARV 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-172 |
2.22e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.03 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlr 85
Cdd:COG1137 4 LEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nrELGFIYqfhhlLP-------DFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIAR 158
Cdd:COG1137 77 --RLGIGY-----LPqeasifrKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170
....*....|....
gi 2055389599 159 ALVNKPRLVLADEP 172
Cdd:COG1137 150 ALATNPKFILLDEP 163
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-208 |
2.43e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 103.67 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKS-TLLHLLGGLDTP---TSGDVIFSGQSMNRLSAAA 80
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RADLRNRELGFIYQ--FHHLLPDFTALENVaMPLLIGKQKAADIERQAKA--MLHAVGL---EHRSNHRPSELSGGERQR 153
Cdd:PRK11022 83 RRNLVGAEVAMIFQdpMTSLNPCYTVGFQI-MEAIKVHQGGNKKTRRQRAidLLNQVGIpdpASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 154 VAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQL 208
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAL 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-223 |
2.86e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 106.08 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVQTDvlhNVSFSIEEGEMMAIVGTSGSGKSTLLH-LLGGLdtPTSGDVIFSGQSMNRLSaaaRADL 84
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAG---PLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELD---PESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnRELGFIYQFHHLLPDfTALENVAMplliGKQKAADIE-----RQAKAM----LHAVGLEHRSNHRPSELSGGERQRVA 155
Cdd:PRK11174 422 R-KHLSWVGQNPQLPHG-TLRDNVLL----GNPDASDEQlqqalENAWVSeflpLLPQGLDTPIGDQAAGLSVGQAQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 156 IARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTafLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT--LMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-204 |
3.45e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.38 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaarADLRNRELGFIYQFHHLLPDFTA 104
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST---TAALAAGVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 105 LENV---AMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNA 181
Cdd:PRK11288 97 AENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180
....*....|....*....|...
gi 2055389599 182 DSIFQLLGELNvAQRTAFLVVTH 204
Cdd:PRK11288 177 EQLFRVIRELR-AEGRVILYVSH 198
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-212 |
3.68e-26 |
|
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: 100.91 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadl 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 rnRELGFIYQFHHLLPDFTALENVA----MPLLIGKQKAADIERQAKAMlhavGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:cd03266 78 --RRLGFVSDSTGLYDRLTARENLEyfagLYGLKGDELTARLEELADRL----GMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM 212
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERL 202
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
4.39e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTvqtDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrLSAAA 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGT---HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RADLRnRELGFIYQF-HHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:PRK13636 77 LMKLR-ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL 206
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDI 202
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-191 |
7.73e-26 |
|
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: 100.43 E-value: 7.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVQTDVlhnvSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLr 85
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDV----SLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nrELGFIYQFHHLLPDFTALENVAMPL-LIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:TIGR04406 77 --GIGYLPQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180
....*....|....*....|....*..
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGEL 191
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKIIKHL 181
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-226 |
8.22e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 101.32 E-value: 8.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILlQCDNLCKRYQEgtvQTDV--LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQsmnRLSA 78
Cdd:PRK13642 1 MNKIL-EVENLVFKYEK---ESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 79 AARADLRnRELGFIYQFhhllPD-----FTALENVAMPLL-IGKQKAADIERQAKAMLhAVGLEHRSNHRPSELSGGERQ 152
Cdd:PRK13642 74 ENVWNLR-RKIGMVFQN----PDnqfvgATVEDDVAFGMEnQGIPREEMIKRVDEALL-AVNMLDFKTREPARLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 153 RVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAE 226
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
2.39e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 2 NKILLQCDNLCKRYQEGTV-QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDV----IFSGQSMNRL 76
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQEnELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 77 SAAARADLRN--------RELGFIYQF--HHLLPDFTALENVAMPLLIGkQKAADIERQAKAMLHAVGLEHRSNHR-PSE 145
Cdd:PRK13631 98 ELITNPYSKKiknfkelrRRVSMVFQFpeYQLFKDTIEKDIMFGPVALG-VKKSEAKKLAKFYLNKMGLDDSYLERsPFG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 146 LSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFlVVTHdlqlakRMNRQLEMRD 220
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVF-VITH------TMEHVLEVAD 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-228 |
3.17e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.81 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTVQTDvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQsmnRLSAAARADLRnREL 89
Cdd:PRK13650 9 NLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIR-HKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQFhhllPD--FT----------ALENVAMPLligkqkaADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIA 157
Cdd:PRK13650 84 GMVFQN----PDnqFVgatveddvafGLENKGIPH-------EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 158 RALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAELT 228
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTST 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-223 |
3.19e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.46 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGL-----DTPTSGDVIFSGQSMnr 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYN----KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 76 lsAAARAD---LRnRELGFIYQFHHLLPdFTALENVAMPLLIG----KQ----------KAADIERQAKAMLH--AVGLe 136
Cdd:PRK14239 75 --YSPRTDtvdLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKgikdKQvldeavekslKGASIWDEVKDRLHdsALGL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 137 hrsnhrpselSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLgeLNVAQRTAFLVVTHDLQLAKRM-NRQ 215
Cdd:PRK14239 150 ----------SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRIsDRT 217
|
....*...
gi 2055389599 216 LEMRDGHL 223
Cdd:PRK14239 218 GFFLDGDL 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-206 |
6.73e-25 |
|
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: 102.21 E-value: 6.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLRnRELGFIYQFHHLLPDfT 103
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT---QASLR-AAIGIVPQDTVLFND-T 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMplliGKQKA--ADIERQAK-AMLHAV------GLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTG 174
Cdd:COG5265 448 IAYNIAY----GRPDAseEEVEAAARaAQIHDFieslpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190
....*....|....*....|....*....|...
gi 2055389599 175 NLDARNADSIfqlLGELN-VAQRTAFLVVTHDL 206
Cdd:COG5265 524 ALDSRTERAI---QAALReVARGRTTLVIAHRL 553
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-211 |
1.04e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.69 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 22 TDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlrnRELGFIYQFHHLLPD 101
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENVAM---PLLIGKQKAADIERQA--KAMlHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNL 176
Cdd:PRK09536 92 FDVRQVVEMgrtPHRSRFDTWTETDRAAveRAM-ERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190
....*....|....*....|....*....|....*
gi 2055389599 177 DARNADSIFQLLGELNVAQRTAfLVVTHDLQLAKR 211
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTA-VAAIHDLDLAAR 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-221 |
1.27e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.42 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIF-SGQSMnrlsaaaradlrnreLgFI----Yqfhhl 98
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV---------------L-FLpqrpY----- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 99 LPDFTALENVAMPlligkQKAADIERQA-KAMLHAVGLEH------RSNHRPSELSGGERQRVAIARALVNKPRLVLADE 171
Cdd:COG4178 437 LPLGTLREALLYP-----ATAEAFSDAElREALEAVGLGHlaerldEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2055389599 172 PTGNLDARNADSIFQLLGELnvAQRTAFLVVTHDLQLAKRMNRQLEMRDG 221
Cdd:COG4178 512 ATSALDEENEAALYQLLREE--LPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-216 |
1.36e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.47 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRY-------QEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLS 77
Cdd:PRK10261 313 ILQVRNLVTRFplrsgllNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 78 AAARADLRnRELGFIYQ--FHHLLPDFTALENVAMPLLI-GKQKAADIERQAKAMLHAVGL--EHRSNHrPSELSGGERQ 152
Cdd:PRK10261 393 PGKLQALR-RDIQFIFQdpYASLDPRQTVGDSIMEPLRVhGLLPGKAAAARVAWLLERVGLlpEHAWRY-PHEFSGGQRQ 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 153 RVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQL 216
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-221 |
1.87e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 100.63 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYqeGTVQTdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAA 80
Cdd:PRK09700 1 MATPYISMAGIGKSF--GPVHA--LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RADLrnrELGFIYQFHHLLPDFTALENvampLLIGKQKA-----------ADIERQAKAMLHAVGLEHRSNHRPSELSGG 149
Cdd:PRK09700 77 AAQL---GIGIIYQELSVIDELTVLEN----LYIGRHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSIS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 150 ERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-206 |
3.04e-24 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 96.02 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLRNRe 88
Cdd:cd03244 6 KNVSLRYRPN--LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQ--------------FHHLLPDFT---ALENVAMPLLIGKQkaadierqakamlhAVGLEHRSNHRPSELSGGER 151
Cdd:cd03244 80 ISIIPQdpvlfsgtirsnldPFGEYSDEElwqALERVGLKEFVESL--------------PGGLDTVVEEGGENLSVGQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 152 QRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLgelnvaqRTAF-----LVVTHDL 206
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTI-------REAFkdctvLTIAHRL 198
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-228 |
3.49e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 15 YQEGT-VQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVifsgqSMNRLSAAARAD---LR--NRE 88
Cdd:PRK13646 12 YQKGTpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV-----TVDDITITHKTKdkyIRpvRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQF--HHLLPDFTALE------NVAMPLLIGKQKAADierqakaMLHAVGLEHR-SNHRPSELSGGERQRVAIARA 159
Cdd:PRK13646 87 IGMVFQFpeSQLFEDTVEREiifgpkNFKMNLDEVKNYAHR-------LLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL-QLAKRMNRQLEMRDGHLDAELT 228
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTS 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-212 |
3.57e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYqegTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRlsaaarADL 84
Cdd:PRK13652 3 LIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK------ENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RN--RELGFIYQFhhllPD-----FTALENVAM-PLLIGKQKAAdIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAI 156
Cdd:PRK13652 74 REvrKFVGLVFQN----PDdqifsPTVEQDIAFgPINLGLDEET-VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 157 ARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM 212
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEM 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-212 |
4.81e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.06 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 21 QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGL-----DTPTSGDVIFSGQSMnrLSAAARADLRNRELGFIYQF 95
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 96 HHLLPDFTALENVAMPL----LIGKQKAADiERQAKAMLHAV---GLEHRSNHRPSELSGGERQRVAIARALVNKPRLVL 168
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVklngLVKSKKELD-ERVEWALKKAAlwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2055389599 169 ADEPTGNLDARNADSIFQLLGELNvaQRTAFLVVTHDLQLAKRM 212
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARV 214
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
23-223 |
6.22e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 99.41 E-value: 6.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 23 DVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAaraDLRnRELGFIYQFHHLLPDf 102
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLA---SLR-RQVALVSQDVVLFND- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 103 TALENVAMPLLiGKQKAADIERqAKAMLHAV--------GLEHRSNHRPSELSGGERQRVAIARALV-NKPRLVLaDEPT 173
Cdd:TIGR02203 421 TIANNIAYGRT-EQADRAEIER-ALAAAYAQdfvdklplGLDTPIGENGVLLSGGQRQRLAIARALLkDAPILIL-DEAT 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2055389599 174 GNLDARNADSIFQLLGELnVAQRTAfLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:TIGR02203 498 SALDNESERLVQAALERL-MQGRTT-LVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-228 |
7.85e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 3 KILLQCDNLCKRyqegtvqtDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARa 82
Cdd:COG1129 254 EVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 83 dLRN---------RELGfiyqfhhLLPDFTALENVAMPLL--------IGKQKaadIERQAKAMLHAVGLEHRSNHRP-S 144
Cdd:COG1129 325 -IRAgiayvpedrKGEG-------LVLDLSIRENITLASLdrlsrgglLDRRR---ERALAEEYIKRLRIKTPSPEQPvG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 145 ELSGGERQRVAIARALVNKPRLVLADEPTGNLD--ARNAdsIFQLLGELnVAQRTAFLVVTHDLQLAKRM-NRQLEMRDG 221
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAE--IYRLIREL-AAEGKAVIVISSELPELLGLsDRILVMREG 470
|
....*..
