|
Name |
Accession |
Description |
Interval |
E-value |
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-233 |
1.03e-168 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 463.90 E-value: 1.03e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAE 233
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAE 233
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-225 |
2.37e-147 |
|
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: 409.43 E-value: 2.37e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-226 |
1.35e-133 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 374.77 E-value: 1.35e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 3 KILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVN 162
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 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 |
5.66e-126 |
|
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: 355.26 E-value: 5.66e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELR 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-226 |
5.24e-102 |
|
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: 295.11 E-value: 5.24e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPL-LIGKKKPAEinsRALEMLKAVGLEHRANHRPSELSGGERQRVAIARA 159
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLeLAGRRDARA---RARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-224 |
3.66e-95 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 277.32 E-value: 3.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELR 85
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:COG2884 79 -RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMpKRVLELEDGRLV 216
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-222 |
7.30e-77 |
|
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: 230.60 E-value: 7.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAhRVIILDDGR 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-223 |
1.14e-75 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 228.79 E-value: 1.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQFHHLLPDFTALENV------AMPL---LIGKKKPAEINsRALEMLKAVGLEHRANHRPSELSGGERQRVA 155
Cdd:COG3638 79 R-RRIGMIFQQFNLVPRLSVLTNVlagrlgRTSTwrsLLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR-MSRQLEMRDGRL 223
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-227 |
2.66e-74 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 225.74 E-value: 2.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaa 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 kaelrnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:COG1116 80 ------PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ----LAKR---MSRqlemRDGRLTAEL 227
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeavfLADRvvvLSA----RPGRIVEEI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-223 |
5.05e-73 |
|
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: 230.56 E-value: 5.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVQT-DVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 84 LRnQKLGFIYQ--FHHLLPDFTALENVAMPLLI-GKKKPAEINSRALEMLKAVGL-EHRANHRPSELSGGERQRVAIARA 159
Cdd:COG1123 340 LR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIAdRVAVMYDGRI 483
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-223 |
6.47e-73 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 224.96 E-value: 6.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRN-- 86
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALS---ERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 87 QKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRIcDRVAVLENGRI 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-227 |
1.91e-72 |
|
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: 219.65 E-value: 1.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelr 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:cd03293 75 ---RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ---LEMRDGRLTAEL 227
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRvvvLSARPGRIVAEV 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-226 |
7.56e-72 |
|
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: 218.60 E-value: 7.56e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRN-- 86
Cdd:cd03258 5 KNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLS---GKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 87 QKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEE 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
1.69e-71 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 221.90 E-value: 1.69e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaa 80
Cdd:COG3842 1 MAMPALELENVSKRY--GDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 kAELRNqkLGFIYQ----FHHLlpdfTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAI 156
Cdd:COG3842 74 -PEKRN--VGMVFQdyalFPHL----TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 157 ARALVNNPRLVLADEPTGNLDARNADsifQLLGELNRLQ---GTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLRE---EMREELRRLQrelGITFIYVTHDQEEALALADRIAvMNDGRI 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-226 |
1.17e-70 |
|
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: 216.00 E-value: 1.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF--GDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELRnQKLGFIYQFHHLLPDFTALENVAMPLLI-GKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARA 159
Cdd:COG1127 77 LYELR-RRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM-RDGRLTAE 226
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVlADGKIIAE 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-223 |
2.05e-67 |
|
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: 206.88 E-value: 2.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKL 89
Cdd:cd03292 5 NVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 170 DEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-222 |
1.40e-66 |
|
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: 205.49 E-value: 1.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELR 85
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDFTALENVAMPLL---------IGKKKPAEINsRALEMLKAVGLEHRANHRPSELSGGERQRVAI 156
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVLSGRLgrrstwrslFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR-MSRQLEMRDGR 222
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGR 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-223 |
2.02e-66 |
|
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: 204.66 E-value: 2.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RNqKLGFIYQ--FHHLLPDFTALENVAMPLLI--GKKKPAEINSRALEMLKAVGL-EHRANHRPSELSGGERQRVAIARA 159
Cdd:cd03257 81 RK-EIQMVFQdpMSSLNPRMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIAdRVAVMYAGKI 224
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
10-223 |
8.13e-66 |
|
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: 202.94 E-value: 8.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQkL 89
Cdd:TIGR02982 6 NLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLRRR-I 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 GFIYQFHHLLPDFTALENVAMPL-LIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
Cdd:TIGR02982 85 GYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:TIGR02982 165 ADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-226 |
8.22e-66 |
|
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: 203.33 E-value: 8.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELR 85
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFhhllPD---F--TALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:COG1122 75 -RKVGLVFQN----PDdqlFapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELAdRVIVLDDGRIVAD 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-226 |
2.84e-65 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 201.93 E-value: 2.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-223 |
5.76e-65 |
|
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: 200.44 E-value: 5.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAELRNqk 88
Cdd:cd03259 4 KGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP----PERRN-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALAdRIAVMNEGRI 209
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
24-218 |
9.36e-65 |
|
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: 199.76 E-value: 9.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFT 103
Cdd:TIGR03608 13 ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENET 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
Cdd:TIGR03608 93 VEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDE 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1600897103 184 IFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLEM 218
Cdd:TIGR03608 173 VLDLLLELND-EGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-222 |
1.97e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 199.84 E-value: 1.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSkLSSAAKAEL 84
Cdd:COG1126 1 MIEIENLHKSF--GDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKP-AEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSkAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 164 PRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAK-EGMTMVVVTHEMGFAREVAdRVVFMDGGR 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-229 |
3.90e-64 |
|
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: 199.64 E-value: 3.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssAAKAEL 84
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR---RRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQ-----FHhllPDFTALENVAMPLLIGKKkpAEINSRALEMLKAVGLEHRANHR-PSELSGGERQRVAIAR 158
Cdd:COG1124 78 R-RRVQMVFQdpyasLH---PRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELSL 229
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCdRVAVMQNGRIVEELTV 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-225 |
9.13e-64 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 209.19 E-value: 9.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-226 |
5.78e-63 |
|
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: 196.18 E-value: 5.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVqtdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELR 85
Cdd:cd03261 1 IELRGLTKSFGGRTV----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NqKLGFIYQFHHLLPDFTALENVAMPLLI-GKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:cd03261 77 R-RMGMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM-RDGRLTAE 226
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVlYDGKIVAE 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
1.82e-62 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 198.76 E-value: 1.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLqcDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
Cdd:COG3839 1 MASLEL--ENVSKSY--GGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 kaelRNqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:COG3839 75 ----RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 161 VNNPRLVLADEPTGNLDA--RNadsifQLLGELNRLQ---GTAFLVVTHDlqlakrmsrQLE----------MRDGRL 223
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAklRV-----EMRAEIKRLHrrlGTTTIYVTHD---------QVEamtladriavMNDGRI 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-223 |
6.53e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 196.95 E-value: 6.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKL 89
Cdd:PRK11153 6 NISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR-RQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
Cdd:PRK11153 165 DEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAvIDAGRL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-213 |
1.11e-61 |
|
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: 195.66 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQ--EGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTP---TSGDVIFNGQPMSKLSSA 79
Cdd:COG0444 1 LLEVRNLKVYFPtrRGVVK--AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 80 AKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLI-GKKKPAEINSRALEMLKAVGL---EHRANHRPSELSGGERQR 153
Cdd:COG0444 79 ELRKIRGREIQMIFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS 213
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIA 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-226 |
6.51e-61 |
|
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: 191.41 E-value: 6.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAel 84
Cdd:COG1120 1 MLEAENLSVGYG----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 rnQKLGFIYQFHHLLPDFTALENVAM---PLL--IGKKKPAEINsRALEMLKAVGLEHRANHRPSELSGGERQRVAIARA 159
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYAdRLVLLKDGRIVAQ 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-222 |
6.01e-60 |
|
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: 187.67 E-value: 6.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 7 QCDNLCKRYQEGsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRn 86
Cdd:cd03225 1 ELKNLSFSYPDG--ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLK---ELR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 87 QKLGFIYQFhhllPD--F---TALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALV 161
Cdd:cd03225 75 RKVGLVFQN----PDdqFfgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELAdRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-223 |
1.34e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 186.56 E-value: 1.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELR 85
Cdd:COG4619 1 LELEGLSFRVG----GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP---EWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDfTALENVAMPLLIGKKKPAEinSRALEMLKAVGLEHRANHRP-SELSGGERQRVAIARALVNNP 164
Cdd:COG4619 74 -RQVAYVPQEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVAdRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-229 |
4.38e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 186.42 E-value: 4.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelr 85
Cdd:COG1131 1 IEVRGLTKRY--GDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAELSL 229
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVaIIDKGRIVADGTP 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-223 |
1.50e-58 |
|
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: 184.27 E-value: 1.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAELR 85
Cdd:cd03262 1 IEIKNLHKSF--GDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKP-AEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSkAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVAdRVIFMDDGRI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-223 |
4.77e-58 |
|
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: 183.59 E-value: 4.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnqK 88
Cdd:cd03300 4 ENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 169 ADEPTGNLDARNADSIfQLlgELNRLQ---GTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:cd03300 154 LDEPLGALDLKLRKDM-QL--ELKRLQkelGITFVFVTHDQEEALTMSdRIAVMNKGKI 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-211 |
9.49e-58 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 182.98 E-value: 9.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssaa 80
Cdd:COG1121 2 MMMPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 kAELRNQKLGFIYQFHHLLPDF--TALENVAMPLL----IGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRV 154
Cdd:COG1121 70 -PRRARRRIGYVPQRAEVDWDFpiTVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKR 211
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVRE 204
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-223 |
5.30e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 184.58 E-value: 5.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP-MSKLSSaakael 84
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RNQKLGFIYQfHHLL-PDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
Cdd:COG1118 73 RERRVGFVFQ-HYALfPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 164 PRLVLADEPTGNLDARNADSIFQLLGEL-NRLQGTAfLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTT-VFVTHDQEEALELAdRVVVMNQGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-226 |
2.12e-56 |
|
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: 187.03 E-value: 2.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVqtDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT---SGDVIFNGQPMSKLSSAak 81
Cdd:COG1123 4 LLEVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 82 aeLRNQKLGFIYQ--FHHLLPdFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARA 159
Cdd:COG1123 80 --LRGRRIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIAdRVVVMDDGRIVED 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-224 |
2.50e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 179.52 E-value: 2.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSKLSSAAKAELRNQKL 89
Cdd:PRK09493 6 NVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 GFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 169 ADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVaSRLIFIDKGRIA 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-223 |
3.16e-56 |
|
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: 179.42 E-value: 3.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVqtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQFHHLLPDFTALENVAMPLL---------IGKKKPAEInSRALEMLKAVGLEHRANHRPSELSGGERQRVA 155
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGRLgykptwrslLGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYAdRIVGLKAGEI 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-223 |
2.06e-55 |
|
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: 176.29 E-value: 2.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELR 85
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL----PPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:cd03301 73 D--IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 166 LVLADEPTGNLDARNAdsiFQLLGELNRLQ---GTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:cd03301 151 VFLMDEPLSNLDAKLR---VQMRAELKRLQqrlGTTTIYVTHDQVEAMTMAdRIAVMNDGQI 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-222 |
3.45e-55 |
|
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: 174.30 E-value: 3.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELR 85
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqKLGFIYQFHHLLPDFTALENVAMPlligkkkpaeinsralemlkavglehranhrpseLSGGERQRVAIARALVNNPR 165
Cdd:cd03229 77 --RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-227 |
1.56e-53 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 171.60 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQkLGFIYQFHHLLPDFTA 104
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1600897103 185 FQLLGELNRLqGTAFLVVTHDLQL-AKRMSRQLEMRDGRLTAEL 227
Cdd:PRK10908 177 LRLFEEFNRV-GVTVLMATHDIGLiSRRSYRMLTLSDGHLHGGV 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-223 |
2.14e-53 |
|
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: 172.83 E-value: 2.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 21 QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLP 100
Cdd:cd03294 36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 DFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
Cdd:cd03294 116 HRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1600897103 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
Cdd:cd03294 196 RREMQDELLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRL 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-229 |
4.39e-53 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 171.97 E-value: 4.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAElR 85
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----AD-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqklGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL---EMRDGRLTAELSL 229
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLvvmSPGPGRIVERLEL 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-223 |
6.46e-52 |
|
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: 167.90 E-value: 6.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSvqtdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELR 85
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL----PPEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:cd03299 72 D--ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAiMLNGKL 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-222 |
9.50e-52 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 171.67 E-value: 9.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaa 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDG----KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 kAELRNqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:PRK09452 83 -AENRH--VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADsifQLLGELNRLQ---GTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRK---QMQNELKALQrklGITFVFVTHDQEEALTMSdRIVVMRDGR 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-208 |
2.37e-51 |
|
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: 165.78 E-value: 2.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 7 QCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssaakAELRN 86
Cdd:cd03235 1 EVEDLTVSYG----GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP---------LEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 87 QKLGFIYQFHHLLPDF--TALENVAMPLLiGKKKPAEINSR-----ALEMLKAVGLEHRANHRPSELSGGERQRVAIARA 159
Cdd:cd03235 68 KRIGYVPQRRSIDRDFpiSVRDVVLMGLY-GHKGLFRRLSKadkakVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1600897103 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQL 208
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGL 194
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-226 |
5.45e-51 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 166.79 E-value: 5.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 4 ILLQCDNLCKRYQEGSV------QTdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLS 77
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLsgkhqhQT-VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 78 -SAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPL--LIGKKKpAEINSRALEMLKAVGL-EHRANHRPSELSGGERQR 153
Cdd:PRK10419 81 rAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLrhLLSLDK-AERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFcQRVMVMDNGQIVET 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-208 |
1.24e-50 |
|
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: 165.21 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 4 ILLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAe 83
Cdd:COG0411 3 PLLEVRGLTKRF--GGLV--AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 84 lrnqKLGFI--YQFHHLLPDFTALENVAMPLLIGKKKP---------------AEINSRALEMLKAVGLEHRANHRPSEL 146
Cdd:COG0411 78 ----RLGIArtFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 147 SGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDL 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-213 |
2.42e-50 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 166.83 E-value: 2.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRY---------QEGSVQTdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ 71
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrTVGVVKA--VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 72 PMSKLSSAAKAELRnQKLGFIYQ--FHHLLPDFTALENVAMPLLI-GKKKPAEINSRALEMLKAVGL--EHrANHRPSEL 146
Cdd:COG4608 81 DITGLSGRELRPLR-RRMQMVFQdpYASLNPRMTVGDIIAEPLRIhGLASKAERRERVAELLELVGLrpEH-ADRYPHEF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 147 SGGERQRVAIARALVNNPRLVLADEPTGNLDArnadSI-FQLLGELNRLQ---GTAFLVVTHDLQLAKRMS 213
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDV----SIqAQVLNLLEDLQdelGLTYLFISHDLSVVRHIS 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-226 |
4.34e-50 |
|
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: 161.45 E-value: 4.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 7 QCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrn 86
Cdd:cd03214 1 EVENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 87 QKLGFIYQfhhllpdftalenvamplligkkkpaeinsraleMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
Cdd:cd03214 73 RKIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYAdRVILLKDGRIVAQ 179
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-173 |
5.39e-50 |
|
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: 160.12 E-value: 5.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAELRNQKLGFIYQFHHLLPDFTA 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 105 LENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHR----PSELSGGERQRVAIARALVNNPRLVLADEPT 173
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-223 |
1.96e-49 |
|
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: 169.09 E-value: 1.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKS----TLLHLLGGLDTPTSGDVIFNGQPMSKL 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 77 SSAAKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKK-KPAEINSRALEMLKAVGL---EHRANHRPSELSGGE 150
Cdd:COG4172 82 SERELRRIRGNRIAMIFQepMTSLNPLHTIGKQIAEVLRLHRGlSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 151 RQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFAdRVAVMRQGEI 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-222 |
8.69e-49 |
|
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: 157.93 E-value: 8.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELR 85
Cdd:cd03228 1 IEFKNVSFSYPGRPKP--VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQkLGFIYQFHHLLPDfTALENVamplligkkkpaeinsralemlkavglehranhrpseLSGGERQRVAIARALVNNPR 165
Cdd:cd03228 76 KN-IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGR 222
Cdd:cd03228 117 ILILDEATSALDPETEALILEAL--RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-226 |
8.76e-49 |
|
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: 160.74 E-value: 8.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSV-----QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLS-S 78
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLfgakqRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 79 AAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLL-IGKKKPAEINSRALEMLKAVGL--EHrANHRPSELSGGERQRVA 155
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrsED-ADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCqRVAVMDKGQIVEE 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-226 |
1.28e-48 |
|
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: 159.52 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelr 85
Cdd:cd03219 1 LEVRGLTKRF--GGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqKLGFIYQFHH--LLPDFTALENVAMPLLIGKKKP----------AEINSRALEMLKAVGLEHRANHRPSELSGGERQR 153
Cdd:cd03219 74 --RLGIGRTFQIprLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLAdRVTVLDQGRVIAE 224
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-223 |
1.89e-48 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 162.51 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaelR 85
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:TIGR03265 77 D--YGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 166 LVLADEPTGNLDARNADSifqLLGELNRLQ---GTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:TIGR03265 155 LLLLDEPLSALDARVREH---LRTEIRQLQrrlGVTTIMVTHDQEEALSMAdRIVVMNHGVI 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-223 |
2.26e-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: 160.31 E-value: 2.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGS-VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQ 87
Cdd:TIGR04521 4 KNVSYIYQPGTpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 88 KLGFIYQF--HHLLPDfTALENVAM-PLLIGKKKpAEINSRALEMLKAVGL-EHRANHRPSELSGGERQRVAIARALVNN 163
Cdd:TIGR04521 83 KVGLVFQFpeHQLFEE-TVYKDIAFgPKNLGLSE-EEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAME 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRL 223
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMeDVAEYADRVIVMHKGKI 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-223 |
9.05e-48 |
|
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: 157.46 E-value: 9.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGSVqtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRnQK 88
Cdd:cd03295 4 ENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV---ELR-RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLE--HRANHRPSELSGGERQRVAIARALVNNPRL 166
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLaDRIAIMKNGEI 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
10-223 |
1.29e-47 |
|
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: 157.12 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYqeGSVQTdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaeLRNQKL 89
Cdd:cd03296 7 NVSKRF--GDFVA--LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKP----AEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRMsrqLEMRDGRL 223
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDqeeaLEVADRV---VVMNKGRI 215
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
5-223 |
2.10e-47 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 159.86 E-value: 2.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSvqtdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAEL 84
Cdd:NF040840 1 MIRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLP----PEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RNqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:NF040840 72 RG--IAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRMSRqleMRDGRL 223
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNfeeaLSLADRVGI---MLNGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-223 |
3.82e-47 |
|
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: 153.71 E-value: 3.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelr 85
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDFTALENVamplligkkkpaeinsralemlkavglehranhrpsELSGGERQRVAIARALVNNPR 165
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCdRVAILNNGRI 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-225 |
6.12e-47 |
|
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: 163.01 E-value: 6.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLR 85
Cdd:COG4987 334 LELEDVSFRYPGA--GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDfTALENvampLLIGKKKPAEinSRALEMLKAVGLEHRANHRP-----------SELSGGERQRV 154
Cdd:COG4987 409 -RRIAVVPQRPHLFDT-TLREN----LRLARPDATD--EELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-226 |
1.08e-46 |
|
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: 164.24 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELR 85
Cdd:COG2274 474 IELENVSFRYPGDS--PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQkLGFIYQFHHLLPDfTALENVAMplliGKKKPAEinSRALEMLKAVGLEHRANHRP-----------SELSGGERQRV 154
Cdd:COG2274 549 RQ-IGVVLQDVFLFSG-TIRENITL----GDPDATD--EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-227 |
4.33e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 159.41 E-value: 4.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 2 NKILLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSkLSSAAK 81
Cdd:COG1129 1 AEPLLEMRGISKSF--GGVK--ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 82 AelrnQKLG--FIYQFHHLLPDFTALENVAMPLLIGKK---KPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAI 156
Cdd:COG1129 76 A----QAAGiaIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL----QLAKRMSrqlEMRDGRLTAEL 227
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLdevfEIADRVT---VLRDGRLVGTG 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-226 |
6.10e-46 |
|
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: 160.31 E-value: 6.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVqtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLR 85
Cdd:COG4988 337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQkLGFIYQFHHLLPDfTALENvampLLIGKKK--PAEIN-----SRALEMLKAV--GLEHRANHRPSELSGGERQRVAI 156
Cdd:COG4988 411 RQ-IAWVPQNPYLFAG-TIREN----LRLGRPDasDEELEaaleaAGLDEFVAALpdGLDTPLGEGGRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-223 |
1.10e-45 |
|
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: 154.57 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 40 IVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAELRNqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKP 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP----PHLRH--INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 120 AEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAF 199
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*
gi 1600897103 200 LVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:TIGR01187 155 VFVTHDQEEAMTMSdRIAIMRKGKI 179
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-205 |
1.51e-45 |
|
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: 150.71 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:COG4133 2 MLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 rnqklGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEInsRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:COG4133 78 -----AYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHD 205
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQ 190
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-226 |
1.03e-44 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 150.27 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:COG4559 1 MLEAENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnqklGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALV--- 161
Cdd:COG4559 77 R----AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 162 ----NNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYAdRILLLHQGRLVAQ 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-222 |
1.19e-44 |
|
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: 156.38 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 3 KILLQCDNLCKRY--QEGSVQTDVLH-----NVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSK 75
Cdd:COG4172 273 PPLLEARDLKVWFpiKRGLFRRTVGHvkavdGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 76 LSSAAKAELRnQKLGFIYQ--FHHLLPDFTALENVAMPLLI--GKKKPAEINSRALEMLKAVGLEHRANHR-PSELSGGE 150
Cdd:COG4172 352 LSRRALRPLR-RRMQVVFQdpFGSLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQ 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 151 RQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAhRVMVMKDGK 503
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-222 |
1.61e-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: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNkILLQCDNLCKR---YQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN--GQP--M 73
Cdd:COG4778 1 MT-TLLEVENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWvdL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 74 SKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGL-EHRANHRPSELSGGERQ 152
Cdd:COG4778 80 AQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVAdRVVDVTPFS 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-226 |
2.42e-44 |
|
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: 149.50 E-value: 2.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSKLSSAAKAELR 85
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFhhllPD--FTA----------LENVAMPlligkkkPAEINSRALEMLKAVGLEHRANHRPSELSGGERQR 153
Cdd:TIGR04520 77 -KKVGMVFQN----PDnqFVGatveddvafgLENLGVP-------REEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ---LAKRMsrqLEMRDGRLTAE 226
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeavLADRV---IVMNKGKIVAE 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-226 |
2.56e-44 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 149.15 E-value: 2.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 4 ILLQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
Cdd:PRK13548 1 AMLEARNLSVRLG----GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 84 LRnqklGFIYQFHHLLPDFTALENVAM---PLLIGKKKPAEINSRALEmlkAVGLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:PRK13548 77 RR----AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAALA---QVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 161 V------NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYAdRIVLLHQGRLVAD 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-223 |
8.56e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 147.47 E-value: 8.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS---KLSSAAKA 82
Cdd:COG4161 3 IQLKNINCFY--GSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 83 ELRnQKLGFIYQFHHLLPDFTALEN-VAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALV 161
Cdd:COG4161 79 LLR-QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVaSQVVYMEKGRI 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-229 |
1.35e-43 |
|
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: 146.93 E-value: 1.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKael 84
Cdd:COG4555 1 MIEVENLSKKY--GKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 rnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:COG4555 74 --RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELSL 229
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCdRVVILHKGKVVAQGSL 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-209 |
1.56e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 149.85 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 22 TDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPD 101
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDRKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 FTALENVAMPL--LIGKKKP--AEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:PRK10851 89 MTVFDNIAFGLtvLPRRERPnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1600897103 178 ArnadsifQLLGELNR--------LQGTAfLVVTHDLQLA 209
Cdd:PRK10851 169 A-------QVRKELRRwlrqlheeLKFTS-VFVTHDQEEA 200
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-223 |
1.69e-43 |
|
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: 145.52 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 27 NVSFSVgEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMskLSSAAKAEL--RNQKLGFIYQFHHLLPDFTA 104
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL--FDSRKKINLppQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENVAMPLliGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
Cdd:cd03297 93 RENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1600897103 185 FQLLGEL-NRLQGTAfLVVTHDLQLAKRM-SRQLEMRDGRL 223
Cdd:cd03297 171 LPELKQIkKNLNIPV-IFVTHDLSEAEYLaDRIVVMEDGRL 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-222 |
2.11e-43 |
|
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: 143.54 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGSVqtdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkL 89
Cdd:cd00267 4 NLSFRYGGRTA----LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE---ELRRR-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 GFIYQfhhllpdftalenvamplligkkkpaeinsralemlkavglehranhrpseLSGGERQRVAIARALVNNPRLVLA 169
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 170 DEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
24-223 |
3.46e-43 |
|
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: 145.40 E-value: 3.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSKLSSAAkAELRnQKLGFIYQFHHL 98
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV-LELR-RRVGMVFQKPNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 99 LPdFTALENVAMPL-LIGKKKPAEINSRALEMLKAVGLEHRANHR--PSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
Cdd:cd03260 93 FP-GSIYDNVAYGLrLHGIKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1600897103 176 LDARNADSIFQLLGELNRlqGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
Cdd:cd03260 172 LDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAfLLNGRL 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-216 |
3.37e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.97 E-value: 3.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQegsvqtDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelr 85
Cdd:COG3840 2 LRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:COG3840 72 --PVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRV 200
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-228 |
3.78e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 143.66 E-value: 3.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVqtdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssAAKAELR 85
Cdd:PRK11247 13 LLLNAVSKRYGERTV----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA----EAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqklgFIYQFHHLLPDFTALENVAMPLLiGKKKPAeinsrALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:PRK11247 85 -----LMFQDARLLPWKKVIDNVGLGLK-GQWRDA-----ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMAdRVLLIEEGKIGLDLT 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-226 |
1.95e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 148.39 E-value: 1.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQk 88
Cdd:COG1132 343 ENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQ- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQFHHLLPDfTALENVAMplliGKKK--PAEINsRALEMLKAV--------GLEHRANHRPSELSGGERQRVAIAR 158
Cdd:COG1132 416 IGVVPQDTFLFSG-TIRENIRY----GRPDatDEEVE-EAAKAAQAHefiealpdGYDTVVGERGVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-216 |
2.26e-41 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 141.38 E-value: 2.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAEL 84
Cdd:PRK11248 1 MLQISHLYADYG----GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 rnqklGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATEL 199
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-221 |
4.60e-41 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 141.13 E-value: 4.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGS-----VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSA 79
Cdd:COG4167 4 LLEVRNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 80 akaeLRNQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKK-KPAEINSRALEMLKAVGL--EHrANHRPSELSGGERQRV 154
Cdd:COG4167 84 ----YRCKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNTDlTAEEREERIFATLRLVGLlpEH-ANFYPHMLSSGQKQRV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDG 221
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKvLVMHQG 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-226 |
1.17e-40 |
|
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: 138.72 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELr 85
Cdd:cd03224 1 LEVENLNAGY--GKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqKLGFIYQFHHLLPDFTALENVAMPLLIGKK-KPAEINSRALEMLKAvgLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:cd03224 76 --GIGYVPEGRRIFPELTVEENLLLGAYARRRaKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIAdRAYVLERGRVVLE 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-226 |
2.85e-40 |
|
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: 137.81 E-value: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:COG0410 3 MLEVENLHAGY--GGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnqkLGFIYQFHHLLPDFTALENVAMPLLI--GKKKPAEINSRALEMLKAvgLEHRANHRPSELSGGERQRVAIARALVN 162
Cdd:COG0410 79 G---IGYVPEGRRIFPSLTVEENLLLGAYArrDRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIAdRAYVLERGRIVLE 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-213 |
3.45e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 141.51 E-value: 3.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYqEGSVQTDvlhNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAel 84
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 rnqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:PRK11607 93 ----INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1600897103 165 RLVLADEPTGNLDARNADSI-FQLLGELNRLqGTAFLVVTHDLQLAKRMS 213
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMqLEVVDILERV-GVTCVMVTHDQEEAMTMA 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-222 |
3.63e-40 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 138.52 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGsvqtDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELRNQKL-----GFIYQfhH----LLPDFTALENVAMPLL-IGKKKPAEINSRALEMLKAVGLE-HRANHRPSELSGG 149
Cdd:PRK11701 78 LSEAERRRLlrtewGFVHQ--HprdgLRMQVSAGGNIGERLMaVGARHYGDIRATAGDWLERVEIDaARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 150 ERQRVAIARALVNNPRLVLADEPTGNLD----ARNADsifqLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLD----LLRGLVRELGLAVVIVTHDLAVARLLAhRLLVMKQGR 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-206 |
4.13e-40 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 140.10 E-value: 4.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRY--------QEGSVQTdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP 72
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrglfkPERLVKA--LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 73 MSKLSSAAKAELRnQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKK-KPAEINSRALEMLKAVGL--EHrANHRPSELS 147
Cdd:PRK11308 79 LLKADPEAQKLLR-QKIQIVFQnpYGSLNPRKKVGQILEEPLLINTSlSAAERREKALAMMAKVGLrpEH-YDRYPHMFS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-221 |
7.62e-40 |
|
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: 135.85 E-value: 7.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQK 88
Cdd:cd03226 3 ENISFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGfiYQFhhllpdFTalENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
Cdd:cd03226 80 VD--YQL------FT--DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 169 ADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKVcDRVLLLANG 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
10-223 |
2.50e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 136.03 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEgsvQTdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV------IFNGQPMSKLSSAAKAe 83
Cdd:PRK11264 8 NLVKKFHG---QT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQKGLIRQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 84 LRnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKP-AEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVN 162
Cdd:PRK11264 83 LR-QHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPkEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 163 NPRLVLADEPTGNLDArnadsifQLLGE-LNRLQGTA-----FLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:PRK11264 162 RPEVILFDEPTSALDP-------ELVGEvLNTIRQLAqekrtMVIVTHEMSFARDVAdRAIFMDQGRI 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-226 |
2.71e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 136.75 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKAEL 84
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQFhhllPD---F--TALENVAM-PLLIGKKKpAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIAR 158
Cdd:PRK13639 77 R-KTVGIVFQN----PDdqlFapTVEEDVAFgPLNLGLSK-EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAE 226
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYvMSDGKIIKE 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-226 |
1.70e-38 |
|
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: 131.01 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELR 85
Cdd:cd03216 1 LELRGITKRF--GGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR---DAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQKLGFIYQfhhllpdftalenvamplligkkkpaeinsralemlkavglehranhrpseLSGGERQRVAIARALVNNPR 165
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIAdRVTVLRDGRVVGT 163
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-223 |
4.13e-38 |
|
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: 131.86 E-value: 4.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYqeGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelr 85