gi 2055389599 222 HLDAELT 228
Cdd:COG1129 471 RIVGELD 477
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-209 |
1.00e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.15 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQegtvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlrnRE 88
Cdd:COG4604 5 KNVSKRYG----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQFHHLLPDFTALENVAM---PLLIGKQKAADIERQAKAmLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAFgrfPYSKGRLTAEDREIIDEA-IAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLL----GELNvaqRTAFLVVtHDLQLA 209
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLrrlaDELG---KTVVIVL-HDINFA 199
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-221 |
1.07e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.23 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGT-VQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSM--NRLSAAARADLR 85
Cdd:PRK13645 10 DNVSYTYAKKTpFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 nRELGFIYQF--HHLLPDfTALENVAM-PLLIGKQKAaDIERQAKAMLHAVGL-EHRSNHRPSELSGGERQRVAIARALV 161
Cdd:PRK13645 90 -KEIGLVFQFpeYQLFQE-TIEKDIAFgPVNLGENKQ-EAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 162 NKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL-QLAKRMNRQLEMRDG 221
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEG 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-208 |
1.32e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.06 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQeGTVQTDvlhNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAA 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFG-GLLAVN---NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RAdlrnrELGFIYQFHH--LLPDFTALEN--VAM------PLLIGKQKAADIER-QAKAM------LHAVGLEHRSNHRP 143
Cdd:PRK11300 77 IA-----RMGVVRTFQHvrLFREMTVIENllVAQhqqlktGLFSGLLKTPAFRRaESEALdraatwLERVGLLEHANRQA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 144 SELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQL 208
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-223 |
1.36e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.64 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQsmnRLSAAARADLRnRELGFIYQfHHLLPDFT 103
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV---PLVQYDHHYLH-RQVALVGQ-EPVLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMplliGKQKAADIERQAKAMLHAV-----GLEHRSN----HRPSELSGGERQRVAIARALVNKPRLVLADEPTG 174
Cdd:TIGR00958 571 VRENIAY----GLTDTPDEEIMAAAKAANAhdfimEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055389599 175 NLDARnadsIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:TIGR00958 647 ALDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-223 |
1.49e-23 |
|
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: 98.19 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 21 QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLrNRELGFIYQFHHLLP 100
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD---RETF-GKHIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 101 DfTALENVA-MPLLIGKQKAadIERQAKAMLHAV------GLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPT 173
Cdd:TIGR01842 406 G-TVAENIArFGENADPEKI--IEAAKLAGVHELilrlpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2055389599 174 GNLDARNADSIFQLLGELNVAQRTAfLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKARGITV-VVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-221 |
1.49e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 95.24 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCK--RYQEGTV---QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMnrlsAA 79
Cdd:PRK15112 4 LLEVRNLSKtfRYRTGWFrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL----HF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 80 ARADLRNRELGFIYQ--FHHLLPDFTALENVAMPLLIGKQ-KAADIERQAKAMLHAVGL--EHrSNHRPSELSGGERQRV 154
Cdd:PRK15112 80 GDYSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLlpDH-ASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 155 AIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQ-LEMRDG 221
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQvLVMHQG 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-213 |
1.60e-23 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 96.41 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 17 EGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTP----TSGDVIFSGQSMNRLSAAARADLRNRELGFI 92
Cdd:PRK15093 17 DGWVK--AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGHNVSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 93 YQFHHLLPDFTALenvampllIGKQKAADI----------------ERQAKAMLHAVGL-EHRSNHR--PSELSGGERQR 153
Cdd:PRK15093 95 FQEPQSCLDPSER--------VGRQLMQNIpgwtykgrwwqrfgwrKRRAIELLHRVGIkDHKDAMRsfPYELTEGECQK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 154 VAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQ----LAKRMN 213
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQmlsqWADKIN 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-209 |
2.10e-23 |
|
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: 93.19 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLsaaarADLRNRELGFIYQFHHLLPDFT 103
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-----RDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAM--PLLIGKQKAADierqakAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDArNA 181
Cdd:TIGR01189 90 ALENLHFwaAIHGGAQRTIE------DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AG 162
|
170 180
....*....|....*....|....*....
gi 2055389599 182 DSIFQLLGELNVAQRTAFLVVTH-DLQLA 209
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTHqDLGLV 191
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-209 |
2.42e-23 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 93.76 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 30 FSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRlsaaaradlRNRELGFIYQFHHLLPDF-TALENV 108
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK---------GWRHIGYVPQRHEFAWDFpISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 109 AM---PLLIG---KQKAADIeRQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNAD 182
Cdd:TIGR03771 72 VMsgrTGHIGwlrRPCVADF-AAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180
....*....|....*....|....*..
gi 2055389599 183 SIFQLLGELNVAQrTAFLVVTHDLQLA 209
Cdd:TIGR03771 151 LLTELFIELAGAG-TAILMTTHDLAQA 176
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-227 |
2.42e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.40 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 3 KILLQCDNLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARA 82
Cdd:COG3845 255 EVVLEVENLSVRDDRGVP---ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 83 DLRnreLGFIYQ--FHH-LLPDFTALENVAMPLLIGKQKA-------ADIERQAKAMLHAVGLEHRSNHRP-SELSGGER 151
Cdd:COG3845 332 RLG---VAYIPEdrLGRgLVPDMSVAENLILGRYRRPPFSrggfldrKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 152 QRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLgelnVAQR---TAFLVVTHDL----QLAKRMnrqLEMRDGHLD 224
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL----LELRdagAAVLLISEDLdeilALSDRI---AVMYEGRIV 481
|
...
gi 2055389599 225 AEL 227
Cdd:COG3845 482 GEV 484
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-223 |
3.52e-23 |
|
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: 93.30 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 22 TDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrlsaAARADLRNRELGFIYQfHHLLPD 101
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS----QYEHKYLHSKVSLVGQ-EPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENVAMplliGKQKAAD---IERQAKAMLH------AVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEP 172
Cdd:cd03248 102 RSLQDNIAY----GLQSCSFecvKEAAQKAHAHsfiselASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 173 TGNLDARNADSIFQLLGELNvaQRTAFLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:cd03248 178 TSALDAESEQQVQQALYDWP--ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-226 |
4.32e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.48 E-value: 4.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGD---VIFSGQSMNrlsAAARADLRNReLGFIYQFhhllP 100
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLT---AKTVWDIREK-VGIVFQN----P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 101 D--FTA----------LENVAMPlligKQKAADIERQAkamLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVL 168
Cdd:PRK13640 94 DnqFVGatvgddvafgLENRAVP----RPEMIKIVRDV---LADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 169 ADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAE 226
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQ 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-223 |
7.73e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.18 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLRnRELGFIYQfHHLLPDFTA 104
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQ-DAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 105 LENvampLLIGKQKAADIERQAKAMLHAV---------GLEHRSNHRPSELSGGERQRVAIARALV-NKPRLVLaDEPTG 174
Cdd:PRK13657 426 EDN----IRVGRPDATDEEMRAAAERAQAhdfierkpdGYDTVVGERGRQLSGGERQRLAIARALLkDPPILIL-DEATS 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055389599 175 NLDARNADSIFQLLGELnVAQRTAFlVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:PRK13657 501 ALDVETEAKVKAALDEL-MKGRTTF-IIAHRLSTVRNADRILVFDNGRV 547
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-228 |
1.06e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 92.25 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAA 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY--GKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 radLRNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADiERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARAL 160
Cdd:PRK11614 77 ---IMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQ-ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 161 VNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAELT 228
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-221 |
2.47e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.92 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKS-TLLHLLGGLDTptSGDVIFSGQ-----------S 72
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ--AGGLVQCDKmllrrrsrqviE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 73 MNRLSAAARADLRNRELGFIYQ--FHHLLPDFTALENVAMPLLI----GKQKAAdieRQAKAMLHAVGLEHRS---NHRP 143
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIRLhqgaSREEAM---VEAKRMLDQVRIPEAQtilSRYP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 144 SELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQ-LAKRMNRQLEMRDG 221
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQG 245
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-190 |
4.04e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.86 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 26 HNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLrnrelgfIYQFHH--LLPDFT 103
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL-------LYLGHQpgIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMPLLIGKQKAADIERQAkamLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADS 183
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
....*..
gi 2055389599 184 IFQLLGE 190
Cdd:PRK13538 168 LEALLAQ 174
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-223 |
9.44e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.16 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMN--RLSaaaraDLRNrELGFIYQFHHLLPDf 102
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLA-----SLRN-QVALVSQNVHLFND- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 103 TALENVAMPLLiGKQKAADIERQAKaMLHAVG----LEHRSNHRPSE----LSGGERQRVAIARALV-NKPRLVLaDEPT 173
Cdd:PRK11176 432 TIANNIAYART-EQYSREQIEEAAR-MAYAMDfinkMDNGLDTVIGEngvlLSGGQRQRIAIARALLrDSPILIL-DEAT 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2055389599 174 GNLDARNADSIFQLLGELNvAQRTAfLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:PRK11176 509 SALDTESERAIQAALDELQ-KNRTS-LVIAHRLSTIEKADEILVVEDGEI 556
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-224 |
1.06e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 3 KILLQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFsGQSMnrlsaaara 82
Cdd:COG0488 313 KKVLELEGLSKSYGDKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV--------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 83 dlrnrELGFIYQFHHLL-PDFTALENVamplligkQKAAD--IERQAKAMLHAVGLEHRSNHRP-SELSGGERQRVAIAR 158
Cdd:COG0488 379 -----KIGYFDQHQEELdPDKTVLDEL--------RDGAPggTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 159 ALVNKPRLVLADEPTGNLD--ARNAdsifqllgeLNVAQRT---AFLVVTHDLQLAKRM-NRQLEMRDGHLD 224
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDieTLEA---------LEEALDDfpgTVLLVSHDRYFLDRVaTRILEFEDGGVR 508
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-221 |
1.10e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 92.88 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLRnrelgfiyQFHHLLP--- 100
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLR--------QFINYLPqep 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 101 ---DFTALENvampLLIGKQKAADIERQAKAMLHA----------VGLEHRSNHRPSELSGGERQRVAIARALVNKPRLV 167
Cdd:TIGR01193 558 yifSGSILEN----LLLGAKENVSQDEIWAACEIAeikddienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 168 LADEPTGNLDARNADSIFQLLgeLNVAQRTaFLVVTHDLQLAKRMNRQLEMRDG 221
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNL--LNLQDKT-IIFVAHRLSVAKQSDKIIVLDHG 684
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-223 |
2.57e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 88.36 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGqsmnRLSAAaradlrnreLGFIYQFHhllPDFT 103
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSSL---------LGLGGGFN---PELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMPLLIGKQKAADIerqaKAMLHAV----GLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDAR 179
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEI----DEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2055389599 180 NADSIFQLLGELnVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:cd03220 177 FQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLcDRALVLEKGKI 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-222 |
2.79e-21 |
|
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: 85.96 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSgqsmnrlsaaaradlR 85
Cdd:cd03221 1 IELENLSKTYGGKLL----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------S 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQfhhllpdftalenvamplligkqkaadierqakamlhavglehrsnhrpseLSGGERQRVAIARALVNKPR 165
Cdd:cd03221 62 TVKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 166 LVLADEPTGNLDarnADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM-NRQLEMRDGH 222
Cdd:cd03221 91 LLLLDEPTNHLD---LESIEALEEALK-EYPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-211 |
7.43e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 87.39 E-value: 7.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQ-----EG------------TVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVif 68
Cdd:cd03267 1 IEVSNLSKSYRvyskePGligslkslfkrkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 69 sgqSMNRLSAAARADLRNRELGFIY-QFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELS 147
Cdd:cd03267 79 ---RVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 148 GGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQ----LAKR 211
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKdieaLARR 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
21-208 |
7.61e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.48 E-value: 7.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 21 QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQsmnrlsaaaradLRnreLGFIYQFHHLLP 100
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LR---IGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 101 DFTALENVAMPLLIGKQKAaDIerqaKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARN 180
Cdd:PRK09544 81 TLPLTVNRFLRLRPGTKKE-DI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*...