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDFTALENVA-MPLLIGKKKpAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRfYARLKGLPK-SEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCdRIAIMSDGKL 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-225 |
4.25e-38 |
|
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: 132.90 E-value: 4.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV--IFnGQPMSKLSSAaka 82
Cdd:COG1119 3 LLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLF-GERRGGEDVW--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 83 ELRnQKLGFIYQFHHLlpDFTALENVAMPLLIGK-------KKP-AEINSRALEMLKAVGLEHRANHRPSELSGGERQRV 154
Cdd:COG1119 75 ELR-KRIGLVSPALQL--RFPRDETVLDVVLSGFfdsiglyREPtDEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDGRLTA 225
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVA 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-226 |
1.35e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 132.45 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGSVQTdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmskLSSAA 80
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYA--LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELRnQKLGFIYQFhhllPD--FT----------ALENVAMPLLigkkkpaEINSRALEMLKAVGLEHRANHRPSELSG 148
Cdd:PRK13635 76 VWDVR-RQVGMVFQN----PDnqFVgatvqddvafGLENIGVPRE-------EMVERVDQALRQVGMEDFLNREPHRLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 149 GERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-223 |
1.85e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.90 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM---SKLSSAAKA 82
Cdd:PRK11124 3 IQLNGINCFY--GAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 83 ELRnQKLGFIYQFHHLLPDFTALEN-VAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALV 161
Cdd:PRK11124 79 ELR-RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 162 NNPRLVLADEPTGNLDARNADSIFQLLGElnrLQGTAF--LVVTHDLQLAKRM-SRQLEMRDGRL 223
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRE---LAETGItqVIVTHEVEVARKTaSRVVYMENGHI 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-220 |
6.96e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 128.37 E-value: 6.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGG-LDTP--TSGDVIFNGQPMSKLssaaKAELRNqkLGFIYQFHHLLPD 101
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTAL----PAEQRR--IGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 FTALENVAMPLligkkkPAEIN-----SRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
Cdd:COG4136 91 LSVGENLAFAL------PPTIGraqrrARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1600897103 177 DARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-212 |
1.07e-36 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 131.89 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQcdNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaa 80
Cdd:PRK11650 1 MAGLKLQ--AVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 kaELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:PRK11650 72 --EPADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 161 VNNPRLVLADEPTGNLDA--RNadsifQLLGELNRLQ---GTAFLVVTHD----LQLAKRM 212
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAklRV-----QMRLEIQRLHrrlKTTSLYVTHDqveaMTLADRV 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-226 |
1.66e-36 |
|
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: 127.87 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAELR 85
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP----REVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCdRVAIIDHGRIIAE 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-225 |
2.21e-36 |
|
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: 130.99 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 27 NVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMskLSSAAK----AELRNqkLGFIYQFHHLLPDF 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGiflpPHRRR--IGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 103 TALENvampLLIGKKKPAEINSRA-----LEMLkavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:COG4148 93 SVRGN----LLYGRKRAPRAERRIsfdevVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 178 -ARNAdsifQLLGELNRLQGTA---FLVVTHDL----QLAKRMsrqLEMRDGRLTA 225
Cdd:COG4148 166 lARKA----EILPYLERLRDELdipILYVSHSLdevaRLADHV---VLLEQGRVVA 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-223 |
3.82e-36 |
|
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: 125.41 E-value: 3.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmskLSSAAKAELR 85
Cdd:cd03246 1 LEVENVSFRYPGA--EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAD---ISQWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDfTALENVamplligkkkpaeinsralemlkavglehranhrpseLSGGERQRVAIARALVNNPR 165
Cdd:cd03246 76 -DHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-205 |
5.44e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 130.15 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqkL 89
Cdd:PRK11000 8 NVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG------V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSR---ALEMLKavgLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRvnqVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1600897103 167 VLADEPTGNLDA--RnadsiFQLLGELNRLQ---GTAFLVVTHD 205
Cdd:PRK11000 155 FLLDEPLSNLDAalR-----VQMRIEISRLHkrlGRTMIYVTHD 193
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-218 |
5.60e-36 |
|
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: 132.80 E-value: 5.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 22 TDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHLLPD 101
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS---WRDQ-IAWVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 fTALENVAMplliGKK--KPAEInSRAL------EMLKAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
Cdd:TIGR02857 411 -TIAENIRL----ARPdaSDAEI-REALeragldEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1600897103 172 PTGNLDarnADSIFQLLGELNRL-QGTAFLVVTHDLQLAKRMSRQLEM 218
Cdd:TIGR02857 485 PTAHLD---AETEAEVLEALRALaQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-226 |
8.72e-36 |
|
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: 125.68 E-value: 8.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 29 SFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqkLGFIYQFHHLLPDFTALENV 108
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 109 AMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLL 188
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1600897103 189 GELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQ 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-206 |
1.21e-35 |
|
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: 125.38 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGsvqtDVLHNVSFSVGEGeMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaAKAELR 85
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNrlQGTAFLVVTHDL 206
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHIV 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-204 |
1.41e-35 |
|
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: 131.85 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDT--PTSGDVIFN-------------- 69
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 70 --GQPMSK--------------LSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAV 133
Cdd:TIGR03269 77 kvGEPCPVcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 134 GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.52e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.77 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILlQCDNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssAA 80
Cdd:PRK13647 1 MDNII-EVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA---EN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELRNqKLGFIYQFhhllPD-----FTALENVAM-PLLIGKKkPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRV 154
Cdd:PRK13647 74 EKWVRS-KVGLVFQD----PDdqvfsSTVWDDVAFgPVNMGLD-KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLTAE 226
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQvIVLKEGRVLAE 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-222 |
1.70e-35 |
|
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: 125.09 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaakaELR 85
Cdd:cd03269 1 LEVENVTKRF--GRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--------IAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQKLGFIYQFHHLLPDFTALEN-VAMPLLIGKKKpAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQlVYLAQLKGLKK-EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRM-SRQLEMRDGR 222
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELcDRVLLLNKGR 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-228 |
2.41e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.92 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAA 80
Cdd:COG3845 1 MMPPALELRGITKRF--GGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAelRNQKLGFIYQfhH--LLPDFTALENVAM---PLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVA 155
Cdd:COG3845 76 DA--IALGIGMVHQ--HfmLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIAdRVTVLRRGKVVGTVD 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-225 |
4.49e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.49 E-value: 4.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 2 NKILLQCDNLCKRYQEGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaK 81
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 82 AELRNqKLGFIYQFhhllPD--F---TALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAI 156
Cdd:PRK13632 79 KEIRK-KIGIIFQN----PDnqFigaTVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLV-VTHDLQLAKRMSRQLEMRDGRLTA 225
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDL-RKTRKKTLIsITHDMDEAILADKVIVFSEGKLIA 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-226 |
6.16e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.99 E-value: 6.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaakAELR 85
Cdd:COG4152 2 LELKGLTKRF--GDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NqKLGF------IYqfhhllPDFTALEN-VAMPLLIGKKKpAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIAR 158
Cdd:COG4152 71 R-RIGYlpeergLY------PKMKVGEQlVYLARLKGLSK-AEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLEM-RDGRLTAE 226
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIiNKGRKVLS 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-218 |
7.68e-35 |
|
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: 123.73 E-value: 7.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqklgfIYQFHHLLPDFTA 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENVAMPLLIGKKKPAEINSRAL--EMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRAIveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1600897103 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVM 187
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-193 |
1.01e-34 |
|
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: 123.54 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 11 LCKRYQEGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTP---TSGDVIFNGQPMSKlssaakaELRNQ 87
Cdd:cd03234 11 LKAKNWNKYAR--ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP-------DQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 88 KLGFIYQFHHLLPDFTALENV--AMPLLIGKKKPAEINSR--ALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
Cdd:cd03234 82 CVAYVRQDDILLPGLTVRETLtyTAILRLPRKSSDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190
....*....|....*....|....*....|
gi 1600897103 164 PRLVLADEPTGNLDARNADSIFQLLGELNR 193
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLAR 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-206 |
1.20e-34 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 124.49 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQFHHLLPDFT 103
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLIGKKKPAEI-NSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
Cdd:PRK11831 101 VFDNVAYPLREHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180
....*....|....*....|....
gi 1600897103 183 SIFQLLGELNRLQGTAFLVVTHDL 206
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHDV 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-205 |
1.37e-34 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 123.29 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 2 NKILLQCDNLckRYQEGSvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaak 81
Cdd:PRK10247 4 NSPLLQLQNV--GYLAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 82 aELRNQKLGFIYQFHHLLPDfTALENVAMPLLIGKKKPAEinSRALEMLKAVGL-EHRANHRPSELSGGERQRVAIARAL 160
Cdd:PRK10247 77 -EIYRQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDP--AIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD 205
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-225 |
1.43e-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: 122.70 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 21 QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRnQKLGFIYQFHHLlp 100
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQDVTL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 dF--TALENVAMplligkKKPAEINSRALEMLKAVGLEHRANHRP-----------SELSGGERQRVAIARALVNNPRLV 167
Cdd:cd03245 90 -FygTLRDNITL------GAPLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 168 LADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPSLLDLVDRIIVMDSGRIVA 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-226 |
1.70e-34 |
|
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: 123.10 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNqKLGFIYQFHHLLPDfT 103
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRS-MIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLIGKKKPAEINSRALEMLKAV-----GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
Cdd:cd03254 93 IMENIRLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1600897103 179 RNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:cd03254 173 ETEKLIQEALEKL--MKGRTSIIIAHRLSTIKNADKILVLDDGKIIEE 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-224 |
2.26e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 128.26 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 8 CDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaelRNQ 87
Cdd:COG0488 1 LENLSKSFGG----RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 88 KLGFIYQFHHLLPDFTALENVAM---PLLIGKKKPAEIN-----------------------------SRALEMLKAVGL 135
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLDgdaELRALEAELEELEaklaepdedlerlaelqeefealggweaeARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 136 EHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTaFLVVTHD---L-QLAK 210
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWLEEFLKNYPGT-VLVVSHDryfLdRVAT 217
|
250
....*....|....
gi 1600897103 211 RMsrqLEMRDGRLT 224
Cdd:COG0488 218 RI---LELDRGKLT 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-226 |
2.40e-34 |
|
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: 125.61 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 28 VSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklSSAAKAEL--RNQKLGFIYQFHHLLPDFTAL 105
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLppEKRRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 106 ENvampLLIGKKK--PAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
Cdd:TIGR02142 94 GN----LRYGMKRarPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1600897103 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLAdRVVVLEDGRVAAA 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-226 |
3.82e-34 |
|
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: 121.56 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVqtdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelr 85
Cdd:cd03268 1 LKTNDLTKTYGKKRV----LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQKLGFIYQFHHLLPDFTALENV-AMPLLIGKKKpaeinSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLrLLARLLGIRK-----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAE 226
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLsEIQKVADRIGIINKGKLIEE 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-222 |
4.52e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 123.23 E-value: 4.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGS-VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAEL 84
Cdd:PRK13637 3 IKIENLTHIYMEGTpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQF-HHLLPDFTALENVAM-PLLIGKKKpAEINSRALEMLKAVGL--EHRANHRPSELSGGERQRVAIARAL 160
Cdd:PRK13637 82 R-KKVGLVFQYpEYQLFEETIEKDIAFgPINLGLSE-EEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDGR 222
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGK 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-213 |
5.27e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.38 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS------ 74
Cdd:PRK10619 1 MSENKLNVIDLHKRYGE----HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 75 -KLSSAAKAELR--NQKLGFIYQFHHLLPDFTALENV-AMPLLIGKKKPAEINSRALEMLKAVGLEHRANHR-PSELSGG 149
Cdd:PRK10619 77 gQLKVADKNQLRllRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 150 ERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS 213
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVS 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-230 |
1.04e-33 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 126.18 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKAelRNQKLGFIYQFHHLLPDFTA 104
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAA--LAAGVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENV---AMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
Cdd:PRK11288 97 AENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1600897103 182 DSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEM-RDGRLTAELSLM 230
Cdd:PRK11288 177 EQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVfKDGRYVATFDDM 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-223 |
1.18e-33 |
|
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: 121.05 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 23 DVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNQkLGFIYQ----FHHL 98
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGH---DLALADPAWLRRQ-VGVVLQenvlFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 99 LPDFTALENVAMPL--LIGKKKPAEINSRALEMlkAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
Cdd:cd03252 92 IRDNIALADPGMSMerVIEAAKLAGAHDFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1600897103 177 DARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:cd03252 170 DYESEHAIMRNMHDI--CAGRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-223 |
1.73e-33 |
|
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: 119.07 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 23 DVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQKLGFI---YQFHHLL 99
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP---RDAIRAGIAYVpedRKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 100 PDFTALENVAMPLLigkkkpaeinsralemlkavglehranhrpseLSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
Cdd:cd03215 91 LDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1600897103 180 NADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:cd03215 139 AKAEIYRLIREL-ADAGKAVLLISSELDELLGLCdRILVMYEGRI 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-192 |
2.10e-33 |
|
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: 120.34 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELr 85
Cdd:cd03218 1 LRAENLSKRYGK----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:cd03218 76 --GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180
....*....|....*....|....*..
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELN 192
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILK 180
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-223 |
2.40e-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: 125.69 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQegSVQTDVLH---NVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN-GQP---MSKLS 77
Cdd:TIGR03269 279 IIKVRNVSKRYI--SVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 78 SAAKAELRnQKLGFIYQFHHLLPDFTALENVAMPllIGKKKPAEINSR-ALEMLKAVGLEHRA-----NHRPSELSGGER 151
Cdd:TIGR03269 357 PDGRGRAK-RYIGILHQEYDLYPHRTVLDNLTEA--IGLELPDELARMkAVITLKMVGFDEEKaeeilDKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 152 QRVAIARALVNNPRLVLADEPTGNLD--ARN--ADSIFQLLGELNRlqgtAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDpiTKVdvTHSILKAREEMEQ----TFIIVSHDMDFVLDVcDRAALMRDGKI 506
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-223 |
3.36e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 121.73 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGS-VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN------------------- 69
Cdd:PRK13651 7 NIVKIFNKKLpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkekekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 70 ---GQPMSKLSSAAKaELRNQkLGFIYQF-HHLLPDFTALENVAM-PLLIGKKKpAEINSRALEMLKAVGL-EHRANHRP 143
Cdd:PRK13651 87 lviQKTRFKKIKKIK-EIRRR-VGVVFQFaEYQLFEQTIEKDIIFgPVSMGVSK-EEAKKRAAKYIELVGLdESYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 144 SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLA-KRMSRQLEMRDGR 222
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVlEWTKRTIFFKDGK 242
|
.
gi 1600897103 223 L 223
Cdd:PRK13651 243 I 243
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-223 |
3.94e-33 |
|
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: 119.94 E-value: 3.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVQTDVlhnvSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIF---NGQP--MSKLSSA 79
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDV----SFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAEleLYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 80 AKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLL-IGKKKPAEINSRALEMLKAVGLEH-RANHRPSELSGGERQRVA 155
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQnpRDGLRMRVSAGANIGERLMaIGARHYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAqRLLVMQQGRV 227
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-230 |
4.19e-33 |
|
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: 119.40 E-value: 4.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 26 HNVSFSVGEGEMMAIVGSSGSGKST----LLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaeLRNQKLGFIYQ--FHHLL 99
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQnpRTAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 100 PDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRA---NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
Cdd:TIGR02770 77 PLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 177 DARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAELSLM 230
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAvMDDGRIVERGTVK 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-205 |
6.32e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 121.75 E-value: 6.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGSVqtdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaa 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTV----IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 kaeLRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:PRK11432 75 ---IQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD 205
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD 196
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-223 |
8.02e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 122.45 E-value: 8.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 27 NVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALE 106
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 107 NVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190
....*....|....*....|....*....|....*...