gi 2055389599 181 ADSIFQLLGELNVAQRTAFLVVTHDLQL 208
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-218 |
8.13e-21 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.39 E-value: 8.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRlsaaaRADLRNRELGFIYQFHHLLPDFT 103
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-----QRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMPLLIGKQKAADierQAKAMLHAVGLEHRSNHrpsELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADS 183
Cdd:cd03231 90 VLENLRFWHADHSDEQVE---EALARVGLNGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*
gi 2055389599 184 IFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEM 218
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-223 |
1.09e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.06 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILlQCDNLCKRYQEGTVQTD------------------VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPT 62
Cdd:COG1134 1 MSSMI-EVENVSKSYRLYHEPSRslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 63 SGDVIFSGqsmnRLSAAAradlrnrELGFIyqFHhllPDFTALENVampLLIG----------KQKAADIERQAkamlha 132
Cdd:COG1134 80 SGRVEVNG----RVSALL-------ELGAG--FH---PELTGRENI---YLNGrllglsrkeiDEKFDEIVEFA------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 133 vGLEH------RSnhrpseLSGGERQRVAIARALVNKPRLVLADEPTGNLDARnadsiFQ-----LLGELnVAQRTAFLV 201
Cdd:COG1134 135 -ELGDfidqpvKT------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA-----FQkkclaRIREL-RESGRTVIF 201
|
250 260
....*....|....*....|...
gi 2055389599 202 VTHDLQLAKRM-NRQLEMRDGHL 223
Cdd:COG1134 202 VSHSMGAVRRLcDRAIWLEKGRL 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-221 |
1.42e-20 |
|
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: 85.98 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 16 QEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLH-LLGGLdTPTSGDVIFSGQsmnrlsaaaradlrnreLGFIYQ 94
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS-----------------IAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 95 FHHLLPDfTALENVamplLIGKQkaADIERQAKAmLHAVGLE-------HRSNHRPSE----LSGGERQRVAIARALVNK 163
Cdd:cd03250 74 EPWIQNG-TIRENI----LFGKP--FDEERYEKV-IKACALEpdleilpDGDLTEIGEkginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 164 PRLVLADEPTGNLDARNADSIFQ--LLGELnVAQRTAFLvVTHDLQLAKRMNRQLEMRDG 221
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFEncILGLL-LNNKTRIL-VTHQLQLLPHADQIVVLDNG 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-226 |
2.39e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.77 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdlrnRELGFIYQFHHLLPDFT 103
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMPLL-----IGKQKAADIERQAKAmLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDA 178
Cdd:PRK10575 102 VRELVAIGRYpwhgaLGRFGAADREKVEEA-ISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055389599 179 RNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAE 226
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAARYcDYLVALRGGEMIAQ 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-213 |
2.51e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.63 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGL-----DTPTSGDVIFSGQS-------MNRLsaaaradlrNRELGF 91
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNiyerrvnLNRL---------RRQVSM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 92 IYQFHHLLPdFTALENVAMPL-LIGKQKAADIERQAKAMLHAVGL----EHRSNHRPSELSGGERQRVAIARALVNKPRL 166
Cdd:PRK14258 93 VHPKPNLFP-MSVYDNVAYGVkIVGWRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2055389599 167 VLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMN 213
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-212 |
2.81e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 87.62 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 39 AIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrlSAAARADL--RNRELGFIYQFHHLLPDFTALENvampLLIG- 115
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF--DAEKGICLppEKRRIGYVFQDARLFPHYKVRGN----LRYGm 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 116 KQKAADIERQAKAMLhavGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQ 195
Cdd:PRK11144 102 AKSMVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
170 180
....*....|....*....|.
gi 2055389599 196 RTAFLVVTHDLQ----LAKRM 212
Cdd:PRK11144 179 NIPILYVSHSLDeilrLADRV 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-233 |
3.29e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 88.92 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQE-GTVQTDVLhNVSFSieEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrlsaaARADLRNRE 88
Cdd:TIGR01257 933 NLVKIFEPsGRPAVDRL-NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-----TNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQ----FHHLlpdfTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:TIGR01257 1005 LGMCPQhnilFHHL----TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 165 RLVLADEPTGNLDARNADSIFqllgelnvaqrtaflvvthDLQLAKRMNRQLEMRDGHLDaELTLMGAR 233
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIW-------------------DLLLKYRSGRTIIMSTHHMD-EADLLGDR 1129
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-204 |
3.45e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.71 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRNRELGFIYQF-HHLLPDFT 103
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAM-PLLIGKQKAaDIERQAKAMLHAVGLEHRSNHR-PSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNA 181
Cdd:PRK13643 102 VLKDVAFgPQNFGIPKE-KAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180
....*....|....*....|...
gi 2055389599 182 DSIFQLLGELNVAQRTAFLvVTH 204
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVL-VTH 202
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
25-223 |
5.52e-20 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 88.02 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaaRADLRnRELGFIYQFHHLLpDFTA 104
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVT---RESLR-KSIATVFQDAGLF-NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 105 LENVAmpllIGKQKAADIERQAKAMLHAVG--LEHRSN-------HRPSELSGGERQRVAIARA-LVNKPRLVLaDEPTG 174
Cdd:TIGR01192 426 RENIR----LGREGATDEEVYEAAKAAAAHdfILKRSNgydtlvgERGNRLSGGERQRLAIARAiLKNAPILVL-DEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 175 NLD----ARNADSIFQLlgelnVAQRTAFlVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:TIGR01192 501 ALDveteARVKNAIDAL-----RKNRTTF-IIAHRLSTVRNADLVLFLDQGRL 547
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-223 |
6.24e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.14 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 19 TVQTDV--LHNVSFSIEEGEMMAIVGTSGSGKS-TLLHLLGGLD---TPTSGDVIFSGQsmnrlsAAARADLRNRELGFI 92
Cdd:PRK10418 11 ALQAAQplVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGK------PVAPCALRGRKIATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 93 YQfhHLLPDFTALENV---AMPLLIGKQKAADiERQAKAMLHAVGLEHRsnHR-----PSELSGGERQRVAIARALVNKP 164
Cdd:PRK10418 85 MQ--NPRSAFNPLHTMhthARETCLALGKPAD-DATLTAALEAVGLENA--ARvlklyPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLE-MRDGHL 223
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAvMSHGRI 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-228 |
6.36e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.80 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 27 NVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADlrnreLGFIY-----QFHHLLPD 101
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLA-----RGLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENVA------MPLLI-GKQKAADIERQAKAMlhAVGLEHrSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTG 174
Cdd:PRK15439 356 APLAWNVCalthnrRGFWIkPARENAVLERYRRAL--NIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 175 NLD--ARNadSIFQLLGELnVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAELT 228
Cdd:PRK15439 433 GVDvsARN--DIYQLIRSI-AAQNVAVLFISSDLEEIEQMaDRVLVMHQGEISGALT 486
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-221 |
7.52e-20 |
|
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: 87.57 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYqeGTVQTdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGL--DTPTSGDVIFSGQSmnrLSAAARA 82
Cdd:TIGR02633 1 LLEMKGIVKTF--GGVKA--LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSP---LKASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 83 DLRNRELGFIYQFHHLLPDFTALENVAMPLLI----GKQKAADIERQAKAMLHAVGLEHRSNHRP-SELSGGERQRVAIA 157
Cdd:TIGR02633 74 DTERAGIVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 158 RALVNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRMNRQLE-MRDG 221
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICvIRDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-223 |
8.25e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYqeGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAaradl 84
Cdd:PRK15439 11 LLCARSISKQY--SGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RNRELGfIY---QFHHLLPDFTALENVamplLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALV 161
Cdd:PRK15439 82 KAHQLG-IYlvpQEPLLFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 162 NKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHDL----QLAKRMNrqlEMRDGHL 223
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLpeirQLADRIS---VMRDGTI 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-206 |
2.22e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.14 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYqeGTVQTdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLdTPT---SGDVIFSGQSmnrLS 77
Cdd:PRK13549 1 MMEYLLEMKNITKTF--GGVKA--LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEE---LQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 78 AAARADLRNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIE---RQAKAMLHAVGLEHRSNHRPSELSGGERQRV 154
Cdd:PRK13549 73 ASNIRDTERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDamyLRAQKLLAQLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 155 AIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDL 206
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKL 203
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-206 |
2.24e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.16 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLsaaaradLRNRELGFIYQFHHLLPDFTA 104
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-------LQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 105 L-ENVAMPLLIG------KQKAADIERQAKAMLHAVGLEHRsnHRP-SELSGGERQRVAIARALVNKPRLVLADEPTGNL 176
Cdd:PRK15056 96 LvEDVVMMGRYGhmgwlrRAKKRDRQIVTAALARVDMVEFR--HRQiGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190
....*....|....*....|....*....|
gi 2055389599 177 DARNADSIFQLLGELNVAQRTaFLVVTHDL 206
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKT-MLVSTHNL 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-207 |
2.78e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMN----RLSAAAradlrnrELGFIYQFHHLLP 100
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQEA-------GIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 101 DFTALENV----AMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNL 176
Cdd:PRK10762 93 QLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190
....*....|....*....|....*....|.
gi 2055389599 177 DARNADSIFQLLGELNvAQRTAFLVVTHDLQ 207
Cdd:PRK10762 173 TDTETESLFRVIRELK-SQGRGIVYISHRLK 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-226 |
3.36e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTvqtDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSG---------QSMNR 75
Cdd:PRK13644 1 MIRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 76 LSAAAradLRNRELGFIYQFHHLLPDFTAlENVAMPlligkqkAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVA 155
Cdd:PRK13644 78 LVGIV---FQNPETQFVGRTVEEDLAFGP-ENLCLP-------PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 156 IARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTaFLVVTHDLQLAKRMNRQLEMRDGHLDAE 226
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-218 |
4.21e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.84 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADlrnrelgfiYQFHH--LLPD 101
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH---------YLGHRnaMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENvampLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDaRNA 181
Cdd:PRK13539 88 LTVAEN----LEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAA 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 2055389599 182 DSIFQLLGELNVAQRTAFLVVTH-DLQLAKrmNRQLEM 218
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAATHiPLGLPG--ARELDL 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-218 |
7.49e-19 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 80.28 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFsgqsmnrlsaaaradLRNRELGFIYQfHHLLPDFT 103
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PEGEDLLFLPQ-RPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMPLLigkqkaadierqakamlhavglehrsnhrpSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADS 183
Cdd:cd03223 80 LREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180 190
....*....|....*....|....*....|....*
gi 2055389599 184 IFQLLGELnvaqRTAFLVVTHDLQLAKRMNRQLEM 218
Cdd:cd03223 130 LYQLLKEL----GITVISVGHRPSLWKFHDRVLDL 160
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-204 |
1.02e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.65 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 23 DVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLD--TPTSGDVIFSGQSMNRLSAAARAdlrnRE---LGFIYqfhh 97
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERA----RAgifLAFQY---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 98 llP---------DF--TALENVAMPLLigkqKAADIERQAKAMLHAVGLEHRSNHRP--SELSGGERQRVAIARALVNKP 164
Cdd:COG0396 86 --PveipgvsvsNFlrTALNARRGEEL----SAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2055389599 165 RLVLADEPTGNLDA---RN-ADSIFQLLGElnvaqRTAFLVVTH 204
Cdd:COG0396 160 KLAILDETDSGLDIdalRIvAEGVNKLRSP-----DRGILIITH 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-211 |
1.81e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLdTPTSGDVIFSGQSMNRLSAAARADLRnrelGFIYQfhHLLPDFta 104
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR----AYLSQ--QQSPPF-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 105 lenvAMP----LLIGKQKAADIERQAKAMLH---AVGLEHRSNHRPSELSGGERQRVAIARAL------VN-KPRLVLAD 170
Cdd:COG4138 83 ----AMPvfqyLALHQPAGASSEAVEQLLAQlaeALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2055389599 171 EPTGNLDARNADSIFQLLGELNVAQRTAfLVVTHDLQLAKR 211
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGITV-VMSSHDLNHTLR 198
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-204 |
1.95e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.39 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 20 VQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGG--LDTPTSGDVifsgqsmnrlsaaaraDLRNRELGfiyqfhh 97
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCV----------------DVPDNQFG------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 98 llPDFTALENVAmplligkqKAADIErQAKAMLHAVGLEHRSNHR--PSELSGGERQRVAIARALVNKPRLVLADEPTGN 175
Cdd:COG2401 98 --REASLIDAIG--------RKGDFK-DAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180
....*....|....*....|....*....