gi 1600897103 187 LLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAiMQNGEV 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-222 |
9.51e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 124.05 E-value: 9.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKS-TLLHLLGGLDTP----TSGDVIFNGQPMSK 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 76 LSSAAKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLI--GKKKPAEiNSRALEMLKAVGLEH---RANHRPSELSG 148
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQepMVSLNPLHTLEKQLYEVLSLhrGMRREAA-RGEILNCLDRVGIRQaakRLTDYPHQLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 149 GERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGR 222
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAvMQNGR 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-204 |
9.88e-33 |
|
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: 117.27 E-value: 9.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 18 GSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTP--TSGDVIFNGQPMSKLSSAAkaelrnqKLGFIYQF 95
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRK-------IIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 96 HHLLPDFTALENvamplligkkkpaeinsralemlkavgLEHRANHRpsELSGGERQRVAIARALVNNPRLVLADEPTGN 175
Cdd:cd03213 91 DILHPTLTVRET---------------------------LMFAAKLR--GLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180
....*....|....*....|....*....
gi 1600897103 176 LDARNADSIFQLLGELnRLQGTAFLVVTH 204
Cdd:cd03213 142 LDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-211 |
1.70e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 119.35 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 14 RYQEGS-VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSG------DVIFNGQPMSKLSSaakaeLRn 86
Cdd:PRK13634 11 RYQYKTpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigeRVITAGKKNKKLKP-----LR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 87 QKLGFIYQF-HHLLPDFTALENVAM-PLLIGKKKpAEINSRALEMLKAVGLEHRANHR-PSELSGGERQRVAIARALVNN 163
Cdd:PRK13634 85 KKVGIVFQFpEHQLFEETVEKDICFgPMNFGVSE-EDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1600897103 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR 211
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-226 |
1.77e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 118.58 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelr 85
Cdd:PRK11231 3 LRTENLTVGYGT----KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nQKLGFIYQfHHLLP-DFTALENVAM---PLL-----IGKKKPAEINsRALEmlkAVGLEHRANHRPSELSGGERQRVAI 156
Cdd:PRK11231 76 -RRLALLPQ-HHLTPeGITVRELVAYgrsPWLslwgrLSAEDNARVN-QAME---QTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAE 226
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVvLANGHVMAQ 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-226 |
2.36e-32 |
|
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: 117.08 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKael 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 rnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:cd03266 78 --RRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLcDRVVVLHRGRVVYE 217
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
28-218 |
3.27e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 119.43 E-value: 3.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 28 VSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQkLGFIYQ--FHHLLPDFTAL 105
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQdpLASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 106 ENVAMPLLI--GKKKPAEINSRALEMLKAVGL-EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
Cdd:PRK15079 119 EIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 1600897103 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEM 218
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISdRVLVM 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-218 |
5.04e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.41 E-value: 5.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 23 DVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsklssAAKAELRnqkLGFIYQfHHLLPD- 101
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGAR---VAYVPQ-RSEVPDs 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 --FTALENVAMPLL--IGKKKPAEINSRAL--EMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
Cdd:NF040873 70 lpLTVRDLVAMGRWarRGLWRRLTRDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1600897103 176 LDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLEM 218
Cdd:NF040873 150 LDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-226 |
5.18e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.88 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 2 NKILLQCDNLCKRYQEG--SVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSA 79
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 80 AkaELRNqKLGFIYQFhhllPDFTAL-----ENVAM-PLLIGKKkPAEINSRALEMLKAVGLEHRANHRPSELSGGERQR 153
Cdd:PRK13633 81 W--DIRN-KAGMVFQN----PDNQIVativeEDVAFgPENLGIP-PEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-223 |
5.71e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 117.42 E-value: 5.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 3 KILLQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQPMSKLSSA 79
Cdd:PRK09984 2 QTIIRVEKLAKTFN----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 80 AKaELRNQK--LGFIYQFHHLLPDFTALENVamplLIGK--KKP----------AEINSRALEMLKAVGLEHRANHRPSE 145
Cdd:PRK09984 78 AR-DIRKSRanTGYIFQQFNLVNRLSVLENV----LIGAlgSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVST 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-228 |
1.26e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.51 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 3 KILLQCDNLCKRyqegsvqtDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKA 82
Cdd:COG1129 254 EVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 83 elrnQKLGFIY-----QFHHLLPDFTALENVAMPLL--IGKK---KPAEINSRALEMLKAVGLEHRANHRP-SELSGGER 151
Cdd:COG1129 325 ----IRAGIAYvpedrKGEGLVLDLSIRENITLASLdrLSRGgllDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 152 QRVAIARALVNNPRLVLADEPTGNLD--ARNAdsIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDvgAKAE--IYRLIRELAA-EGKAVIVISSELPELLGLSdRILVMREGRIVGELD 477
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-216 |
4.57e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 119.42 E-value: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKST----LLHLLggldtPTSGDVIFNGQPMSKLSSAAKAELRNQkLGFIYQ--FHH 97
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 98 LLPDFTALENVAMPLLIGKKK--PAEINSRALEMLKAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTG 174
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPTlsAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1600897103 175 NLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQV 496
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-226 |
5.05e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.06 E-value: 5.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGD----KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KaelrnQKLGFIYQFHHLLPDFTALENVampLLIGKK---KPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIA 157
Cdd:PRK13537 79 R-----QRVGVVPQFDNLDPDFTVRENL---LVFGRYfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRD-GRLTAE 226
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEeGRKIAE 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-226 |
5.22e-31 |
|
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: 113.77 E-value: 5.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELr 85
Cdd:TIGR03410 1 LEVSNLNVYYG----QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAvgLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:TIGR03410 76 --GIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELAdRYYVMERGRVVAS 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-223 |
8.81e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.77 E-value: 8.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 2 NKILLQCDNLCKRYQEGsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAk 81
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQ--PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 82 aeLRNQkLGFIYQFHHLLPDfTALENvampLLIGKkkPAEINSRALEMLKAVGLEHRANH------------RPseLSGG 149
Cdd:PRK11160 412 --LRQA-ISVVSQRVHLFSA-TLRDN----LLLAA--PNASDEALIEVLQQVGLEKLLEDdkglnawlgeggRQ--LSGG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 150 ERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-226 |
9.94e-31 |
|
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: 111.64 E-value: 9.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELR 85
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL----EKALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQkLGFIYQFHHLLpDFTALENVAMPLligkkkpaeinsralemlkavglehranhrpselSGGERQRVAIARALVNNPR 165
Cdd:cd03247 75 SL-ISVLNQRPYLF-DTTLRNNLGRRF----------------------------------SGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEV--LKDKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-226 |
1.54e-30 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 113.54 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHHLLPDFT 103
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVA------MPLLIG-KKKPAEINSRALemlKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
Cdd:PRK10253 98 VQELVArgryphQPLFTRwRKEDEEAVTKAM---QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 177 DARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAE 226
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLiALREGKIVAQ 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-206 |
1.79e-30 |
|
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: 117.85 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmskLSSAAKAELRnQKLGFIYQFHHLLpDFT 103
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP---VSSLDQDEVR-RRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENvampLLIGKKKPAEinSRALEMLKAVGLEHRANHRP-----------SELSGGERQRVAIARALVNNPRLVLADEP 172
Cdd:TIGR02868 425 VREN----LRLARPDATD--EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....
gi 1600897103 173 TGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDL 206
Cdd:TIGR02868 499 TEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-172 |
2.82e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.04 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelr 85
Cdd:COG1137 4 LEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqKLGFIYqfhhlLP-------DFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIAR 158
Cdd:COG1137 77 --RLGIGY-----LPqeasifrKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170
....*....|....
gi 1600897103 159 ALVNNPRLVLADEP 172
Cdd:COG1137 150 ALATNPKFILLDEP 163
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
3.88e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.54 E-value: 3.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGSVQTdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmskLSSAA 80
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA---ITDDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELR-----------NQKLGFIYQFhhllpDFT-ALENVAMPLligkkkpAEINSRALEMLKAVGLEHRANHRPSELSG 148
Cdd:PRK13648 78 FEKLRkhigivfqnpdNQFVGSIVKY-----DVAfGLENHAVPY-------DEMHRRVSEALKQVDMLERADYEPNALSG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 149 GERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
Cdd:PRK13648 146 GQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-223 |
4.57e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.00 E-value: 4.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 15 YQEGS-VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM-SKLSSAAKAELRnQKLGFI 92
Cdd:PRK13641 12 YSPGTpMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLR-KKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 93 YQFHHL-LPDFTALENVAM-PLLIGKKKpAEINSRALEMLKAVGL-EHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
Cdd:PRK13641 91 FQFPEAqLFENTVLKDVEFgPKNFGFSE-DEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 170 DEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDL-QLAKRMSRQLEMRDGRL 223
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQK-AGHTVILVTHNMdDVAEYADDVLVLEHGKL 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-221 |
5.58e-30 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 112.19 E-value: 5.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCK--RYQEG---SVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssA 79
Cdd:PRK15112 4 LLEVRNLSKtfRYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH----F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 80 AKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKK-KPAEINSRALEMLKAVGL--EHrANHRPSELSGGERQRV 154
Cdd:PRK15112 80 GDYSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLlpDH-ASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDG 221
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQvLVMHQG 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-227 |
6.47e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 111.21 E-value: 6.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 29 SFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqkLGFIYQFHHLLPDFTALENV 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP------VSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 109 AMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLL 188
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1600897103 189 GELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL-----TAEL 227
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIApRSLVVADGRIawdgpTDEL 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-213 |
8.14e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.28 E-value: 8.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 3 KILLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSKlS 77
Cdd:COG1117 9 EPKIEVRNLNVYY--GDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIYD-P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 78 SAAKAELRnQKLGFIYQFHHLLPdFTALENVAMPL-LIGKKKPAEINSRALEMLKAVGL----EHRANHRPSELSGGERQ 152
Cdd:COG1117 84 DVDVVELR-RRVGMVFQKPNPFP-KSIYDNVAYGLrLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL-NRLqgtAFLVVTHDLQLAKRMS 213
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELkKDY---TIVIVTHNMQQAARVS 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-213 |
9.77e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 113.08 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 16 QEGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTP----TSGDVIFNGQPMSKLSSAAKAELRNQKLGF 91
Cdd:COG4170 16 PQGRVK--AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 92 IYQ--FHHLLPDFTALENV--AMP--LLIGK--KKPAEINSRALEMLKAVGL-EHRA--NHRPSELSGGERQRVAIARAL 160
Cdd:COG4170 94 IFQepSSCLDPSAKIGDQLieAIPswTFKGKwwQRFKWRKKRAIELLHRVGIkDHKDimNSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL----QLAKRMS 213
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLesisQWADTIT 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-206 |
1.46e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 112.51 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRY--QEGSVqTDVlHNVSFSVGEGEMMAIVGSSGSGKS-TLLHLLGGL--DTPTSGDVIFNGQPMSKLSSA 79
Cdd:PRK09473 12 LLDVKDLRVTFstPDGDV-TAV-NDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLaaNGRIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 80 AKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKK-KPAEINSRALEMLKAVGL---EHRANHRPSELSGGERQR 153
Cdd:PRK09473 90 ELNKLRAEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGmSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-213 |
1.47e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.77 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 21 QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQF 95
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVI---ELR-RRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 96 HHLLPDFTALENVAMPLLIGK--KKPAEINSRALEMLKAVGL----EHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1600897103 170 DEPTGNLDARNADSIFQLLGELNRlqGTAFLVVTHDLQLAKRMS 213
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARIS 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-227 |
1.62e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.74 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 3 KILLQCDNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakA 82
Cdd:COG3845 255 EVVLEVENLSVRDDRG---VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP---R 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 83 ELRNQKLGFIYQ--FHH-LLPDFTALENVAMPLLIGKK-------KPAEINSRALEML-----KAVGLEHRAnhrpSELS 147
Cdd:COG3845 329 ERRRLGVAYIPEdrLGRgLVPDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIeefdvRTPGPDTPA----RSLS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL----QLAKRMsrqLEMRDGRL 223
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLdeilALSDRI---AVMYEGRI 480
|
....
gi 1600897103 224 TAEL 227
Cdd:COG3845 481 VGEV 484
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-221 |
1.71e-29 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 114.88 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYqeGSVQTdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
Cdd:PRK09700 1 MATPYISMAGIGKSF--GPVHA--LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELrnqKLGFIYQFHHLLPDFTALENVAMPLLIGKK-------KPAEINSRALEMLKAVGLEHRANHRPSELSGGERQR 153
Cdd:PRK09700 77 AAQL---GIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-226 |
1.79e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 110.56 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQK 88
Cdd:COG4604 5 KNVSKRYG----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQFHHLLPDFTALENVAM---PLLIGKKKPA--EINSRALEMLKAVGLEHRanhRPSELSGGERQRVAIARALVNN 163
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAFgrfPYSKGRLTAEdrEIIDEAIAYLDLEDLADR---YLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYAdHIVAMKDGRVVAQ 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
1.87e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.09 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSkLSSAA 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELRnQKLGFIYQF-HHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARA 159
Cdd:PRK13636 77 LMKLR-ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1600897103 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDI 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-206 |
2.91e-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: 109.63 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGSvqtDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQK 88
Cdd:cd03253 4 ENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR-RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQFHHLLPDfTALENVAMPLL-------IGKKKPAEINSRALEMLKavGLEHRANHRPSELSGGERQRVAIARALV 161
Cdd:cd03253 77 IGVVPQDTVLFND-TIGYNIRYGRPdatdeevIEAAKAAQIHDKIMRFPD--GYDTIVGERGLKLSGGEKQRVAIARAIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1600897103 162 NNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDL 206
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRL 196
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-233 |
3.77e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.79 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSV-QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
Cdd:COG1101 2 LELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 rnqkLGFIYQfHHLL---PDFTALENVAMPLLIGKKKPAeinSRAL---------EMLKAV--GLEHRANHRPSELSGGE 150
Cdd:COG1101 82 ----IGRVFQ-DPMMgtaPSMTIEENLALAYRRGKRRGL---RRGLtkkrrelfrELLATLglGLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 151 RQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSl 229
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMHEGRIILDVS- 232
|
....
gi 1600897103 230 mGAE 233
Cdd:COG1101 233 -GEE 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-225 |
4.19e-29 |
|
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: 114.07 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 21 QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRnQKLGFIYQFHHLLP 100
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REELG-RHIGYLPQDVELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 DfTALENVA-MPlligkkkpaEINSRA-LEMLKAVGL-----------EHRANHRPSELSGGERQRVAIARALVNNPRLV 167
Cdd:COG4618 420 G-TIAENIArFG---------DADPEKvVAAAKLAGVhemilrlpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 168 LADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRVQA 546
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-208 |
4.47e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 110.99 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKS-TLLHLLGGLDTP---TSGDVIFNGQPMSKLSSAA 80
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLI---GKKKpaEINSRALEMLKAVGL---EHRANHRPSELSGGERQ 152
Cdd:PRK11022 83 RRNLVGAEVAMIFQdpMTSLNPCYTVGFQIMEAIKVhqgGNKK--TRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAL 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-216 |
5.13e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 114.18 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 27 NVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQ--FHHLLPDFTA 104
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQdpYASLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENVAMPLLI-GKKKPAEINSRALEMLKAVGL--EHrANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
Cdd:PRK10261 421 GDSIMEPLRVhGLLPGKAAAARVAWLLERVGLlpEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190
....*....|....*....|....*....|....*
gi 1600897103 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-222 |
8.10e-29 |
|
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: 108.47 E-value: 8.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQk 88
Cdd:cd03251 4 KNVTFRYPGD--GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLA---SLRRQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQFHHLLPDfTALENVAmpllIGKkkPAEINSRALEMLKAV-----------GLEHRANHRPSELSGGERQRVAIA 157
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIA----YGR--PGATREEVEEAARAAnahefimelpeGYDTVIGERGVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGEL--NRlqgTAFlVVTHDLQLAKRMSRQLEMRDGR 222
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLmkNR---TTF-VIAHRLSTIENADRIVVLEDGK 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-226 |
8.93e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 110.69 E-value: 8.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaAKAELRNQKLGFIYQFHHLLPDFT 103
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-----ARARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVampLLIGK---KKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
Cdd:PRK13536 131 VRENL---LVFGRyfgMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1600897103 181 ADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAE 226
Cdd:PRK13536 208 RHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLcVLEAGRKIAE 253
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-222 |
1.01e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 108.54 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQeGSVQTDvlhNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFG-GLLAVN---NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAelrnqKLGFIYQFHH--LLPDFTALEN--VAM------PLLIG-------KKKPAEINSRALEMLKAVGLEHRANHRP 143
Cdd:PRK11300 77 IA-----RMGVVRTFQHvrLFREMTVIENllVAQhqqlktGLFSGllktpafRRAESEALDRAATWLERVGLLEHANRQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 144 SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISdRIYVVNQGT 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-191 |
1.45e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 112.83 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTP---TSGDVIFNGQPMSKlssaakAELRnQKLGFIYQFHHLLPD 101
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDA------KEMR-AISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 FTALEN------VAMPLLIGKKKPAEinsRALEMLKAVGLEHRAN------HRPSELSGGERQRVAIARALVNNPRLVLA 169
Cdd:TIGR00955 114 LTVREHlmfqahLRMPRRVTKKEKRE---RVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180
....*....|....*....|..