gi 2055389599 176 LDARNADSIFQLLGELNVAQRTAFLVVTH 204
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-212 |
5.87e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.90 E-value: 5.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRY-----QEG------------TVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQ 71
Cdd:COG4586 5 ENLSKTYrvyekEPGlkgalkglfrreYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 72 SMNRLsaaaRADLRnRELGFIY-QFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEH------Rsnhrps 144
Cdd:COG4586 85 VPFKR----RKEFA-RRIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGElldtpvR------ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 145 ELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDL----QLAKRM 212
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMddieALCDRV 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-227 |
6.33e-18 |
|
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: 78.72 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLD--TPTSGDVIFSGQSMNRLSAAARAdlrNRELGFIYQfhhllpd 101
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQ------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 ftalenvaMPLLIGKQKAADIERQAKamlhaVGlehrsnhrpseLSGGERQRVAIARALVNKPRLVLADEPTGNLDARNA 181
Cdd:cd03217 85 --------YPPEIPGVKNADFLRYVN-----EG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 182 DSIFQLLGELNvAQRTAFLVVTHDLQLAKRM--NRQLEMRDGHL----DAEL 227
Cdd:cd03217 141 RLVAEVINKLR-EEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIvksgDKEL 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-221 |
1.05e-17 |
|
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: 78.53 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLL-HLLGGLDTpTSGDVIFSGQSMNRLSAAArADLRNR-ELGFIYQFHHLLpDF 102
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEA-TRSRNRySVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 103 TALENVAMPLLIGKQKAADI----ERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDA 178
Cdd:cd03290 94 TVEENITFGSPFNKQRYKAVtdacSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2055389599 179 RNADSIFQ--LLGELNVAQRTAFLvVTHDLQLAKRMNRQLEMRDG 221
Cdd:cd03290 174 HLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-177 |
1.14e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARAdl 84
Cdd:PRK10895 3 TLTAKNLAKAYKGRRV----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 rNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADI-ERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNK 163
Cdd:PRK10895 77 -RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170
....*....|....
gi 2055389599 164 PRLVLADEPTGNLD 177
Cdd:PRK10895 156 PKFILLDEPFAGVD 169
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
25-211 |
2.80e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.29 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLD--TPT---SGDVIFSGQSMNrlsaAARAD---LRNReLGFIYQFH 96
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlIPGfrvEGKVTFHGKNLY----APDVDpveVRRR-IGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 97 HLLPDfTALENVAM-PLLIGKQKAAD--IERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPT 173
Cdd:PRK14243 101 NPFPK-SIYDNIAYgARINGYKGDMDelVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 2055389599 174 GNLDARNADSIFQLLGELnvAQRTAFLVVTHDLQLAKR 211
Cdd:PRK14243 180 SALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAAR 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-206 |
4.68e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.38 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 9 DNLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAAradLRNrE 88
Cdd:PRK10790 344 DNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV---LRQ-G 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 89 LGFIYQFHHLLPDfTALENVAMPLLIGKQKA---------ADIERQAKAMLHAVGLEHRSNhrpseLSGGERQRVAIARA 159
Cdd:PRK10790 417 VAMVQQDPVVLAD-TFLANVTLGRDISEEQVwqaletvqlAELARSLPDGLYTPLGEQGNN-----LSVGQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLGElnVAQRTAFLVVTHDL 206
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAA--VREHTTLVVIAHRL 535
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-205 |
8.06e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 78.82 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSgqsmnrlsaaaradlRNRELGFIYQFHHLLPDFT 103
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ---------------PGIKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVA--------------------------MPLLIGKQ----------KAADIERQAKAMLHAVGLehrsnhrP---- 143
Cdd:TIGR03719 85 VRENVEegvaeikdaldrfneisakyaepdadFDKLAAEQaelqeiidaaDAWDLDSQLEIAMDALRC-------Ppwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 144 --SELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELnvaqRTAFLVVTHD 205
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY----PGTVVAVTHD 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-222 |
9.43e-17 |
|
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: 78.80 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 22 TDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGqsmnRLSaaaradlrnrelgFIYQFHHLLPD 101
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----RIS-------------FSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 fTALENVAMPLligkqkAADiERQAKAMLHAVGLEHRSNHRPSE-----------LSGGERQRVAIARALVNKPRLVLAD 170
Cdd:TIGR01271 502 -TIKDNIIFGL------SYD-EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 171 EPTGNLDARNADSIFQ-LLGELnVAQRTAfLVVTHDLQLAKRMNRQLEMRDGH 222
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFEsCLCKL-MSNKTR-ILVTSKLEHLKKADKILLLHEGV 624
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-226 |
1.03e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.06 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSG-----DVIFSGQSMnrLSAAARADLRnRELGFIYQFHHL 98
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFR-RRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 99 LPdFTALENVamplLIGKQKAADIERQ-----AKAMLHAVGL----EHRSNHRPSELSGGERQRVAIARALVNKPRLVLA 169
Cdd:PRK14271 113 FP-MSIMDNV----LAGVRAHKLVPRKefrgvAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 170 DEPTGNLDARNADSIFQLLGELnvAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAE 226
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEE 243
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
24-210 |
1.16e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.37 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadlrnRELGFIYQFHHLLPDFT 103
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ-----KQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMPLLIGKQKAADIErqakaMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADS 183
Cdd:PRK13540 91 LRENCLYDIHFSPGAVGITE-----LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*...
gi 2055389599 184 IFQLLgELNVAQRTAFLVVTH-DLQLAK 210
Cdd:PRK13540 166 IITKI-QEHRAKGGAVLLTSHqDLPLNK 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-206 |
2.34e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 28 VSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLdTPTSGDVIFSGQSMNRLSAAARADLRnrelGFIYQ----------FHH 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQqqtppfampvFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 98 L---LPDFTALenvamplligkqkaADIERQAKAMLHAVGLEHRSnHRP-SELSGGERQRVAIARAL-----VNKP--RL 166
Cdd:PRK03695 90 LtlhQPDKTRT--------------EAVASALNEVAEALGLDDKL-GRSvNQLSGGEWQRVRLAAVVlqvwpDINPagQL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2055389599 167 VLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHDL 206
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDL 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-208 |
3.31e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEgtvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrLSAAARADL 84
Cdd:PRK13638 1 MLATSDLWFRYQD----EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnRELGFIYQFhhllPD----FTALE-NVAMPLLIGKQKAADIERQAKAMLHAVGLEHrSNHRPSE-LSGGERQRVAIAR 158
Cdd:PRK13638 76 R-QQVATVFQD----PEqqifYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQH-FRHQPIQcLSHGQKKRVAIAG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2055389599 159 ALVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHDLQL 208
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRI-VAQGNHVIISSHDIDL 198
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-223 |
4.84e-16 |
|
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: 73.99 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrLSAAARADLR 85
Cdd:cd03369 7 IEVENLSVRYAPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID---ISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NReLGFIYQfhhllpDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLehrsnhrpsELSGGERQRVAIARALVNKPR 165
Cdd:cd03369 82 SS-LTIIPQ------DPTLFSGTIRSNLDPFDEYSDEEIYGALRVSEGGL---------NLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELnvAQRTAFLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREE--FTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-178 |
8.70e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.54 E-value: 8.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLCKRYQEGTVqtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVifsgqsmnRLSAAA 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA--------RPAPGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RadlrnreLGFIYQFHHLLPDFTALENVAMPLliGKQKAA------------------D--IERQAK--AMLHAVG---L 135
Cdd:PRK11819 71 K-------VGYLPQEPQLDPEKTVRENVEEGV--AEVKAAldrfneiyaayaepdadfDalAAEQGElqEIIDAADawdL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2055389599 136 EHR------------SNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDA 178
Cdd:PRK11819 142 DSQleiamdalrcppWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-191 |
1.14e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLdTPT---SGDVIFSGQsmnrlsAAARADLRNRE-LG--FIYQFHHL 98
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGE------VCRFKDIRDSEaLGivIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 99 LPDFTALENvampLLIGKQKA-------ADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADE 171
Cdd:NF040905 90 IPYLSIAEN----IFLGNERAkrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180
....*....|....*....|
gi 2055389599 172 PTGNLDARNADSIFQLLGEL 191
Cdd:NF040905 166 PTAALNEEDSAALLDLLLEL 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-221 |
1.61e-15 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 73.74 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 22 TDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGqsmnRLSaaaradlrnrelgFIYQFHHLLPD 101
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----RIS-------------FSSQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 fTALENVAMPLligkqkAADiERQAKAMLHAVGLEHRSNHRPSE-----------LSGGERQRVAIARALVNKPRLVLAD 170
Cdd:cd03291 113 -TIKENIIFGV------SYD-EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 171 EPTGNLDARNADSIFQLLGELNVAQRTAFLvVTHDLQLAKRMNRQLEMRDG 221
Cdd:cd03291 185 SPFGYLDVFTEKEIFESCVCKLMANKTRIL-VTSKMEHLKKADKILILHEG 234
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-223 |
1.95e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.75 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 21 QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLsaaaRADLRNRELGFIYQFHHLLP 100
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL----QLDSWRSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 101 DfTALENVAMplliGKQKA--ADIERQAK-AMLH------AVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADE 171
Cdd:PRK10789 403 D-TVANNIAL----GRPDAtqQEIEHVARlASVHddilrlPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 172 PTGNLDARNADSIFQLLGELNvAQRTaFLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWG-EGRT-VIISAHRLSALTEASEILVMQHGHI 527
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-228 |
2.35e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.62 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTVQtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrLSAAARADLRNrel 89
Cdd:PRK10522 327 NVTFAYQDNGFS---VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---VTAEQPEDYRK--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 gfiyQFHHLLPDFTALENvamplLIGKQKAADIERQAKAMLHAVGLEHR---SNHRPS--ELSGGERQRVAIARALVNKP 164
Cdd:PRK10522 398 ----LFSAVFTDFHLFDQ-----LLGPEGKPANPALVEKWLERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 165 RLVLADEPtgnldARNADSIF------QLLGELNVAQRTAFlVVTHDLQLAKRMNRQLEMRDGHLdAELT 228
Cdd:PRK10522 469 DILLLDEW-----AADQDPHFrrefyqVLLPLLQEMGKTIF-AISHDDHYFIHADRLLEMRNGQL-SELT 531
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-209 |
2.87e-15 |
|
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: 72.44 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 31 SIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrlsaaaradlrnrelgfiYQFHHLLPDFtalENVAM 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------------------YKPQYIKADY---EGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 111 PLLIGKQKAADIERQAKA-MLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARN---ADSIFQ 186
Cdd:cd03237 80 DLLSSITKDFYTHPYFKTeIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKVIR 159
|
170 180
....*....|....*....|...