gi 1600897103 170 DEPTGNLDARNADSIFQLLGEL 191
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGL 212
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-207 |
1.68e-28 |
|
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: 107.75 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVQTDVlhnvSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELr 85
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDV----SLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqKLGFIYQFHHLLPDFTALENVAMPL-LIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:TIGR04406 77 --GIGYLPQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVR 196
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-206 |
3.06e-28 |
|
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: 106.85 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQFHHLLpDFT 103
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR---WLRSQ-IGLVSQEPVLF-DGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMplliGKkkpaeiNSRALEMLKAV---------------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
Cdd:cd03249 93 IAENIRY----GK------PDATDEEVEEAakkanihdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1600897103 169 ADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDL 206
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRL 198
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-226 |
3.92e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.58 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQeGSVqtDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssAAKAEL 84
Cdd:PRK13652 3 LIETRDLCYSYS-GSK--EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQFhhllPD-----FTALENVAM-PLLIGKKKPAeINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIAR 158
Cdd:PRK13652 77 R-KFVGLVFQN----PDdqifsPTVEQDIAFgPINLGLDEET-VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAE 226
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYvMDKGRIVAY 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-223 |
5.87e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.12 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGSVQTDvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRnQKL 89
Cdd:PRK13650 9 NLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIR-HKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 GFIYQFhhllPD--FT----------ALENVAMPLligkkkpAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIA 157
Cdd:PRK13650 84 GMVFQN----PDnqFVgatveddvafGLENKGIPH-------EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-223 |
8.75e-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: 104.94 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 29 SFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqkLGFIYQFHHLLPDFTALENV 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 109 AMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLL 188
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1600897103 189 GELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIaSQIAVVSQGKI 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-225 |
7.76e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.46 E-value: 7.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 22 TDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHHLLPD 101
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 FTALENVAM---PLLIGKKKPAEINSRALE-MLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:PRK09536 92 FDVRQVVEMgrtPHRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1600897103 178 ARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTA 225
Cdd:PRK09536 172 INHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVlLADGRVRA 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-221 |
9.27e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 9.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIF-NGQPMSKLSsaakaelrnQKLgfiYqfhhlLPDF 102
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP---------QRP---Y-----LPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 103 TALENVAMPLLIGKKKPAEInsraLEMLKAVGLEHRANH------RPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
Cdd:COG4178 441 TLREALLYPATAEAFSDAEL----REALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1600897103 177 DARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
Cdd:COG4178 517 DEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-223 |
1.73e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 106.85 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVQTDvlhNVSFSVGEGEMMAIVGSSGSGKSTLLH-LLGGLdtPTSGDVIFNGQPMSKLSsaaKAEL 84
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAG---PLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELD---PESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQFHHLLPDfTALENVAMplliGKKK--PAEIN-----SRALEMLKAV--GLEHRANHRPSELSGGERQRVA 155
Cdd:PRK11174 422 R-KHLSWVGQNPQLPHG-TLRDNVLL----GNPDasDEQLQqalenAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT--LMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-204 |
1.78e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 15 YQEGS-VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIY 93
Cdd:PRK13649 12 YQAGTpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 94 QF-HHLLPDFTALENVAM-PLLIGKKKpAEINSRALEMLKAVGL-EHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
Cdd:PRK13649 92 QFpESQLFEETVLKDVAFgPQNFGVSQ-EEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190
....*....|....*....|....*....|....
gi 1600897103 171 EPTGNLDARNADSIFQLLGELNRlQGTAFLVVTH 204
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTH 203
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-228 |
1.94e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.32 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 15 YQEGS-VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG-QPMSKLSSAAKAELRnQKLGFI 92
Cdd:PRK13646 12 YQKGTpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRPVR-KRIGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 93 YQFhhllPDFTALE-NVAMPLLIGKKK----PAEINSRALEMLKAVGLEHRA-NHRPSELSGGERQRVAIARALVNNPRL 166
Cdd:PRK13646 91 FQF----PESQLFEdTVEREIIFGPKNfkmnLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAELS 228
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTS 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
23-223 |
2.25e-26 |
|
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: 106.34 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 23 DVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQFHHLLPDf 102
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLA---SLRRQ-VALVSQDVVLFND- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 103 TALENVAMPLLIGKKKpAEInSRALEMLKAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
Cdd:TIGR02203 421 TIANNIAYGRTEQADR-AEI-ERALAAAYAQdfvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1600897103 175 NLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:TIGR02203 499 ALDNESERLVQAALERL--MQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-233 |
2.69e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.56 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHHLLPDFT 103
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAmpllIGK--------KKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
Cdd:PRK10575 102 VRELVA----IGRypwhgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 176 LDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAE---LSLMGAE 233
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLvALRGGEMIAQgtpAELMRGE 239
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-223 |
3.29e-26 |
|
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: 101.39 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 22 TDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssAAKAELRNQKLGFIYQ----FHH 97
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS----QYEHKYLHSKVSLVGQepvlFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 98 LLPDFTA--LENVAMPLLIGKKKPAEINSRALEMlkAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
Cdd:cd03248 103 SLQDNIAygLQSCSFECVKEAAQKAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1600897103 176 LDARNADSIFQLLGELNrlQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:cd03248 181 LDAESEQQVQQALYDWP--ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-226 |
5.64e-26 |
|
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: 100.87 E-value: 5.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQ--------EGSVQT---------DVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIF 68
Cdd:cd03267 1 IEVSNLSKSYRvyskepglIGSLKSlfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 69 NGQPMSKLSSAAKAelrnqKLGFIY-QFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELS 147
Cdd:cd03267 81 AGLVPWKRRKKFLR-----RIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDGRLTAE 226
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRLLYD 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-218 |
8.17e-26 |
|
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: 99.36 E-value: 8.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakAELRNQKLGFIYQFHHLLPDFT 103
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-----RDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAM--PLLIGKKKPAEinsralEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
Cdd:TIGR01189 90 ALENLHFwaAIHGGAQRTIE------DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1600897103 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKrmSRQLEM 218
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTHQDLGLVE--ARELRL 198
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-226 |
1.32e-25 |
|
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: 99.54 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 30 FSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaelRNQKLGFIYQFHHLLPDFTAleNVA 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK---------GWRHIGYVPQRHEFAWDFPI--SVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 110 MPLLIGK-------KKPAEINSRAL-EMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
Cdd:TIGR03771 70 HTVMSGRtghigwlRRPCVADFAAVrDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1600897103 182 DSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:TIGR03771 150 ELLTELFIELAG-AGTAILMTTHDLAQAMATCDRVVLLNGRVIAD 193
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-226 |
1.78e-25 |
|
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: 99.14 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaelrnqklGFiyqfhhlLPDFT 103
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG---------GF-------NPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1600897103 184 IFQLLGELNRlQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
Cdd:cd03220 181 CQRRLRELLK-QGKTVILVSHDPSSIKRLcDRALVLEKGKIRFD 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-223 |
2.16e-25 |
|
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: 99.11 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGSVqtDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRnQK 88
Cdd:cd03244 6 KNVSLRYRPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR-SR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQFHHLLPDfTALENVAmPLliGKKKPAEINsRALEM--LKAV------GLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLD-PF--GEYSDEELW-QALERvgLKEFveslpgGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-226 |
3.92e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILlQCDNLCKRYQEGSvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAA 80
Cdd:PRK13642 1 MNKIL-EVENLVFKYEKES-DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 KAELRnQKLGFIYQFhhllPD-----FTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVA 155
Cdd:PRK13642 76 VWNLR-RKIGMVFQN----PDnqfvgATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-223 |
8.80e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.11 E-value: 8.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaELRNQKLGFIYQfHHLLPDFT 103
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH----HYLHRQVALVGQ-EPVLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLliGKKKPAEINSRALE-------MLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
Cdd:TIGR00958 571 VRENIAYGL--TDTPDEEIMAAAKAanahdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1600897103 177 DARnadsIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:TIGR00958 649 DAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-213 |
1.27e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQegsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSK 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYN----KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 76 lSSAAKAELRnQKLGFIYQFHHLLPdFTALENVAMPLLIGKKKPAEINSRALEM-LKAVGLEHRANHRPSE----LSGGE 150
Cdd:PRK14239 77 -PRTDTVDLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKsLKGASIWDEVKDRLHDsalgLSGGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 151 RQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrlQGTAFLVVTHDLQLAKRMS 213
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRIS 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-213 |
2.02e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.43 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGL------DTPTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQFHH 97
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAI---KLR-KEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 98 LLPDFTALENVAMPLLI-GKKKPAEINSRALEMLKAVGL----EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKShGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1600897103 173 TGNLDARNADSIFQLLGELNRlqGTAFLVVTHDLQLAKRMS 213
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVA 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-223 |
2.69e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 97.08 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 19 SVQTDV--LHNVSFSVGEGEMMAIVGSSGSGKS-TLLHLLGGLD---TPTSGDVIFNGQPmsklssAAKAELRNQKLGFI 92
Cdd:PRK10418 11 ALQAAQplVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKP------VAPCALRGRKIATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 93 YQfhHLLPDFTALENV---AMPLLIGKKKPAEiNSRALEMLKAVGLEHRA---NHRPSELSGGERQRVAIARALVNNPRL 166
Cdd:PRK10418 85 MQ--NPRSAFNPLHTMhthARETCLALGKPAD-DATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAvMSHGRI 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-223 |
2.80e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.77 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGS-VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM-SKLSSAAKAELRN 86
Cdd:PRK13645 10 DNVSYTYAKKTpFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 87 QKLGFIYQF--HHLLPDfTALENVAM-PLLIGKKKpAEINSRALEMLKAVGL-EHRANHRPSELSGGERQRVAIARALVN 162
Cdd:PRK13645 90 KEIGLVFQFpeYQLFQE-TIEKDIAFgPVNLGENK-QEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRL 223
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKV 229
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
14-226 |
3.04e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 100.59 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 14 RYQEGSvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNQkLGFIY 93
Cdd:TIGR01846 464 RYAPDS--PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGV---DLAIADPAWLRRQ-MGVVL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 94 Q----FHHLLPDFTALENVAMPL--LIGKKKPAEinsrALEMLKAV--GLEHRANHRPSELSGGERQRVAIARALVNNPR 165
Cdd:TIGR01846 538 QenvlFSRSIRDNIALCNPGAPFehVIHAAKLAG----AHDFISELpqGYNTEVGEKGANLSGGQRQRIAIARALVGNPR 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRlqGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRACDRIIVLEKGQIAES 672
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-221 |
5.96e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 99.35 E-value: 5.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLsSAAKAel 84
Cdd:PRK15439 11 LLCARSISKQY--SGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 rnQKLGfIY---QFHHLLPDFTALENVamplLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALV 161
Cdd:PRK15439 84 --HQLG-IYlvpQEPLLFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 162 NNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL----QLAKRMSrqlEMRDG 221
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLpeirQLADRIS---VMRDG 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-224 |
6.20e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 3 KILLQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQpmsklssaaka 82
Cdd:COG0488 313 KKVLELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE----------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 83 elrNQKLGFIYQFHHLL-PDFTALENVAMplliGKKKPAEINSRAL---------EMLKAVGlehranhrpsELSGGERQ 152
Cdd:COG0488 377 ---TVKIGYFDQHQEELdPDKTVLDELRD----GAPGGTEQEVRGYlgrflfsgdDAFKPVG----------VLSGGEKA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 153 RVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHDLQLAKRM-SRQLEMRDGRLT 224
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLD---IETLEALEEALDDFPGTV-LLVSHDRYFLDRVaTRILEFEDGGVR 508
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-213 |
9.28e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.29 E-value: 9.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 21 QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSKlSSAAKAELRnQKLGFIYQF 95
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVR-REVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 96 HHLLPDFTALENVAMPLLIGK--KKPAEINSRALEMLKAVGL----EHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1600897103 170 DEPTGNLDARNADSIFQLLGELNrlQGTAFLVVTHDLQLAKRMS 213
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVS 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-218 |
9.39e-24 |
|
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: 94.10 E-value: 9.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssAAKAELRNQKLGFIYQFHHLLPDFT 103
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLIGKKKPAEinsRALEMLKAVGLEHRANHrpsELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
Cdd:cd03231 90 VLENLRFWHADHSDEQVE---EALARVGLNGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1600897103 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-206 |
2.48e-23 |
|
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: 97.58 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHLLPDfT 103
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS---LRAA-IGIVPQDTVLFND-T 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPlligkkKP----AEINSRA--------LEMLKAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
Cdd:COG5265 448 IAYNIAYG------RPdaseEEVEAAAraaqihdfIESLPD-GYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190
....*....|....*....|....*....|....*.
gi 1600897103 172 PTGNLDARNADSIfqlLGELNRL-QGTAFLVVTHDL 206
Cdd:COG5265 521 ATSALDSRTERAI---QAALREVaRGRTTLVIAHRL 553
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-222 |
2.55e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 97.31 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYqeGSVQTdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLdTPT---SGDVIFNGQPMsKLS 77
Cdd:PRK13549 1 MMEYLLEMKNITKTF--GGVKA--LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEEL-QAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 78 SAAKAELRNqkLGFIYQFHHLLPDFTALENVAM---PLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRV 154
Cdd:PRK13549 75 NIRDTERAG--IAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLE-MRDGR 222
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICvIRDGR 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
21-208 |
3.56e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.03 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 21 QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaeLRnqkLGFIYQFHHLLP 100
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LR---IGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 dftalenvAMPLLIGK---KKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:PRK09544 81 --------TLPLTVNRflrLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190
....*....|....*....|....*....|.
gi 1600897103 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-223 |
3.80e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.34 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkLGFIYQfHHLLPDFTA 104
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRN-IAVVFQ-DAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENvampLLIGKK--KPAEInSRALE--------MLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
Cdd:PRK13657 426 EDN----IRVGRPdaTDEEM-RAAAEraqahdfiERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 175 NLDARNADSIFQLLGEL--NRlqgTAFlVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:PRK13657 501 ALDVETEAKVKAALDELmkGR---TTF-IIAHRLSTVRNADRILVFDNGRV 547
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-222 |
3.93e-23 |
|
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: 90.97 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGsvqtDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaelR 85
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------S 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQKLGFIYQfhhllpdftalenvamplligkkkpaeinsralemlkavglehranhrpseLSGGERQRVAIARALVNNPR 165
Cdd:cd03221 62 TVKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 166 LVLADEPTGNLDarnADSIFQLLGELNRLQGTaFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:cd03221 91 LLLLDEPTNHLD---LESIEALEEALKEYPGT-VILVSHDRYFLDQVAtKIIELEDGK 144
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-225 |
4.43e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 95.33 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 39 AIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAK-----AELRnqKLGFIYQFHHLLPDFTALENvampLL 113
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLFDAEKgiclpPEKR--RIGYVFQDARLFPHYKVRGN----LR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 114 IG--KKKPAEINsRALEMLkavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL 191
Cdd:PRK11144 99 YGmaKSMVAQFD-KIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1600897103 192 NRLQGTAFLVVTHDLQ----LAKRMsrqLEMRDGRLTA 225
Cdd:PRK11144 175 AREINIPILYVSHSLDeilrLADRV---VVLEQGKVKA 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-216 |
7.93e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.79 E-value: 7.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 26 HNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqklgfIYQFHH--LLPDFT 103
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL-------LYLGHQpgIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLIGKKKPAEINSRALEmlkAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDEALWEALA---QVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170 180 190
....*....|....*....|....*....|...