gi 2055389599 187 LLGELNvaQRTAFlVVTHDLQLA 209
Cdd:cd03237 160 RFAENN--EKTAF-VVEHDIIMI 179
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-191 |
4.49e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.62 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 27 NVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARadlrnRELGFIYQFHHLLPDFTALE 106
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR-----RRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 107 NVA-------MPlligkqkAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLD-- 177
Cdd:NF033858 359 NLElharlfhLP-------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpv 431
|
170
....*....|....
gi 2055389599 178 ARnaDSIFQLLGEL 191
Cdd:NF033858 432 AR--DMFWRLLIEL 443
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-223 |
6.38e-15 |
|
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: 73.29 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQegTVQTD---VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQsmnRLSAAARA 82
Cdd:COG4615 328 LELRGVTYRYP--GEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 83 DLRNRelgF--IYQFHHLLPDftalenvamplLIGKQKAADiERQAKAMLHAVGLEHR---SNHRPS--ELSGGERQRVA 155
Cdd:COG4615 403 AYRQL---FsaVFSDFHLFDR-----------LLGLDGEAD-PARARELLERLELDHKvsvEDGRFSttDLSQGQRKRLA 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 156 IARALV-NKPRLVL----ADEptgnldarnaDSIF------QLLGELNVAQRTAfLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:COG4615 468 LLVALLeDRPILVFdewaADQ----------DPEFrrvfytELLPELKARGKTV-IAISHDDRYFDLADRVLKMDYGKL 535
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-212 |
1.53e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.22 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 13 KRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSgdviFSGQSMNRLSAAARADLRnrELGFI 92
Cdd:PLN03211 76 RQIQERTI----LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILK--RTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 93 YQFHHLLPDFTALENVA------MPLLIGKQkaaDIERQAKAMLHAVGLEHRSNHRPSE-----LSGGERQRVAIARALV 161
Cdd:PLN03211 146 TQDDILYPHLTVRETLVfcsllrLPKSLTKQ---EKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEML 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 162 NKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTaflVVTHDLQLAKRM 212
Cdd:PLN03211 223 INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKT---IVTSMHQPSSRV 270
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-228 |
2.45e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 14 RYQEGTVQtdvlhNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLS-------AAARADLRN 86
Cdd:PRK09700 273 SRDRKKVR-----DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkGMAYITESR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 87 RELGFiyqfhhlLPDFTALENVAMP--LLIGKQKAA-------DIERQAKAMLHAVGLE-HRSNHRPSELSGGERQRVAI 156
Cdd:PRK09700 348 RDNGF-------FPNFSIAQNMAISrsLKDGGYKGAmglfhevDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 157 ARALVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHDL-QLAKRMNRQLEMRDGHLDAELT 228
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILT 492
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-177 |
4.06e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 1 MNKILLQCDNLckryQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLD--TPTSGDVIFSGQSMNRLSA 78
Cdd:CHL00131 3 KNKPILEIKNL----HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 79 AARADLrNRELGFIYQFHhlLP-----DFTALENVAMPLLIGKQKAADIE--RQAKAMLHAVGLEHRSNHRPSE--LSGG 149
Cdd:CHL00131 79 EERAHL-GIFLAFQYPIE--IPgvsnaDFLRLAYNSKRKFQGLPELDPLEflEIINEKLKLVGMDPSFLSRNVNegFSGG 155
|
170 180
....*....|....*....|....*...
gi 2055389599 150 ERQRVAIARALVNKPRLVLADEPTGNLD 177
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLD 183
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-197 |
7.65e-14 |
|
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: 67.65 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTP--TSGDVIFSGQsmnrlsaaARADLRNRELGFIYQFHHLLPDF 102
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGR--------PLDKNFQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 103 TALEnvamPLLIgkqkaadierqaKAMLHAVGLEHrsnhrpselsggeRQRVAIARALVNKPRLVLADEPTGNLDARNAD 182
Cdd:cd03232 95 TVRE----ALRF------------SALLRGLSVEQ-------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170
....*....|....*
gi 2055389599 183 SIFQLLGELNVAQRT 197
Cdd:cd03232 146 NIVRFLKKLADSGQA 160
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-206 |
1.35e-13 |
|
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: 67.78 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 33 EEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSG---------DVI--FSGQSMNRLSAaaraDLRNRELGFIY--QFHHLL 99
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdeFRGSELQNYFT----KLLEGDVKVIVkpQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 100 PDftALENVAMPLLigkqKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDAR 179
Cdd:cd03236 100 PK--AVKGKVGELL----KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....*..
gi 2055389599 180 NADSIFQLLGELNVAQRtAFLVVTHDL 206
Cdd:cd03236 174 QRLNAARLIRELAEDDN-YVLVVEHDL 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-177 |
2.94e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.50 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYqEGTvQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMnrLSAAARAdl 84
Cdd:TIGR01257 1937 ILRLNELTKVY-SGT-SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDV-- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 rNRELGFIYQFHHLLPDFTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:TIGR01257 2011 -HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170
....*....|...
gi 2055389599 165 RLVLADEPTGNLD 177
Cdd:TIGR01257 2090 PLVLLDEPTTGMD 2102
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-206 |
5.48e-13 |
|
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: 67.50 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 33 EEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGD---------VI--FSGQSM-NRLSaaaraDLRNRELGFIY--QFHHL 98
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdeVLkrFRGTELqDYFK-----KLANGEIKVAHkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 99 LPDftALENVAMPLLigkqKAADiERQAKAML-HAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLD 177
Cdd:COG1245 172 IPK--VFKGTVRELL----EKVD-ERGKLDELaEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|..
gi 2055389599 178 AR---NADSIFQLLGELNvaqrTAFLVVTHDL 206
Cdd:COG1245 245 IYqrlNVARLIRELAEEG----KYVLVVEHDL 272
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-178 |
7.19e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 64.98 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPT---SGDVIFSGQSMnrlsaaaradlrn 86
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 87 reLGFIYQFHHLLPdFTALENVAMPLLIGKQKaadIERQAKAmlhavglehRSNHRPSELSGGERQRVAIARALVNKPRL 166
Cdd:cd03233 75 --KEFAEKYPGEII-YVSEEDVHFPTLTVRET---LDFALRC---------KGNEFVRGISGGERKRVSIAEALVSRASV 139
|
170
....*....|..
gi 2055389599 167 VLADEPTGNLDA 178
Cdd:cd03233 140 LCWDNSTRGLDS 151
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-226 |
1.09e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaaRADLRNrelGFIY-----QFHHLL 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSP--QDGLAN---GIVYisedrKRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 100 PDFTALENVAMPLL------IGKQKAADiERQA------------KAMLHAVGLehrsnhrpseLSGGERQRVAIARALV 161
Cdd:PRK10762 343 LGMSVKENMSLTALryfsraGGSLKHAD-EQQAvsdfirlfniktPSMEQAIGL----------LSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 162 NKPRLVLADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAE 226
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSEMPEVLGMsDRILVMHEGRISGE 476
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-177 |
1.31e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrlsaAARADlRNRELGFIYQFHHLLPDFT 103
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT------ATRGD-RSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 104 ALENvaMPLLIGKQKaadieRQAKAM----LHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLD 177
Cdd:PRK13543 99 TLEN--LHFLCGLHG-----RRAKQMpgsaLAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-218 |
1.44e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGlDTPTS---------GDVIFSGQSMNRLSAAARADLRnrelGFIYQ 94
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLR----AVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 95 FHHLLPDFTALENVamplLIGKQKAA-----------DIERQAKAMLHAVGLEHRSnhrPSELSGGERQRVAIARALVN- 162
Cdd:PRK13547 91 AAQPAFAFSAREIV----LLGRYPHArragalthrdgEIAWQALALAGATALVGRD---VTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 163 --------KPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTHDLQLAKRMNRQLEM 218
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAM 227
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-208 |
2.92e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.65 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 27 NVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnRLSaaaradlrnrelgfIYQFHHLlpdfTALE 106
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV--RMA--------------VFSQHHV----DGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 107 NVAMPLL-IGKQKAADIERQAKAMLHAVGLEHRSNHRPS-ELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSI 184
Cdd:PLN03073 587 LSSNPLLyMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL 666
|
170 180
....*....|....*....|....
gi 2055389599 185 FQLLgelnVAQRTAFLVVTHDLQL 208
Cdd:PLN03073 667 IQGL----VLFQGGVLMVSHDEHL 686
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-208 |
4.29e-12 |
|
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: 64.81 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 31 SIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVifsgqsmnrlsaaaradlrNRELGFIYQFHHLLPDF-----TAL 105
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------------DEDLKISYKPQYISPDYdgtveEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 106 ENVAMPLLIGKQKAADIerqakamLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDA--R-NAD 182
Cdd:COG1245 423 RSANTDDFGSSYYKTEI-------IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqRlAVA 495
|
170 180
....*....|....*....|....*.
gi 2055389599 183 SIFQLLGElnvAQRTAFLVVTHDLQL 208
Cdd:COG1245 496 KAIRRFAE---NRGKTAMVVDHDIYL 518
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-204 |
4.37e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 18 GTVQTD---VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGlDTPT--SGDVIFSGQsmNRLSAAARADLRnRELGFI 92
Cdd:PRK10938 266 GVVSYNdrpILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTLFGR--RRGSGETIWDIK-KHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 93 YQFHHLlpDF---TALENVAMPLL---IGKQKAADIERQAKAM--LHAVGLEHRSNHRP-SELSGGERQRVAIARALVNK 163
Cdd:PRK10938 342 SSSLHL--DYrvsTSVRNVILSGFfdsIGIYQAVSDRQQKLAQqwLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKH 419
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2055389599 164 PRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVTH 204
Cdd:PRK10938 420 PTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-177 |
5.33e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGG---LDtptSGDVIFSGQ-SMNRLsaaaRADLRNRELGFIY------- 93
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLD---DGRIIYEQDlIVARL----QQDPPRNVEGTVYdfvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 94 --------QFHHLL------PDFTALENVA-MPLLIGKQKAADIERQAKAMLHAVGLEhrSNHRPSELSGGERQRVAIAR 158
Cdd:PRK11147 92 eeqaeylkRYHDIShlvetdPSEKNLNELAkLQEQLDHHNLWQLENRINEVLAQLGLD--PDAALSSLSGGWLRKAALGR 169
|
170
....*....|....*....
gi 2055389599 159 ALVNKPRLVLADEPTGNLD 177
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLD 188
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-207 |
9.18e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 3 KILLQCDNLCkrYQEGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVifsgQSMNRLSAA--- 79
Cdd:PRK11147 317 KIVFEMENVN--YQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAyfd 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 80 -ARADLRnrelgfiyqfhhllPDFTALENVAMplliGKQkaaDIERQAKAMlHAVG-----LEH--RSNHRPSELSGGER 151
Cdd:PRK11147 389 qHRAELD--------------PEKTVMDNLAE----GKQ---EVMVNGRPR-HVLGylqdfLFHpkRAMTPVKALSGGER 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 152 QRVAIARALVNKPRLVLADEPTGNLDARNadsiFQLLGELNVAQRTAFLVVTHDLQ 207
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHDRQ 498
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-206 |
9.26e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 9.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 32 IEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGD---------VI--FSGQSM-NRLSaaaraDLRNRELGFIY--QFHH 97
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdeVLkrFRGTELqNYFK-----KLYNGEIKVVHkpQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 98 LLPDftALENVAMPLLigkqKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLD 177
Cdd:PRK13409 171 LIPK--VFKGKVRELL----KKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*....
gi 2055389599 178 ARNADSIFQLLGELnvAQRTAFLVVTHDL 206
Cdd:PRK13409 245 IRQRLNVARLIREL--AEGKYVLVVEHDL 271
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-223 |
1.18e-11 |
|
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: 63.81 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLH-LLGGLDTpTSGDVIFSGQsmnrlsaaaradlrnreLGFIYQfHHLLPDFT 103
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS-----------------VAYVPQ-QAWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVamplLIGKQKAadiERQAKAMLHAVGLEHRSNHRPS-----------ELSGGERQRVAIARALVNKPRLVLADEP 172
Cdd:TIGR00957 715 LRENI----LFGKALN---EKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 173 TGNLDARNADSIFQ-LLGELNVAQRTAFLVVTHDLQLAKRMNRQLEMRDGHL 223
Cdd:TIGR00957 788 LSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-177 |
1.47e-11 |
|
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: 63.42 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 4 ILLQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFsGQSMnrlsaaarad 83
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLL----IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV---------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 84 lrnrELGFIYQFH-HLLPDFTALENVAMP---LLIGKqkaadIERQAKAMLHAVGLEHRSNHRP-SELSGGERQRVAIAR 158
Cdd:TIGR03719 386 ----KLAYVDQSRdALDPNKTVWEEISGGldiIKLGK-----REIPSRAYVGRFNFKGSDQQKKvGQLSGGERNRVHLAK 456
|
170
....*....|....*....
gi 2055389599 159 ALVNKPRLVLADEPTGNLD 177
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLD 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-227 |
1.54e-11 |
|
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: 63.31 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 27 NVSFSIEEGEMMAIVGTSGSGKSTLLH-LLGGLDTPTSGDVIFSGQSMNRLSA--AARADL------RNRelgfiyqfHH 97
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPaqAIRAGIamvpedRKR--------HG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 98 LLPDFTALENVAMPLL--IGKQKAADIERQAKAMLHAVGLEHRSNHRP----SELSGGERQRVAIARALVNKPRLVLADE 171
Cdd:TIGR02633 350 IVPILGVGKNITLSVLksFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 172 PTGNLDARNADSIFQLLGELnVAQRTAFLVVTHDL-QLAKRMNRQLEMRDGHLDAEL 227
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKGDF 485
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-214 |
6.84e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGL-DTPTSGDVIFSGQ----------------------SMNRLSAAA 80
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEhtndmtneqdyqgdeeqnvgmkNVNEFSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 81 RA----------------------------DLRNreLGFIYQFHHLLPDFTALENVAMplliGKQKAA--DIERQAK--- 127
Cdd:PTZ00265 1263 EGgsgedstvfknsgkilldgvdicdynlkDLRN--LFSIVSQEPMLFNMSIYENIKF----GKEDATreDVKRACKfaa 1336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 128 --AMLHAVGLEHRSNHRP--SELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVT 203
Cdd:PTZ00265 1337 idEFIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIA 1416
|
250
....*....|.
gi 2055389599 204 HDLQLAKRMNR 214
Cdd:PTZ00265 1417 HRIASIKRSDK 1427
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-208 |
6.87e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 32 IEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVifsgqsmnrlsaaaradlrNRELGFIYQFHHLLPDFTalENVAMP 111
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------------DPELKISYKPQYIKPDYD--GTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 112 LligkqkaadieRQAKAMLHA----------VGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDarna 181
Cdd:PRK13409 421 L-----------RSITDDLGSsyykseiikpLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD---- 485
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2055389599 182 dsifqllgelnVAQRT---------------AFLVVTHDLQL 208
Cdd:PRK13409 486 -----------VEQRLavakairriaeereaTALVVDHDIYM 516
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-213 |
1.02e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 23 DVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSgQSMN-----------RLSAAARADL------R 85
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-DSHNlkdinlkwwrsKIGVVSQDPLlfsnsiK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQFHHL--LPD------FTALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHR--------------- 142
Cdd:PTZ00265 478 NNIKYSLYSLKDLeaLSNyynedgNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQtikdsevvdvskkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 143 -------------------PSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELNVAQRTAFLVVT 203
Cdd:PTZ00265 558 ihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
250
....*....|
gi 2055389599 204 HDLQLAKRMN 213
Cdd:PTZ00265 638 HRLSTIRYAN 647
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-221 |
2.83e-10 |
|
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: 59.76 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 23 DVLHN-VSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLdTPTSGdvifsgqsmNRLSAAARAdlrnrELGFIYQfhhlLPD 101
Cdd:TIGR00954 465 DVLIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYG---------GRLTKPAKG-----KLFYVPQ----RPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 F---TALENVAMPLLIGKQKAADI-ERQAKAMLHAVGLEHRSNHRPS---------ELSGGERQRVAIARALVNKPRLVL 168
Cdd:TIGR00954 526 MtlgTLRDQIIYPDSSEDMKRRGLsDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 169 ADEPTGNLDARNADSIFQLLGELNVaqrtAFLVVTHDLQLAKRMNRQLEMrDG 221
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCREFGI----TLFSVSHRKSLWKYHEYLLYM-DG 653
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-191 |
5.02e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSaaARADLRNrELGFIYQFHHLLPDFTA 104
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKS--SKEALEN-GISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 105 LENVAMPLLIGKQKAAD---IERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNA 181
Cdd:PRK10982 91 MDNMWLGRYPTKGMFVDqdkMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170
....*....|
gi 2055389599 182 DSIFQLLGEL 191
Cdd:PRK10982 171 NHLFTIIRKL 180
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-177 |
5.11e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSG--------QSMNRLSAAA-----RADLRNRELG 90
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPAleyviDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 91 FIYQFHHLLPDftaleNVAMPLLIGKQKAAD---IERQAKAMLHAVGLEHRSNHRP-SELSGGERQRVAIARALVNKPRL 166
Cdd:PRK10636 96 AQLHDANERND-----GHAIATIHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDL 170
|
170
....*....|.
gi 2055389599 167 VLADEPTGNLD 177
Cdd:PRK10636 171 LLLDEPTNHLD 181
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-233 |
6.66e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 21 QTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAARADLRNRElgFIYQFHHLL- 99
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE--WQRNNTDMLs 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 100 --PDFTALeNVAMPLLIGKQKAADIERQAKAMlhavGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLD 177
Cdd:PRK10938 93 pgEDDTGR-TTAEIIQDEVKDPARCEQLAQQF----GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 178 ARNADSIFQLLGELNVAQRTAFLVVthdlqlakrmNRQLEMRD-----GHL-DAELTLMGAR 233
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVL----------NRFDEIPDfvqfaGVLaDCTLAETGER 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-228 |
7.09e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 28 VSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQ--SMNRLSAAARADL----RNRELGFIYQFHhllpd 101
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGImlcpEDRKAEGIIPVH----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 fTALENVAMP----------LLIGKQKAADIERQAKAMlhavGLEHRSNHRP-SELSGGERQRVAIARALVNKPRLVLAD 170
Cdd:PRK11288 347 -SVADNINISarrhhlragcLINNRWEAENADRFIRSL----NIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 171 EPTGNLD--ARNadSIFQLLGELnVAQRTAFLVVTHDlqLAKRM---NRQLEMRDGHLDAELT 228
Cdd:PRK11288 422 EPTRGIDvgAKH--EIYNVIYEL-AAQGVAVLFVSSD--LPEVLgvaDRIVVMREGRIAGELA 479
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-213 |
7.55e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaarADLRNReL 89
Cdd:TIGR00957 1289 NYCLRYREDL--DLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGL---HDLRFK-I 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQFHHL--------LPDFTAL--ENVAMPLLIGKQKAADIERQAKamlhavgLEHRSNHRPSELSGGERQRVAIARA 159
Cdd:TIGR00957 1363 TIIPQDPVLfsgslrmnLDPFSQYsdEEVWWALELAHLKTFVSALPDK-------LDHECAEGGENLSVGQRQLVCLARA 1435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 160 LVNKPRLVLADEPTGNLDARNADSIFQLLgelnvaqRTAFLVVTHdLQLAKRMN 213
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTI-------RTQFEDCTV-LTIAHRLN 1481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-227 |
9.93e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 9.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLH-LLGGLDTPTSGDVIFSGQ--SMNRLSAAARADL------RNRelgfiyq 94
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKpvKIRNPQQAIAQGIamvpedRKR------- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 95 fHHLLPDFTALENVAMPLL--IGKQKAADIERQAKAMLHAVG-LEHRSNH---RPSELSGGERQRVAIARALVNKPRLVL 168
Cdd:PRK13549 350 -DGIVPVMGVGKNITLAALdrFTGGSRIDDAAELKTILESIQrLKVKTASpelAIARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 169 ADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHDLQLAKRM-NRQLEMRDGHLDAEL 227
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLsDRVLVMHEGKLKGDL 487
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-173 |
1.02e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNrlSAAARADLRNR------ELGfiyqfHHL 98
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRiaympqGLG-----KNL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 99 LPDFTALENVA-MPLLIGkQKAADIERQAKAMLHAVGLeHRSNHRPS-ELSGGERQRVAIARALVNKPRLVLADEPT 173
Cdd:NF033858 90 YPTLSVFENLDfFGRLFG-QDAAERRRRIDELLRATGL-APFADRPAgKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-191 |
1.04e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAA-------ARADLRNRELGfIY---- 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfALVTEERRSTG-IYayld 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 94 -QFHHLLPDFTALENvAMPLLIGKQKAADIERQAKAMlhAVGLEHRSNHRPSeLSGGERQRVAIARALVNKPRLVLADEP 172
Cdd:PRK10982 343 iGFNSLISNIRNYKN-KVGLLDNSRMKSDTQWVIDSM--RVKTPGHRTQIGS-LSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170
....*....|....*....
gi 2055389599 173 TGNLDARNADSIFQLLGEL 191
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAEL 437
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
27-205 |
1.48e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 27 NVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDV-IFSGQSMNRLsaaaradlrnRELGFIYQfhhllpDFTAL 105
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGKL----------RQDQFAFE------EFTVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 106 ENVAM---PLLIGKQ-----------------KAADIERQ------------AKAMLHAVGLEHRSNHRP-SELSGGERQ 152
Cdd:PRK15064 83 DTVIMghtELWEVKQerdriyalpemseedgmKVADLEVKfaemdgytaearAGELLLGVGIPEEQHYGLmSEVAPGWKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 153 RVAIARALVNKPRLVLADEPTGNLDarnADSIFQLLGELNVAQRTaFLVVTHD 205
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD---INTIRWLEDVLNERNST-MIIISHD 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-221 |
1.76e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 6 LQCDNLCKRYQEGTVqtdvLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSgqsmnrlsaaaradlR 85
Cdd:PRK15064 320 LEVENLTKGFDNGPL----FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS---------------E 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 86 NRELGFIYQFHHllPDFTALENVaMPLLIGKQKAADIERQAKAMLhavGL----EHRSNHRPSELSGGERQRVAIARALV 161
Cdd:PRK15064 381 NANIGYYAQDHA--YDFENDLTL-FDWMSQWRQEGDDEQAVRGTL---GRllfsQDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055389599 162 NKPRLVLADEPTGNLDarnADSIFQLLGELNVAQRTaFLVVTHDLQ----LAkrmNRQLEMRDG 221
Cdd:PRK15064 455 QKPNVLVMDEPTNHMD---MESIESLNMALEKYEGT-LIFVSHDREfvssLA---TRIIEITPD 511
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
25-188 |
2.25e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.26 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMA------------IVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAAAradlrnreLGFI 92
Cdd:PRK13541 4 LHQLQFNIEQKNLFDlsitflpsaityIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--------CTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 93 YQFHHLLPDFTALENVAMplligKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEP 172
Cdd:PRK13541 76 GHNLGLKLEMTVFENLKF-----WSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
170
....*....|....*.