gi 1600897103 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
Cdd:PRK13538 168 LEALLAQHAEQGGMVILTTHQDLPVASDKVRKL 200
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-223 |
9.13e-23 |
|
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: 96.35 E-value: 9.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSvqtDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELR 85
Cdd:TIGR01193 474 IVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 nqklgfiyQFHHLLP------DFTALENvampLLIGKKKPAEINS--RALEMLK--------AVGLEHRANHRPSELSGG 149
Cdd:TIGR01193 548 --------QFINYLPqepyifSGSILEN----LLLGAKENVSQDEiwAACEIAEikddienmPLGYQTELSEEGSSISGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 150 ERQRVAIARALVNNPRLVLADEPTGNLDARNADSIfqlLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKI---VNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-225 |
1.36e-22 |
|
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: 95.49 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 21 QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakAELRN-------QKLGFIY 93
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG-----------ADLKQwdretfgKHIGYLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 94 QFHHLLPDfTALENVA-MPLLIGKKK--PAEINSRALEMLKAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
Cdd:TIGR01842 399 QDVELFPG-TVAENIArFGENADPEKiiEAAKLAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 169 ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRIAR 533
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-225 |
1.39e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.21 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLSSAAKAELR-----NQKLGFIYQFHHLL 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 100 pdftALenvAMPlligKKKPAEINSRALEML-KAVGLEHRANHRPSELSGGERQRVAIARALV-----NNP--RLVLADE 171
Cdd:COG4138 91 ----AL---HQP----AGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPegQLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 172 PTGNLDARNADSIFQLLGELNRLQGTAfLVVTHDLQLAKRMSRQ-LEMRDGRLTA 225
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQGITV-VMSSHDLNHTLRHADRvWLLKQGKLVA 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-226 |
1.68e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.86 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAa 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY--GKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 kaELRNQKLGFIYQFHHLLPDFTALENVAMP-LLIGKKKPAEINSRALEMLKAvgLEHRANHRPSELSGGERQRVAIARA 159
Cdd:PRK11614 76 --KIMREAVAIVPEGRRVFSRMTVEENLAMGgFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
2.44e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.99 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 2 NKILLQCDNLCKRYQEGSV-QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV----IFNGQ---PM 73
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQEnELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDkknNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 74 SKLSSAAKAELRNQK-----LGFIYQF--HHLLPDFTALENVAMPLLIGKKKpAEINSRALEMLKAVGLEHRANHR-PSE 145
Cdd:PRK13631 98 ELITNPYSKKIKNFKelrrrVSMVFQFpeYQLFKDTIEKDIMFGPVALGVKK-SEAKKLAKFYLNKMGLDDSYLERsPFG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFlVVTHdlqlakRMSRQLEMRD 220
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVF-VITH------TMEHVLEVAD 244
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
3.36e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.91 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILlQCDNLCKRYQEGSVQTD------------------VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT 62
Cdd:COG1134 1 MSSMI-EVENVSKSYRLYHEPSRslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 63 SGDVIFNGQPMSKLSsaakaelrnqkLGFIyqFHhllPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEhRANHR 142
Cdd:COG1134 80 SGRVEVNGRVSALLE-----------LGAG--FH---PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELG-DFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 143 P-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARnadsiFQ--LLGELNRL--QGTAFLVVTHDLQLAKRM-SRQL 216
Cdd:COG1134 143 PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA-----FQkkCLARIRELreSGRTVIFVSHSMGAVRRLcDRAI 217
|
250
....*....|
gi 1600897103 217 EMRDGRLTAE 226
Cdd:COG1134 218 WLEKGRLVMD 227
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-208 |
3.52e-22 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 92.56 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 17 EGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTP----TSGDVIFNGQPMSKLSSAAKAELRNQKLGFI 92
Cdd:PRK15093 17 DGWVK--AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGHNVSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 93 YQFHHLLPDFTalENVAMPLL---------------IGKKKpaeinSRALEMLKAVGL-EHRANHR--PSELSGGERQRV 154
Cdd:PRK15093 95 FQEPQSCLDPS--ERVGRQLMqnipgwtykgrwwqrFGWRK-----RRAIELLHRVGIkDHKDAMRsfPYELTEGECQKV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQM 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-226 |
7.20e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 7.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP---MSKLSSAAK 81
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 82 ---AELRNQKLGFIYQFHHLLPDFTAlENVAMPlligkkkPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIAR 158
Cdd:PRK13644 78 lvgIVFQNPETQFVGRTVEEDLAFGP-ENLCLP-------PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-204 |
9.31e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.16 E-value: 9.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqklgfiYQFHH--LLPD 101
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH---------YLGHRnaMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 FTALENVAMplligkkkPAEI----NSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:PRK13539 88 LTVAENLEF--------WAAFlggeELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*..
gi 1600897103 178 aRNADSIFQLLGELNRLQGTAFLVVTH 204
Cdd:PRK13539 160 -AAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-206 |
9.50e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 90.33 E-value: 9.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaELRNQKLGFIYQFHHLLPDFTA 104
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 L-ENVAMP--------LLIGKKKPAEINSRALEMLKAVGLEHRanhRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
Cdd:PRK15056 96 LvEDVVMMgryghmgwLRRAKKRDRQIVTAALARVDMVEFRHR---QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190
....*....|....*....|....*....|.
gi 1600897103 176 LDARNADSIFQLLGELnRLQGTAFLVVTHDL 206
Cdd:PRK15056 173 VDVKTEARIISLLREL-RDEGKTMLVSTHNL 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-222 |
1.39e-21 |
|
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: 88.30 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 16 QEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLH-LLGGLdTPTSGDVIFNG-------QP--MSklssaakAELR 85
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGsiayvsqEPwiQN-------GTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQKLgFIYQFHH-----------LLPDFTALENVAMpLLIGKKKpaeINsralemlkavglehranhrpseLSGGERQRV 154
Cdd:cd03250 84 ENIL-FGKPFDEeryekvikacaLEPDLEILPDGDL-TEIGEKG---IN----------------------LSGGQKQRI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQ--LLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGR 222
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-225 |
1.45e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 89.61 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 28 VSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLSSAAKAELR-----NQKLGFIYQ-FHHL--- 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRaylsqQQTPPFAMPvFQYLtlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 99 LPDFTALENVAmplligkkkpaeinsRALEML-KAVGLEHRAnHRP-SELSGGERQRVAIARAL-----VNNP--RLVLA 169
Cdd:PRK03695 94 QPDKTRTEAVA---------------SALNEVaEALGLDDKL-GRSvNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 170 DEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTA 225
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLnHTLRHADRVWLLKQGKLLA 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-222 |
1.73e-21 |
|
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: 92.20 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYqeGSVQTdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGL--DTPTSGDVIFNGQPMsKLSSAAKA 82
Cdd:TIGR02633 1 LLEMKGIVKTF--GGVKA--LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPL-KASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 83 ELRNqkLGFIYQFHHLLPDFTALENVAMPLLI----GKKKPAEINSRALEMLKAVGLEHRANHRP-SELSGGERQRVAIA 157
Cdd:TIGR02633 76 ERAG--IVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLE-MRDGR 222
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICvIRDGQ 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-204 |
2.01e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 15 YQEGS-VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIY 93
Cdd:PRK13643 11 YQPNSpFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 94 QF-HHLLPDFTALENVAM-PLLIGKKKpAEINSRALEMLKAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLAD 170
Cdd:PRK13643 91 QFpESQLFEETVLKDVAFgPQNFGIPK-EKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190
....*....|....*....|....*....|....
gi 1600897103 171 EPTGNLDARNADSIFQLLGELNRlQGTAFLVVTH 204
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIHQ-SGQTVVLVTH 202
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-226 |
2.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.86 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD---VIFNGqpmSKLSSAAKAELRnQKLGFIYQFhhllP 100
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDG---ITLTAKTVWDIR-EKVGIVFQN----P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 D--FTA----------LENVAMPlligKKKPAEINSRALEmlkAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
Cdd:PRK13640 94 DnqFVGatvgddvafgLENRAVP----RPEMIKIVRDVLA---DVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQ 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-212 |
3.08e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.76 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL------RNQklgfiyqfhhL 98
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIgvvfgqRSQ----------L 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 99 LPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANhRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:COG4586 108 WWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD-TPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 1600897103 178 ARNADSIFQLLGELNRLQGTAFLVVTHDL----QLAKRM 212
Cdd:COG4586 187 VVSKEAIREFLKEYNRERGTTILLTSHDMddieALCDRV 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-204 |
3.67e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.20 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 23 DVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLD--TPTSGDVIFNGQPMSKLSSAAKAelrnqKLGFIYQFHHllP 100
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERA-----RAGIFLAFQY--P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 ---------DF--TALENVAMPLLigkkKPAEINSRALEMLKAVGLEHRANHRP--SELSGGERQRVAIARALVNNPRLV 167
Cdd:COG0396 87 veipgvsvsNFlrTALNARRGEEL----SAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1600897103 168 LADEPTGNLDarnADSiFQLLGE-LNRL--QGTAFLVVTH 204
Cdd:COG0396 163 ILDETDSGLD---IDA-LRIVAEgVNKLrsPDRGILIITH 198
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-207 |
6.56e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEl 84
Cdd:PRK10895 3 TLTAKNLAKAYKG----RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 rnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEI-NSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
Cdd:PRK10895 78 --RGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1600897103 164 PRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVR 198
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-226 |
1.19e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS----KLSSAAKaelrnqkLGFIYQFHHLLP 100
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQEAG-------IGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 DFTALENV----AMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
Cdd:PRK10762 93 QLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 177 DARNADSIFQLLGELnRLQGTAFLVVTHdlqlakRMSRQLE-------MRDGRLTAE 226
Cdd:PRK10762 173 TDTETESLFRVIREL-KSQGRGIVYISH------RLKEIFEicddvtvFRDGQFIAE 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-223 |
2.80e-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: 89.30 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQE-GSVQTDVLhNVSFSvgEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQK 88
Cdd:TIGR01257 933 NLVKIFEPsGRPAVDRL-NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR-----QS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQ----FHHLlpdfTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:TIGR01257 1005 LGMCPQhnilFHHL----TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAiISQGRL 1138
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-222 |
3.22e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.76 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKS-TLLHLLGGLDTpTSGDVifNGQPM---------- 73
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLV--QCDKMllrrrsrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 74 --SKLSSAAKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLI----GKKKPAEINSRALEMLKAVGLEHRANHRPSE 145
Cdd:PRK10261 89 elSEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIRLhqgaSREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIAdRVLVMYQGE 246
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-206 |
1.21e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.08 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 9 DNLCKRYQEGSVqtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQK 88
Cdd:PRK10790 344 DNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV---LR-QG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQFHHLLPDfTALENVAMplliGKKKPAEINSRALEMLKAV--------GLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:PRK10790 417 VAMVQQDPVVLAD-TFLANVTL----GRDISEEQVWQALETVQLAelarslpdGLYTPLGEQGNNLSVGQKQLLALARVL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNrlQGTAFLVVTHDL 206
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVR--EHTTLVVIAHRL 535
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-228 |
3.10e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.87 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 27 NVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqklGFIY-----QFHHLLPD 101
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR-----GLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 FTALENVA------MPLLIGKKKPAEINSRALEMLkAVGLEHrANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
Cdd:PRK15439 356 APLAWNVCalthnrRGFWIKPARENAVLERYRRAL-NIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 176 LD--ARNadSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
Cdd:PRK15439 434 VDvsARN--DIYQLIRSIAA-QNVAVLFISSDLEEIEQMAdRVLVMHQGEISGALT 486
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-226 |
3.53e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.19 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLD--TPTSGDVIFNGQPMSKLSsaakaelrnqklgfiyqfhhllPD 101
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLP----------------------PE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 ftalENVAMPLLIGKKKPAEINS-RALEMLKAVGLEhranhrpseLSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
Cdd:cd03217 73 ----ERARLGIFLAFQYPPEIPGvKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1600897103 181 ADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS--RQLEMRDGRLTAE 226
Cdd:cd03217 140 LRLVAEVINKLRE-EGKSVLIITHYQRLLDYIKpdRVHVLYDGRIVKS 186
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-204 |
4.50e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.31 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 20 VQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLdtptsgdvifngqpMSKLSSAAKAELRNQKLGfiyqfhhll 99
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA--------------LKGTPVAGCVDVPDNQFG--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 100 PDFTALENVAMplligKKKPAEinsrALEMLKAVGLEHRANHR--PSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:COG2401 98 REASLIDAIGR-----KGDFKD----AVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*..
gi 1600897103 178 ARNADSIFQLLGELNRLQGTAFLVVTH 204
Cdd:COG2401 169 RQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
24-210 |
5.44e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 81.53 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFT 103
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ-----KQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLligkkKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
Cdd:PRK13540 91 LRENCLYDI-----HFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*...
gi 1600897103 184 IFQLLgELNRLQGTAFLVVTH-DLQLAK 210
Cdd:PRK13540 166 IITKI-QEHRAKGGAVLLTSHqDLPLNK 192
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-213 |
6.95e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSkLSSAAKAEL 84
Cdd:PRK13638 1 MLATSDLWFRYQD----EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQFhhllPD----FTALE-NVAMPLLIGKKKPAEINSRALEMLKAVGLEHrANHRPSE-LSGGERQRVAIAR 158
Cdd:PRK13638 76 R-QQVATVFQD----PEqqifYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQH-FRHQPIQcLSHGQKKRVAIAG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 159 ALVNNPRLVLADEPTGNLDARNADsifQLLGELNRL--QGTAFLVVTHDLQLAKRMS 213
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRT---QMIAIIRRIvaQGNHVIISSHDIDLIYEIS 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-206 |
7.61e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS--KLSSaakaeLRNQkLGFIYQFHHLLPDf 102
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLAS-----LRNQ-VALVSQNVHLFND- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 103 TALENVAMPLLiGKKKPAEInSRALEMLKAVG----LEHRANHRPSE----LSGGERQRVAIARALVNN-PRLVLaDEPT 173
Cdd:PRK11176 432 TIANNIAYART-EQYSREQI-EEAARMAYAMDfinkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDsPILIL-DEAT 508
|
170 180 190
....*....|....*....|....*....|....*
gi 1600897103 174 GNLDARNADSIFQLLGEL--NRlqgTAfLVVTHDL 206
Cdd:PRK11176 509 SALDTESERAIQAALDELqkNR---TS-LVIAHRL 539
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-206 |
1.11e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLdTPT---SGDVIFNGQPMsKLSSAAKAElrnqKLG--FIYQFHHLL 99
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVC-RFKDIRDSE----ALGivIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 100 PDFTALENVAMPLLIGKKKP---AEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
Cdd:NF040905 91 PYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190
....*....|....*....|....*....|
gi 1600897103 177 DARNADSIFQLLGELnRLQGTAFLVVTHDL 206
Cdd:NF040905 171 NEEDSAALLDLLLEL-KAQGITSIIISHKL 199
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
25-223 |
1.72e-18 |
|
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: 83.79 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmSKLSSAAKAELRNQkLGFIYQFHHLLpDFTA 104
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDG---IDINTVTRESLRKS-IATVFQDAGLF-NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENVAmpllIGKKKP--AEINSRALEMLKAVGLEHRAN-------HRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
Cdd:TIGR01192 426 RENIR----LGREGAtdEEVYEAAKAAAAHDFILKRSNgydtlvgERGNRLSGGERQRLAIARAILKNAPILVLDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 176 LD----ARNADSIFQLlgelnRLQGTAFlVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:TIGR01192 502 LDveteARVKNAIDAL-----RKNRTTF-IIAHRLSTVRNADLVLFLDQGRL 547
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-213 |
1.73e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.62 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSKlSSAAKAELRNQkLGFIYQFHHL 98
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYE-RRVNLNRLRRQ-VSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 99 LPdFTALENVAMPL-LIGKKKPAEINSRALEMLKAVGL----EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
Cdd:PRK14258 100 FP-MSVYDNVAYGVkIVGWRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1600897103 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS 213
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-205 |
1.90e-18 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 83.45 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFngQPmsklssaakaelrNQKLGFIYQFHHLLPDFT 103
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QP-------------GIKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLliGKKK----------------PAEINSRALEM------LKAVG---LEHR------ANHRP------SEL 146
Cdd:TIGR03719 85 VRENVEEGV--AEIKdaldrfneisakyaepDADFDKLAAEQaelqeiIDAADawdLDSQleiamdALRCPpwdadvTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1600897103 147 SGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVTHD 205
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTV-VAVTHD 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-204 |
4.21e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.48 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 27 NVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssAAKAELRnQKLGFIYQFHHLLPDFTALE 106
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD----AGDIATR-RRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 107 NVA-------MPlligkkkPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD-- 177
Cdd:NF033858 359 NLElharlfhLP-------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpv 431
|
170 180
....*....|....*....|....*...