gi 2055389599 173 TGNLDARNADSIFQLL 188
Cdd:PRK13541 151 ETNLSKENRDLLNNLI 166
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-208 |
2.68e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSgqsmnrlsaaaradlRNRELGFI--YQFHHLLPD 101
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA---------------KGIKLGYFaqHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENVAmplligKQKAADIERQAKAMLHAVGLEHRSNHRPSE-LSGGERQRVAIARALVNKPRLVLADEPTGNLDArn 180
Cdd:PRK10636 392 ESPLQHLA------RLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL-- 463
|
170 180
....*....|....*....|....*...
gi 2055389599 181 adSIFQLLGELNVAQRTAFLVVTHDLQL 208
Cdd:PRK10636 464 --DMRQALTEALIDFEGALVVVSHDRHL 489
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-186 |
2.73e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaarADLRNReLGFIYQfhhllpdft 103
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGL---MDLRKV-LGIIPQ--------- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 alenvaMPLL-----------IGKQKAADI-ERQAKAMLHAV------GLEHRSNHRPSELSGGERQRVAIARALVNKPR 165
Cdd:PLN03130 1321 ------APVLfsgtvrfnldpFNEHNDADLwESLERAHLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180
....*....|....*....|.
gi 2055389599 166 LVLADEPTGNLDARnADSIFQ 186
Cdd:PLN03130 1395 ILVLDEATAAVDVR-TDALIQ 1414
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
10-177 |
3.32e-09 |
|
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: 55.63 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLdTPTSGDVIFSGQSMNRLSAAAradlRNREL 89
Cdd:cd03289 7 DLTAKYTEGG--NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQK----WRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQfhhllPDFTALENVAMPL-LIGKQKAADIERQAKamlhAVGLEHRSNHRPSE-----------LSGGERQRVAIA 157
Cdd:cd03289 80 GVIPQ-----KVFIFSGTFRKNLdPYGKWSDEEIWKVAE----EVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLA 150
|
170 180
....*....|....*....|
gi 2055389599 158 RALVNKPRLVLADEPTGNLD 177
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLD 170
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-219 |
3.81e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.90 E-value: 3.81e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055389599 146 LSGGERQRVAIARALVN---KPR-LVLADEPTGNLDARNADSIFQLLGELNVAQRTaFLVVTHDLQLAKRMNRQLEMR 219
Cdd:cd03227 78 LSGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLPELAELADKLIHIK 154
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-191 |
4.77e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTP---TSGDVIFSGQsmnrlsaaARADLRNRELGFIYQFHHLLP 100
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGR--------PLDSSFQRSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 101 DFT---ALENVA---MPLLIGKQKAAD----------IERQAKAMlhaVGLehrsnhrPSE-LSGGERQRVAIARALVNK 163
Cdd:TIGR00956 850 TSTvreSLRFSAylrQPKSVSKSEKMEyveeviklleMESYADAV---VGV-------PGEgLNVEQRKRLTIGVELVAK 919
|
170 180
....*....|....*....|....*....
gi 2055389599 164 PRLVL-ADEPTGNLDARNADSIFQLLGEL 191
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-218 |
5.23e-09 |
|
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: 54.57 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLlhllggldtptSGDVIFS-GQS--MNRLSAAARadlrnrelgfiyQFHHLL-- 99
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL-----------AFDTIYAeGQRryVESLSAYAR------------QFLGQMdk 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 100 PDFTALENVAmPLLIGKQKAAD-------------------------IERQAKAMLHaVGLEHRSNHRPSE-LSGGERQR 153
Cdd:cd03270 68 PDVDSIEGLS-PAIAIDQKTTSrnprstvgtvteiydylrllfarvgIRERLGFLVD-VGLGYLTLSRSAPtLSGGEAQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 154 VAIARALVNKPRLVL--ADEPTGNLDARNADSIFQLLGELNVAQRTaFLVVTHDLQLAKRMNRQLEM 218
Cdd:cd03270 146 IRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNT-VLVVEHDEDTIRAADHVIDI 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-177 |
1.40e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 27 NVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFsGQSMnrlsaaaradlrnrELGFIYQFH-HLLPDFTAL 105
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------------KLAYVDQSRdALDPNKTVW 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 106 ENVAMPL---LIGKQ-------------KAADierQAKamlhAVGlehrsnhrpsELSGGERQRVAIARALVNKPRLVLA 169
Cdd:PRK11819 407 EEISGGLdiiKVGNReipsrayvgrfnfKGGD---QQK----KVG----------VLSGGERNRLHLAKTLKQGGNVLLL 469
|
....*...
gi 2055389599 170 DEPTGNLD 177
Cdd:PRK11819 470 DEPTNDLD 477
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-221 |
1.52e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVifsgqsmnrlsaaaradLRNRELGFIYQFHHLLpDFT 103
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------------WAERSIAYVPQQAWIM-NAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVampLLIGKQKAADIER-------QAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNL 176
Cdd:PTZ00243 737 VRGNI---LFFDEEDAARLADavrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2055389599 177 DARNADSIFQ--LLGELnvAQRTAFLvVTHDLQLAKRMNRQLEMRDG 221
Cdd:PTZ00243 814 DAHVGERVVEecFLGAL--AGKTRVL-ATHQVHVVPRADYVVALGDG 857
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-177 |
1.68e-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: 54.53 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 10 NLCKRYQEGTvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTpTSGDVIFSGQSMNRLSAAAradlRNREL 89
Cdd:TIGR01271 1222 GLTAKYTEAG--RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQT----WRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 90 GFIYQFHHLLPDfTALENvamplLIGKQKAADIERQAKAmlHAVGLEHRSNHRPSE-----------LSGGERQRVAIAR 158
Cdd:TIGR01271 1295 GVIPQKVFIFSG-TFRKN-----LDPYEQWSDEEIWKVA--EEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLAR 1366
|
170
....*....|....*....
gi 2055389599 159 ALVNKPRLVLADEPTGNLD 177
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLD 1385
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-177 |
1.68e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 14 RYQEGTVQtdVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSmnrLSAAARADLRnRELGFIY 93
Cdd:PTZ00243 1317 RYREGLPL--VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE---IGAYGLRELR-RQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 94 QfHHLLPDFTALENVAmPLLigkqKAADIErqAKAMLHAVGLEHR----------------SNHrpselSGGERQRVAIA 157
Cdd:PTZ00243 1391 Q-DPVLFDGTVRQNVD-PFL----EASSAE--VWAALELVGLRERvasesegidsrvleggSNY-----SVGQRQLMCMA 1457
|
170 180
....*....|....*....|.
gi 2055389599 158 RALVNKPR-LVLADEPTGNLD 177
Cdd:PTZ00243 1458 RALLKKGSgFILMDEATANID 1478
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-228 |
1.87e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 17 EGTVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLH-LLGGLDTPTSGDVIFSGQsmnrlsaaaradlrnreLGFIYQF 95
Cdd:PLN03130 625 DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-----------------VAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 96 HHLLpDFTALENVamplLIGKQkaADIERQAKAmLHAVGLEH-----------RSNHRPSELSGGERQRVAIARALVNKP 164
Cdd:PLN03130 688 SWIF-NATVRDNI----LFGSP--FDPERYERA-IDVTALQHdldllpggdltEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055389599 165 RLVLADEPTGNLDARNADSIFQ--LLGELnvaQRTAFLVVTHDLQLAKRMNRQLEMRDGHLDAELT 228
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDkcIKDEL---RGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGT 822
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-229 |
2.67e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLH-LLGGLDTPTSGDVIFSGQS--MNRLSAAARADLRNREL---GFIYQFHHL 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVayVPQVSWIFNATVRENILfgsDFESERYWR 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 99 LPDFTALENvamplligkqkaaDIERQAKAMLHAVGlehrsnHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDA 178
Cdd:PLN03232 713 AIDVTALQH-------------DLDLLPGRDLTEIG------ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2055389599 179 RNADSIFQLLGELNVAQRTAFLvVTHDLQLAKRMNRQLEMRDGHLDAELTL 229
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVL-VTNQLHFLPLMDRIILVSEGMIKEEGTF 823
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-186 |
3.15e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 5 LLQCDNLCKRYQEGTvqTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQSMNRLSAaarADL 84
Cdd:PLN03232 1234 SIKFEDVHLRYRPGL--PPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGL---TDL 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 85 RnRELGFIYQFHHL--------LPDFTALENVAMPLLIGKQKAADIERQakamlHAVGLEHRSNHRPSELSGGERQRVAI 156
Cdd:PLN03232 1309 R-RVLSIIPQSPVLfsgtvrfnIDPFSEHNDADLWEALERAHIKDVIDR-----NPFGLDAEVSEGGENFSVGQRQLLSL 1382
|
170 180 190
....*....|....*....|....*....|
gi 2055389599 157 ARALVNKPRLVLADEPTGNLDARnADSIFQ 186
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVR-TDSLIQ 1411
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-181 |
3.81e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTP--TSGDVIFSGQSMNRLSAAaradlrnRELGFIYQFHHLLPD 101
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQETFA-------RISGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENVA------MPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRP--SELSGGERQRVAIARALVNKPRLVLADEPT 173
Cdd:PLN03140 968 VTVRESLIysaflrLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
....*...
gi 2055389599 174 GNLDARNA 181
Cdd:PLN03140 1048 SGLDARAA 1055
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-218 |
5.49e-08 |
|
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: 51.17 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLhllggLDTptsgdvifsgqsmnrLSAAARADLRNrelgfiyqfhhLLPDFta 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV-----NEG---------------LYASGKARLIS-----------FLPKF-- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 105 lenvamplliGKQKAADIErQAKAMLhAVGLEHRSNHRP-SELSGGERQRVAIARALV--NKPRLVLADEPTGNLDARNa 181
Cdd:cd03238 58 ----------SRNKLIFID-QLQFLI-DVGLGYLTLGQKlSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQD- 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 2055389599 182 dsIFQLLGELN--VAQRTAFLVVTHDLQLAKRMNRQLEM 218
Cdd:cd03238 125 --INQLLEVIKglIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-72 |
6.44e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 6.44e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQS 72
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA 87
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-181 |
7.11e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 19 TVQTDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLG----GLDTPTSGDVIFSGQSMNRLSAAARADLrnrelgfIY- 93
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDV-------VYn 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 94 -----QFHHLLPDFTaLENVAM-------PLLIGKQKAAdiERQAKAMLHAVGLEHRSNHRPSE-----LSGGERQRVAI 156
Cdd:TIGR00956 144 aetdvHFPHLTVGET-LDFAARcktpqnrPDGVSREEYA--KHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSI 220
|
170 180
....*....|....*....|....*
gi 2055389599 157 ARALVNKPRLVLADEPTGNLDARNA 181
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSATA 245
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-211 |
2.10e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFSGQ-SMNRLSAAARADLrnrelgfiyqfhhllpdfT 103
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQL------------------T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMPLLIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADS 183
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180
....*....|....*....|....*...
gi 2055389599 184 IFQLLGELNVAQRTAFLvVTHDLQLAKR 211
Cdd:PRK13546 182 CLDKIYEFKEQNKTIFF-VSHNLGQVRQ 208
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-213 |
8.44e-07 |
|
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: 47.37 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 35 GEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVIFsgQSMNRLSAAARADLRNrelgfiyqfhhllpdftalenvamplli 114
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLL---------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 115 gkqkaadierqakamlhavgleHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQL-----LG 189
Cdd:smart00382 52 ----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180
....*....|....*....|....
gi 2055389599 190 ELNVAQRTAFLVVTHDLQLAKRMN 213
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-209 |
1.07e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.18 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 32 IEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDVifsgqSMNRLSAAARadlrnrelgfiyqfhhllpdftalenvamP 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-----EWDGITPVYK-----------------------------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 112 LLIgkqkaadierqakamlhavglehrsnhrpsELSGGERQRVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGEL 191
Cdd:cd03222 68 QYI------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170
....*....|....*...
gi 2055389599 192 NVAQRTAFLVVTHDLQLA 209
Cdd:cd03222 118 SEEGKKTALVVEHDLAVL 135
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-204 |
1.22e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 22 TDVLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLD--TPTSGDVIFSGQSMNRLSAAARAdlrNRELGFIYQFHHLL 99
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 100 PDF-------TALENVAMpllIGKQKAAD-------IERQAKAMLHAVGLEHRSNHrpSELSGGERQRVAIARALVNKPR 165
Cdd:PRK09580 91 PGVsnqfflqTALNAVRS---YRGQEPLDrfdfqdlMEEKIALLKMPEDLLTRSVN--VGFSGGEKKRNDILQMAVLEPE 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 2055389599 166 LVLADEPTGNLDARNADSIFQLLGELNVAQRtAFLVVTH 204
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTH 203
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-210 |
1.26e-06 |
|
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: 47.99 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLH----------LLGGLDTPTSGDVIFSGQSMNRLSAAARA------------ 82
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypalarrLHLKKEQPGNHDRIEGLEHIDKVIVIDQSpigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 83 ------DLR------------NRELGFIyQFHHllpdftalENVAMPLLIGKQKAAD-------IERQAKAmLHAVGLEH 137
Cdd:cd03271 91 ytgvfdEIRelfcevckgkryNRETLEV-RYKG--------KSIADVLDMTVEEALEffenipkIARKLQT-LCDVGLGY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055389599 138 RSNHRPS-ELSGGERQRVAIARALVNKPR---LVLADEPTGNLdarNADSIFQLLGELN--VAQRTAFLVVTHDLQLAK 210
Cdd:cd03271 161 IKLGQPAtTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL---HFHDVKKLLEVLQrlVDKGNTVVVIEHNLDVIK 236
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
28-204 |
2.10e-06 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 46.69 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 28 VSFSIEEGeMMAIVGTSGSGKST----LLHLLG-----GLDTPTSGDVIFSGQS----MNRLSAAARADLRNRELGFIYQ 94
Cdd:cd03278 16 TTIPFPPG-LTAIVGPNGSGKSNiidaIRWVLGeqsakSLRGEKMSDVIFAGSEtrkpANFAEVTLTFDNSDGRYSIISQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 95 fhhllpdftalenvamplligkqkaADIERqakaMLHAVGlehRSNHRPSELSGGERQRVAIAR--AL--VNKPRLVLAD 170
Cdd:cd03278 95 -------------------------GDVSE----IIEAPG---KKVQRLSLLSGGEKALTALALlfAIfrVRPSPFCVLD 142
|
170 180 190
....*....|....*....|....*....|....
gi 2055389599 171 EPTGNLDARNADSIFQLLGELnvAQRTAFLVVTH 204
Cdd:cd03278 143 EVDAALDDANVERFARLLKEF--SKETQFIVITH 174
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-233 |
2.15e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 102 FTALENVAMpllIGKQ---KAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADEPTGNLDA 178
Cdd:NF000106 101 FSGRENLYM---IGR*ldlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055389599 179 RNADSIFQLLGELnVAQRTAFLVVTHDLQLAKRMNRQLE-------MRDGHLDAELTLMGAR 233
Cdd:NF000106 178 RTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTvidrgrvIADGKVDELKTKVGGR 238
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-213 |
2.21e-06 |
|
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: 46.83 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 39 AIVGTSGSGKSTLLH-LLGGL--DTPTSGDVIFSGQSMNRlSAAARADLrnrELGFIYQF---HHLLPDFTALENVAM-- 110
Cdd:cd03240 26 LIVGQNGAGKTTIIEaLKYALtgELPPNSKGGAHDPKLIR-EGEVRAQV---KLAFENANgkkYTITRSLAILENVIFch 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 111 ------PLLigkqkaadierqakamlhavglEHRSNhrpseLSGGERQ------RVAIARAL-VNKPRLVLaDEPTGNLD 177
Cdd:cd03240 102 qgesnwPLL----------------------DMRGR-----CSGGEKVlasliiRLALAETFgSNCGILAL-DEPTTNLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2055389599 178 ARNAD----SIFQLLGELNVAQrtaFLVVTHDLQLAKRMN 213
Cdd:cd03240 154 EENIEeslaEIIEERKSQKNFQ---LIVITHDEELVDAAD 190
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
39-206 |
1.57e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 39 AIVGTSGSGKSTLLH----LLGGldtPTSGDVIFSGQSMNRLSAAARADLR----------NRELGFIYQFHHLLPD--F 102
Cdd:COG0419 27 LIVGPNGAGKSTILEairyALYG---KARSRSKLRSDLINVGSEEASVELEfehggkryriERRQGEFAEFLEAKPSerK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 103 TALENV--AMPLLIGKQKAADIERQAKAMLHAVG-LEHRSNHR---------PSELSGGERQRVAIARALvnkpRLVLaD 170
Cdd:COG0419 104 EALKRLlgLEIYEELKERLKELEEALESALEELAeLQKLKQEIlaqlsgldpIETLSGGERLRLALADLL----SLIL-D 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 2055389599 171 epTGNLDARNADSIFQLLGELNvaqrtaflVVTHDL 206
Cdd:COG0419 179 --FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-218 |
1.90e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 130 LHAVGLEHRSNHRP-SELSGGERQRVAIARALVN---KPRLVLADEPTGNLDARNADSIFQLLGELnVAQRTAFLVVTHD 205
Cdd:PRK00635 793 LCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSL-THQGHTVVIIEHN 871
|
90
....*....|...
gi 2055389599 206 LQLAKRMNRQLEM 218
Cdd:PRK00635 872 MHVVKVADYVLEL 884
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
69-177 |
1.94e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 69 SGQSMNRLSAAARADLRNRELGFIYQFHHLLPDFTAlENVAMPLLIGKQKAADIERQAKamlhavglehrsnhrpSELSG 148
Cdd:PLN03073 285 TGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTA-EARAASILAGLSFTPEMQVKAT----------------KTFSG 347
|
90 100
....*....|....*....|....*....
gi 2055389599 149 GERQRVAIARALVNKPRLVLADEPTGNLD 177
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
24-210 |
5.06e-05 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 43.12 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 24 VLHNVSFSIEEGEMMAIVGTSGSGKSTLLHLLGGLDTPTSGDviFSGQSMNRLSAAARAdlrnrelgfiyqfhHLLPDFT 103
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGD--FIGLRGDALPLGANS--------------FILPGLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 104 ALENVAMpllIGKQKAADIERQAKAMLHAVGLEHRSNHRPSELSGGERQRVAIARALVNKPRLVLADeptGNLdaRNADS 183
Cdd:PRK15177 66 GEENARM---MASLYGLDGDEFSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIAD---GKL--YTGDN 137
|
170 180 190
....*....|....*....|....*....|
gi 2055389599 184 IFQLLGELNVA---QRTAFLVVTHDLQLAK 210
Cdd:PRK15177 138 ATQLRMQAALAcqlQQKGLIVLTHNPRLIK 167
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
25-210 |
3.01e-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: 41.54 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLH----------LLGGLDTPTSGDVIFSGQSMNRL-----SAAARADLRN--- 86
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypalanrLNGAKTVPGRYTSIEGLEHLDKVihidqSPIGRTPRSNpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 87 --------REL--------------------------------GFIYQFHHLLPDF--------------TALE------ 106
Cdd:TIGR00630 704 ytgvfdeiRELfaetpeakvrgytpgrfsfnvkggrceacqgdGVIKIEMHFLPDVyvpcevckgkrynrETLEvkykgk 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 107 NVAMPLLIGKQKAAD-------IERQAKAMLhAVGLEHRSNHRPS-ELSGGERQRVAIARALVNK---PRLVLADEPTGN 175
Cdd:TIGR00630 784 NIADVLDMTVEEAYEffeavpsISRKLQTLC-DVGLGYIRLGQPAtTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTG 862
|
250 260 270
....*....|....*....|....*....|....*..
gi 2055389599 176 LdarNADSIFQLLGELN--VAQRTAFLVVTHDLQLAK 210
Cdd:TIGR00630 863 L---HFDDIKKLLEVLQrlVDKGNTVVVIEHNLDVIK 896
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
129-188 |
6.44e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.60 E-value: 6.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055389599 129 MLHAVGLEHRSNHRPSELSGGERQR---VAIARALV----------NKPRLVLADEPTGNLDARNADSIFQLL 188
Cdd:pfam13558 16 VRDEDGSEVETYRRSGGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
26-52 |
1.89e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 1.89e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
25-53 |
2.54e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.52 E-value: 2.54e-03
10 20
....*....|....*....|....*....
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLH 53
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
28-217 |
3.90e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 37.25 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 28 VSFS-IEEGEMMAIVGTSGSGKSTLLH-----LLGglDTPTSGDVIFSGQSMNRLSAAARADLRNRELGFIYQFH---HL 98
Cdd:cd03279 20 IDFTgLDNNGLFLICGPTGAGKSTILDaityaLYG--KTPRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKYRVErsrGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 99 lpDFTALENVAMplLIGKQKAADIERQAKAmlhavglehrsnhrpseLSGGERQRVAIARAL--------VNKPRL--VL 168
Cdd:cd03279 98 --DYDQFTRIVL--LPQGEFDRFLARPVST-----------------LSGGETFLASLSLALalsevlqnRGGARLeaLF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2055389599 169 ADEPTGNLDARNADSIFQLLGELNVAQRtAFLVVTHDLQLAKRMNRQLE 217
Cdd:cd03279 157 IDEGFGTLDPEALEAVATALELIRTENR-MVGVISHVEELKERIPQRLE 204
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-208 |
4.73e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055389599 128 AMLHAVGLEHRSNHRP-SELSGGERQRVAIARALVNKPRLV--LADEPTGNLDARNADSIFQLLGELNvAQRTAFLVVTH 204
Cdd:PRK00635 458 SILIDLGLPYLTPERAlATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLR-DQGNTVLLVEH 536
|
....
gi 2055389599 205 DLQL 208
Cdd:PRK00635 537 DEQM 540
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
25-53 |
8.98e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 36.93 E-value: 8.98e-03
10 20
....*....|....*....|....*....
gi 2055389599 25 LHNVSFSIEEGEMMAIVGTSGSGKSTLLH 53
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
153-214 |
9.13e-03 |
|
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: 36.95 E-value: 9.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055389599 153 RVAIARALVNKPRLVLADEPTGNLDARNADSIFQLLGELnVAQRT-----AFLVVTHDLQLAKRMNR 214
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEI-IKSRSqqrnfQLLVITHDEDFVELLGR 1278
|
|
| |