gi 1600897103 178 ARnaDSIFQLLGELNRLQG-TAFlVVTH 204
Cdd:NF033858 432 AR--DMFWRLLIELSREDGvTIF-ISTH 456
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-218 |
6.66e-18 |
|
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: 77.58 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFngqpmsklssaakaeLRNQKLGFIYQfHHLLPDFT 103
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PEGEDLLFLPQ-RPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLigkkkpaeinsralemlkavglehranhrpSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
Cdd:cd03223 80 LREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180 190
....*....|....*....|....*....|....*
gi 1600897103 184 IFQLLgelnRLQGTAFLVVTHDLQLAKRMSRQLEM 218
Cdd:cd03223 130 LYQLL----KELGITVISVGHRPSLWKFHDRVLDL 160
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-228 |
1.13e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 14 RYQEGSVQtdvlhNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ---PMSKLSSAAKAelrnqkLG 90
Cdd:PRK09700 273 SRDRKKVR-----DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDAVKKG------MA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 91 FIYQFHH---LLPDFTALENVAMP--LLIGK-------------KKPAEiNSRALEMLKAvgleHRANHRPSELSGGERQ 152
Cdd:PRK09700 342 YITESRRdngFFPNFSIAQNMAISrsLKDGGykgamglfhevdeQRTAE-NQRELLALKC----HSVNQNITELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAELS 228
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELpEIITVCDRIAVFCEGRLTQILT 492
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-226 |
1.21e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSG-----DVIFNGQPMSKLSSAAkaELRnQKLGFIYQFHHL 98
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVL--EFR-RRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 99 LPdFTALENVAMPLLIGKKKP-AEINSRALEMLKAVGL----EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
Cdd:PRK14271 113 FP-MSIMDNVLAGVRAHKLVPrKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 174 GNLDARNADSIFQLLGEL-NRLqgtAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLaDRL---TVIIVTHNLAQAARISdRAALFFDGRLVEE 243
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-226 |
9.18e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.79 E-value: 9.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGlDTPTS---------GDVIFNGQPMSKLSSAAKAELRnqklGFIYQ 94
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLR----AVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 95 FHHLLPDFTALENVamplLIGKKKPA-----------EINSRALEMLKAVGLEHRanhRPSELSGGERQRVAIARALVN- 162
Cdd:PRK13547 91 AAQPAFAFSAREIV----LLGRYPHArragalthrdgEIAWQALALAGATALVGR---DVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 163 --------NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM-RDGRLTAE 226
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMlADGAIVAH 236
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-205 |
1.58e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.85 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEGSVqtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFngQPmsklssaa 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--AP-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 81 kaelrNQKLGFIYQFHHLLPDFTALENVAMPLliGKKKPA-----EINSR---------AL--------EMLKAVG---L 135
Cdd:PRK11819 69 -----GIKVGYLPQEPQLDPEKTVRENVEEGV--AEVKAAldrfnEIYAAyaepdadfdALaaeqgelqEIIDAADawdL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 136 EHR------------ANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfLVVT 203
Cdd:PRK11819 142 DSQleiamdalrcppWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQFLHDYPGTV-VAVT 217
|
..
gi 1600897103 204 HD 205
Cdd:PRK11819 218 HD 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-221 |
2.07e-16 |
|
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: 75.52 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 31 SVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaakaelrnqklgfiYQFHHLLPDFtalENVAM 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------------------YKPQYIKADY---EGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 111 PLLIGKKKPAEINSR-ALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN---ADSIFQ 186
Cdd:cd03237 80 DLLSSITKDFYTHPYfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKVIR 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1600897103 187 LLGELNrlQGTAFlVVTHDLQLAKRMSRQLEMRDG 221
Cdd:cd03237 160 RFAENN--EKTAF-VVEHDIIMIDYLADRLIVFEG 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-221 |
2.62e-16 |
|
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: 74.67 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLL-HLLGGLDTpTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLpDFT 103
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLIGKKK-PAEINSRALEM---LKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
Cdd:cd03290 95 VEENITFGSPFNKQRyKAVTDACSLQPdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1600897103 180 NADSIFQlLGELNRLQGT--AFLVVTHDLQLAKRMSRQLEMRDG 221
Cdd:cd03290 175 LSDHLMQ-EGILKFLQDDkrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-223 |
3.56e-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: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLR 85
Cdd:cd03369 7 IEVENLSVRYAPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NqKLGFIYQFHHLLpDFTALENVAMpllIGKKKPAEINSrALEmLKAVGLehranhrpsELSGGERQRVAIARALVNNPR 165
Cdd:cd03369 82 S-SLTIIPQDPTLF-SGTIRSNLDP---FDEYSDEEIYG-ALR-VSEGGL---------NLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREE--FTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
25-213 |
3.72e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.20 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLD--TPT---SGDVIFNGQPMSKlSSAAKAELRnQKLGFIYQFHHLL 99
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlIPGfrvEGKVTFHGKNLYA-PDVDPVEVR-RRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 100 PDfTALENVAM-PLLIGKKKPA-EINSRAL----------EMLKAVGLEhranhrpseLSGGERQRVAIARALVNNPRLV 167
Cdd:PRK14243 104 PK-SIYDNIAYgARINGYKGDMdELVERSLrqaalwdevkDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1600897103 168 LADEPTGNLDARNADSIFQLLGELNRlQGTaFLVVTHDLQLAKRMS 213
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKE-QYT-IIIVTHNMQQAARVS 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-201 |
3.95e-16 |
|
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: 73.84 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT---SGDVIFNGQPMSKLSSAAKAELrn 86
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 87 qklgfIYqfhhllpdfTALENVAMPLLIGKkkpaeinsralEMLKAVgLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
Cdd:cd03233 86 -----IY---------VSEEDVHFPTLTVR-----------ETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190
....*....|....*....|....*....|....*
gi 1600897103 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLV 201
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFV 174
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-225 |
1.18e-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: 75.22 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQegsvqtDVLHNVSFSVG-------EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmskLSS 78
Cdd:COG4615 328 LELRGVTYRYP------GEDGDEGFTLGpidltirRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 79 AAKAELRNQklgF--IYQFHHLLPDFTALENVAMPlligkkkpaeinSRALEMLKAVGLEHR---ANHRPS--ELSGGER 151
Cdd:COG4615 399 DNREAYRQL---FsaVFSDFHLFDRLLGLDGEADP------------ARARELLERLELDHKvsvEDGRFSttDLSQGQR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 152 QRVAIARALVNN-PRLVL----ADEptgnldarnaDSIF------QLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
Cdd:COG4615 464 KRLALLVALLEDrPILVFdewaADQ----------DPEFrrvfytELLPEL-KARGKTVIAISHDDRYFDLADRVLKMDY 532
|
....*
gi 1600897103 221 GRLTA 225
Cdd:COG4615 533 GKLVE 537
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-204 |
3.11e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.80 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklssAAKAElRNQKLGFIYQFHHLLPDFT 103
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT------ATRGD-RSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLIGKKKPAEINSRALEMlkaVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
Cdd:PRK13543 99 TLENLHFLCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180
....*....|....*....|.
gi 1600897103 184 IFQLLGELNRLQGTAfLVVTH 204
Cdd:PRK13543 176 VNRMISAHLRGGGAA-LVTTH 195
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-229 |
3.84e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.98 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 1 MNKILLQCDNLCKRYQEgsvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLD--TPTSGDVIFNGQPMSKLSs 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNE----NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLE- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 79 aakAELRNQK---LGFIYQFHhlLP-----DF--TALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSE--L 146
Cdd:CHL00131 78 ---PEERAHLgifLAFQYPIE--IPgvsnaDFlrLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNegF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 147 SGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRL--QGTAFLVVTHdlqlakrMSRQLE------- 217
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLD---IDALKIIAEGINKLmtSENSIILITH-------YQRLLDyikpdyv 222
|
250
....*....|....*...
gi 1600897103 218 --MRDGRL----TAELSL 229
Cdd:CHL00131 223 hvMQNGKIiktgDAELAK 240
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-191 |
6.36e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.38 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSgdviFNGQPMSKLSSAAKAELRnqKLGFIYQFHHLLPDFT 103
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILK--RTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVA------MPLLIGKKKPAEINSRALEMLKAVGLEHR--ANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
Cdd:PLN03211 157 VRETLVfcsllrLPKSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170
....*....|....*.
gi 1600897103 176 LDARNADSIFQLLGEL 191
Cdd:PLN03211 237 LDATAAYRLVLTLGSL 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-221 |
7.51e-15 |
|
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: 73.41 E-value: 7.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 22 TDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLLPD 101
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 fTALENVAMPLLIGKkkpaeinSRALEMLKAVGLEHRANHRPSE-----------LSGGERQRVAIARALVNNPRLVLAD 170
Cdd:TIGR01271 502 -TIKDNIIFGLSYDE-------YRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 171 EPTGNLDARNADSIFQ-----LLGELNRlqgtafLVVTHDLQLAKRMSRQLEMRDG 221
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFEsclckLMSNKTR------ILVTSKLEHLKKADKILLLHEG 623
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
25-204 |
9.83e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 69.96 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTP--TSGDVIFNGQPMsklssaaKAELRNQkLGFIYQFHHLLPDF 102
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPL-------DKNFQRS-TGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 103 TALEnvamplligkkkpaeinsralemlkavGLEHRANHRpsELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
Cdd:cd03232 95 TVRE---------------------------ALRFSALLR--GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180
....*....|....*....|..
gi 1600897103 183 SIFQLLGELNRlQGTAFLVVTH 204
Cdd:cd03232 146 NIVRFLKKLAD-SGQAILCTIH 166
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-228 |
1.13e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.31 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGSVQtdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmskLSSAAKAELRNqkl 89
Cdd:PRK10522 327 NVTFAYQDNGFS---VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---VTAEQPEDYRK--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 gfiyQFHHLLPDFTALENvampLLIGKKKPAEiNSRALEMLKAVGLEHR---ANHRPS--ELSGGERQRVAIARALVNNP 164
Cdd:PRK10522 398 ----LFSAVFTDFHLFDQ----LLGPEGKPAN-PALVEKWLERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTaELS 228
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS-ELT 531
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-228 |
1.49e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaAKAELRNqklGFIY-----QFHHLL 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS--PQDGLAN---GIVYisedrKRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 100 PDFTALENVAMPlligkkkpaeinsrALEML--KAVGLEHRANHR-------------PS------ELSGGERQRVAIAR 158
Cdd:PRK10762 343 LGMSVKENMSLT--------------ALRYFsrAGGSLKHADEQQavsdfirlfniktPSmeqaigLLSGGNQQKVAIAR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSdRILVMHEGRISGEFT 478
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-177 |
2.16e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.50 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 4 ILLQCDNLCKRYQEGSVqtdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMsklssaakae 83
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLL----IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV---------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 84 lrnqKLGFIYQFH-HLLPDFTALENVAMP---LLIGKKkpaEINSRAL---------EMLKAVGlehranhrpsELSGGE 150
Cdd:TIGR03719 386 ----KLAYVDQSRdALDPNKTVWEEISGGldiIKLGKR---EIPSRAYvgrfnfkgsDQQKKVG----------QLSGGE 448
|
170 180
....*....|....*....|....*..
gi 1600897103 151 RQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-188 |
2.83e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.28 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 21 QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQFHHLLP 100
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRS-RLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 DfTALENVAMplliGK--KKPAEINSRAleMLKAV---------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
Cdd:PRK10789 403 D-TVANNIAL----GRpdATQQEIEHVA--RLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
170
....*....|....*....
gi 1600897103 170 DEPTGNLDARNADSIFQLL 188
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNL 494
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-227 |
2.91e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLH-LLGGLDTPTSGDVIFNGQPMsKLSSAAKA---------ELRNQklgfiy 93
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPV-KIRNPQQAiaqgiamvpEDRKR------ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 94 qfHHLLPDFTALENVAMPLLIGKKKPAEINSrALEmLKAVG-----LEHRANH---RPSELSGGERQRVAIARALVNNPR 165
Cdd:PRK13549 350 --DGIVPVMGVGKNITLAALDRFTGGSRIDD-AAE-LKTILesiqrLKVKTASpelAIARLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 166 LVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAEL 227
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSdRVLVMHEGKLKGDL 487
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-227 |
2.93e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.39 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 27 NVSFSVGEGEMMAIVGSSGSGKSTLLH-LLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnQKLGFI---YQFHHLLPDF 102
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAIR---AGIAMVpedRKRHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 103 TALENVAMPLLIGKKKPAEINSRALE--MLKAVGLEHRANHRP----SELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
Cdd:TIGR02633 355 GVGKNITLSVLKSFCFKMRIDAAAELqiIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 177 DARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAEL 227
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSdRVLVIGEGKLKGDF 485
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-224 |
4.57e-14 |
|
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: 71.13 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLH-LLGGLDTpTSGDVIFNGqpmSKLSSAAKAELRNQKLGFIYQF-HHLLPDF 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKG---SVAYVPQQAWIQNDSLRENILFgKALNEKY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 103 TALENVAMPLLIGkkkpaeinsraLEMLKAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
Cdd:TIGR00957 730 YQQVLEACALLPD-----------LEILPS-GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1600897103 183 SIFQ-LLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLT 224
Cdd:TIGR00957 798 HIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKIS 840
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-206 |
6.91e-14 |
|
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: 68.55 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSG---------DVI--FNGQPMSKLSsaakAELRNQKLGFIY--QFHHLLP 100
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdeFRGSELQNYF----TKLLEGDVKVIVkpQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 DftALENVAMPLLIGKKKPAEINsralEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
Cdd:cd03236 101 K--AVKGKVGELLKKKDERGKLD----ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*.
gi 1600897103 181 ADSIFQLLGELNRlQGTAFLVVTHDL 206
Cdd:cd03236 175 RLNAARLIRELAE-DDNYVLVVEHDL 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-221 |
7.09e-14 |
|
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: 70.20 E-value: 7.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmSKLSsaakaelrnqklgfiYQFHHLLPDF-----TALENV 108
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKIS---------------YKPQYISPDYdgtveEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 109 AMPLLIGKKKPAEInsralemLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA--R-NADSIF 185
Cdd:COG1245 426 NTDDFGSSYYKTEI-------IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqRlAVAKAI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1600897103 186 QLLGELNrlqGTAFLVVTHDLQL----AKRM-------------SRQLEMRDG 221
Cdd:COG1245 499 RRFAENR---GKTAMVVDHDIYLidyiSDRLmvfegepgvhghaSGPMDMREG 548
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-206 |
1.01e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 23 DVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP----------MSKLSSAAKAEL---RNQKL 89
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwRSKIGVVSQDPLlfsNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 GFIYQFHHLlPDFTALEN----------------------VAMPL-----------LIGKKKPAEI--NSRALEMLKAVG 134
Cdd:PTZ00265 479 NIKYSLYSL-KDLEALSNyynedgndsqenknkrnscrakCAGDLndmsnttdsneLIEMRKNYQTikDSEVVDVSKKVL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 135 LEHRANHRP-----------SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN----ADSIFQLLGELNRLQgtaf 199
Cdd:PTZ00265 558 IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylvQKTINNLKGNENRIT---- 633
|
....*..
gi 1600897103 200 LVVTHDL 206
Cdd:PTZ00265 634 IIIAHRL 640
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-224 |
1.26e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.59 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGG---LDtptSGDVIFNGQ-PMSKLS---------------SAAKAELR 85
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLD---DGRIIYEQDlIVARLQqdpprnvegtvydfvAEGIEEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQklgfIYQFHHLLPDftaLENVAMPLLIgkKKPAEI------------NSRALEMLKAVGLEhrANHRPSELSGGERQR 153
Cdd:PRK11147 96 EY----LKRYHDISHL---VETDPSEKNL--NELAKLqeqldhhnlwqlENRINEVLAQLGLD--PDAALSSLSGGWLRK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600897103 154 VAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGtAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLD---IETIEWLEGFLKTFQG-SIIFISHDRSFIRNMaTRIVDLDRGKLV 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-186 |
1.57e-13 |
|
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: 67.96 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLLPDfT 103
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLIGKkkpaeinSRALEMLKAVGLEHRANHRPSE-----------LSGGERQRVAIARALVNNPRLVLADEP 172
Cdd:cd03291 114 IKENIIFGVSYDE-------YRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170
....*....|....
gi 1600897103 173 TGNLDARNADSIFQ 186
Cdd:cd03291 187 FGYLDVFTEKEIFE 200
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
27-205 |
1.78e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.77 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 27 NVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNGQPMSKLSS----------------------AAKAE 83
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGKLRQdqfafeeftvldtvimghtelwEVKQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 84 lRNQklgfIYQfhhlLPDFTalENVAMPLLIGKKKPAEIN-----SRALEMLKAVGLEHRANHRP-SELSGGERQRVAIA 157
Cdd:PRK15064 99 -RDR----IYA----LPEMS--EEDGMKVADLEVKFAEMDgytaeARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1600897103 158 RALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTaFLVVTHD 205
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLD---INTIRWLEDVLNERNST-MIIISHD 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-218 |
2.37e-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: 68.89 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGSvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmSKLSSAAKAel 84
Cdd:TIGR01257 1937 ILRLNELTKVYSGTS--SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK--SILTNISDV-- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 rNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
Cdd:TIGR01257 2011 -HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 165 RLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLEM 218
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAI 2142
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-206 |
4.49e-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: 67.89 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD---------VI--FNGqpmSKLSSAAKAeLRNQKLGFIY--QFHHLLP 100
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdeVLkrFRG---TELQDYFKK-LANGEIKVAHkpQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 DftALENVAMPLLigkKKPAEiNSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR- 179
Cdd:COG1245 174 K--VFKGTVRELL---EKVDE-RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYq 247
|
170 180
....*....|....*....|....*....
gi 1600897103 180 --NADSIFQLLGELNRlqgtAFLVVTHDL 206
Cdd:COG1245 248 rlNVARLIRELAEEGK----YVLVVEHDL 272
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-228 |
5.41e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.63 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 28 VSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSkLSSAAKA---------ELRNQKlGFIyqfhhl 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSPRDAiragimlcpEDRKAE-GII------ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 99 lPDFTALENVAMP---------LLIGKKKPAEINSRALEMLKavgLEHRANHRP-SELSGGERQRVAIARALVNNPRLVL 168
Cdd:PRK11288 344 -PVHSVADNINISarrhhlragCLINNRWEAENADRFIRSLN---IKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVIL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 169 ADEPTGNLD--ARNadSIFQLLGELNRlQGTAFLVVTHDLQ----LAKRMsrqLEMRDGRLTAELS 228
Cdd:PRK11288 420 LDEPTRGIDvgAKH--EIYNVIYELAA-QGVAVLFVSSDLPevlgVADRI---VVMREGRIAGELA 479
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-207 |
9.12e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 3 KILLQCDNLCkrYQEGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngQPMSKLSSAAKA 82
Cdd:PRK11147 317 KIVFEMENVN--YQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 83 ELRNQklgfiyqfhhLLPDFTALENVAmplliGKKKPAEINSR---ALEMLKAVgLEH--RANHRPSELSGGERQRVAIA 157
Cdd:PRK11147 389 QHRAE----------LDPEKTVMDNLA-----EGKQEVMVNGRprhVLGYLQDF-LFHpkRAMTPVKALSGGERNRLLLA 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 158 RALVNNPRLVLADEPTGNLDARNadsiFQLLGEL-NRLQGTaFLVVTHDLQ 207
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVET----LELLEELlDSYQGT-VLLVSHDRQ 498
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-206 |
2.16e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD---------VI--FNGqpmSKLSSAAKaELRNQKLGFIY--QFHHLLP 100
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdeVLkrFRG---TELQNYFK-KLYNGEIKVVHkpQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 DftALENVAMPLLigkKKPAEiNSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
Cdd:PRK13409 174 K--VFKGKVRELL---KKVDE-RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180
....*....|....*....|....*.
gi 1600897103 181 ADSIFQLLGELnrLQGTAFLVVTHDL 206
Cdd:PRK13409 248 RLNVARLIREL--AEGKYVLVVEHDL 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-208 |
2.29e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmSKLSsaakaelrnqklgfiYQFHHLLPDFtaleNVAMPLL 113
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKIS---------------YKPQYIKPDY----DGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 114 IGKKKPAeINSRAL--EMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR---NADSIFQLL 188
Cdd:PRK13409 421 LRSITDD-LGSSYYksEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRI 499
|
170 180
....*....|....*....|
gi 1600897103 189 GELNrlqGTAFLVVTHDLQL 208
Cdd:PRK13409 500 AEER---EATALVVDHDIYM 516
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-204 |
2.84e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTP---TSGDVIFNGQPMSklSSAAKaelrnqKLGFIYQFHHLLP 100
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD--SSFQR------SIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 DFTALENVAMPLLIgkKKPAEI-----NSRALEMLKAVGLEHRANH---RPSE-LSGGERQRVAIARALVNNPRLVL-AD 170
Cdd:TIGR00956 850 TSTVRESLRFSAYL--RQPKSVsksekMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190
....*....|....*....|....*....|....
gi 1600897103 171 EPTGNLDARNADSIFQLLGELNRlQGTAFLVVTH 204
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIH 960
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-177 |
3.50e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 27 NVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMsklssaakaelrnqKLGFIYQFH-HLLPDFTAL 105
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------------KLAYVDQSRdALDPNKTVW 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 106 ENVAMPL---LIGKKkpaEINSRAL---------EMLKAVGlehranhrpsELSGGERQRVAIARALVNNPRLVLADEPT 173
Cdd:PRK11819 407 EEISGGLdiiKVGNR---EIPSRAYvgrfnfkggDQQKKVG----------VLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
....
gi 1600897103 174 GNLD 177
Cdd:PRK11819 474 NDLD 477
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-177 |
1.51e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 14 RYQEGsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmskLSSAAKAELRNQkLGFIY 93
Cdd:PTZ00243 1317 RYREG--LPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE---IGAYGLRELRRQ-FSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 94 QfHHLLPDFTALENVAmPLLigKKKPAEInSRALEML--------KAVGLEHRANHRPSELSGGERQRVAIARALVN-NP 164
Cdd:PTZ00243 1391 Q-DPVLFDGTVRQNVD-PFL--EASSAEV-WAALELVglrervasESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGS 1465
|
170
....*....|...
gi 1600897103 165 RLVLADEPTGNLD 177
Cdd:PTZ00243 1466 GFILMDEATANID 1478
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-231 |
5.75e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaaKAELRNqKLGFIYQFHHLLPDFTA 104
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSS--KEALEN-GISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENvampLLIG---KKKPAEINSRALEMLKAVGLEHRANHRPSE----LSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:PRK10982 91 MDN----MWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 178 ARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAELSLMG 231
Cdd:PRK10982 167 EKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITiLRDGQWIATQPLAG 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-226 |
6.30e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLH-LLGGLDTPTSGDVIFNGqpmsklsSAAKAElrnqKLGFIYqfhhllpDFT 103
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-------SVAYVP----QVSWIF-------NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVamplLIGKKKPAEINSRALEmlkAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNNPRLVLADEP 172
Cdd:PLN03232 695 VRENI----LFGSDFESERYWRAID---VTALQHDLDllpgrdlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 173 TGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-208 |
6.86e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 27 NVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqpmsklsSAAKAELRnqklgfIYQFHHLlpdfTALE 106
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF----------RSAKVRMA------VFSQHHV----DGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 107 NVAMPLL-IGKKKPAEINSRALEMLKAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSI 184
Cdd:PLN03073 587 LSSNPLLyMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDAV 663
|
170 180
....*....|....*....|....
gi 1600897103 185 FQLLGELNRLQGtAFLVVTHDLQL 208
Cdd:PLN03073 664 EALIQGLVLFQG-GVLMVSHDEHL 686
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-203 |
2.39e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 21 QTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKlgFIYQFHHLL- 99
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE--WQRNNTDMLs 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 100 --PDFTALeNVAMPLLIGKKKPAeinsRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:PRK10938 93 pgEDDTGR-TTAEIIQDEVKDPA----RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180
....*....|....*....|....*.
gi 1600897103 178 ARNADSIFQLLGELNRLQGTAFLVVT 203
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLN 193
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-226 |
5.36e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLH-LLGGLDTPTSGDVIFNGQP--MSKLSSAAKAELRNQKLgFIYQF----HH 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTVayVPQVSWIFNATVRDNIL-FGSPFdperYE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 98 LLPDFTALENvAMPLLIGKKKpAEINSRALEmlkavglehranhrpseLSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:PLN03130 712 RAIDVTALQH-DLDLLPGGDL-TEIGERGVN-----------------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 178 ARNADSIFQ--LLGElnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
Cdd:PLN03130 773 AHVGRQVFDkcIKDE---LRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-205 |
1.52e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrNQKLGFIYQFHHLLpDFT 103
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---------------NWQLAWVNQETPAL-PQP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENV------------------------AMPLLIGKKKPAE---INSRALEMLKAVGLEHRANHRP-SELSGGERQRVA 155
Cdd:PRK10636 80 ALEYVidgdreyrqleaqlhdanerndghAIATIHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1600897103 156 IARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAFLvVTHD 205
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLIL-ISHD 205
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-210 |
2.31e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.82 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmSKLSSAAKAELRNQklgfiyqfhhllpdFTA 104
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---SAALIAISSGLNGQ--------------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENVAMP-LLIG--KKKPAEINSRALEMLKaVGlehRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
Cdd:PRK13545 103 IENIELKgLMMGltKEKIKEIIPEIIEFAD-IG---KFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180 190
....*....|....*....|....*....|
gi 1600897103 181 ADSIFQLLGELNRlQGTAFLVVTHDLQLAK 210
Cdd:PRK13545 179 TKKCLDKMNEFKE-QGKTIFFISHSLSQVK 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-213 |
3.09e-09 |
|
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: 54.92 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 39 AIVGSSGSGKSTLLH-LLGGL--DTPTSGDvifNGQPMSKLssAAKAELRNQ-KLGFIYQF---HHLLPDFTALENVAMp 111
Cdd:cd03240 26 LIVGQNGAGKTTIIEaLKYALtgELPPNSK---GGAHDPKL--IREGEVRAQvKLAFENANgkkYTITRSLAILENVIF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 112 lligkKKPAEINSRALEMLKAvglehranhrpseLSGGERQ------RVAIARALVNNPRLVLADEPTGNLDARNAD-SI 184
Cdd:cd03240 100 -----CHQGESNWPLLDMRGR-------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSL 161
|
170 180
....*....|....*....|....*....
gi 1600897103 185 FQLLGELNRLQGTAFLVVTHDLQLAKRMS 213
Cdd:cd03240 162 AEIIEERKSQKNFQLIVITHDEELVDAAD 190
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-181 |
3.50e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.39 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTP--TSGDVIFNGQPmsklssaAKAELRNQKLGFIYQFHHLLPD 101
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFP-------KKQETFARISGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 FTALENVA------MPLLIGKKKPAEINSRALEMLKAVGLEHRANHRP--SELSGGERQRVAIARALVNNPRLVLADEPT 173
Cdd:PLN03140 968 VTVRESLIysaflrLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
....*...
gi 1600897103 174 GNLDARNA 181
Cdd:PLN03140 1048 SGLDARAA 1055
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-211 |
3.90e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.21 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpMSKLssAAKAELRNQklgfiyqfhhllpdFTA 104
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVI--AISAGLSGQ--------------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENVAMPLLIGKKKPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180
....*....|....*....|....*..
gi 1600897103 185 FQLLGELNRLQGTAFLvVTHDLQLAKR 211
Cdd:PRK13546 183 LDKIYEFKEQNKTIFF-VSHNLGQVRQ 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-218 |
4.32e-09 |
|
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: 54.25 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLhlLGGLdtptsgdvifngqpmsklssAAKAELRNQKLgfiyqfhhlLPDFTA 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGL--------------------YASGKARLISF---------LPKFSR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 105 LENVAmpllIGKkkpaeinsraLEMLKAVGLEHRANHRP-SELSGGERQRVAIARALVNNPR--LVLADEPTGNLDARNa 181
Cdd:cd03238 60 NKLIF----IDQ----------LQFLIDVGLGYLTLGQKlSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD- 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 1600897103 182 dsIFQLLGELNRL--QGTAFLVVTHDLQLAKRMSRQLEM 218
Cdd:cd03238 125 --INQLLEVIKGLidLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-208 |
4.48e-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: 54.96 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLlhllggldtptSGDVIF-NGQP--MSKLSSAAKaelrnqklgfiyQFHHLL-- 99
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL-----------AFDTIYaEGQRryVESLSAYAR------------QFLGQMdk 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 100 PDFTALENVAMPLLIGKKKPA-----------EINS------------RALEMLKAVGLEHRANHRPSE-LSGGERQRVA 155
Cdd:cd03270 68 PDVDSIEGLSPAIAIDQKTTSrnprstvgtvtEIYDylrllfarvgirERLGFLVDVGLGYLTLSRSAPtLSGGEAQRIR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 156 IARALVNNPRLVL--ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQL 208
Cdd:cd03270 148 LATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDT 201
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-219 |
6.20e-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: 53.52 E-value: 6.20e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600897103 146 LSGGERQRVAIARALVN---NPR-LVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMR 219
Cdd:cd03227 78 LSGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEH-LVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-222 |
6.57e-09 |
|
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: 55.53 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 23 DVLHN-VSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLdTPtsgdvIFNGqpmsKLSSAAKaelrnQKLGFIYQfhhlLPD 101
Cdd:TIGR00954 465 DVLIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WP-----VYGG----RLTKPAK-----GKLFYVPQ----RPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 F---TALENVAMPLLIGKKKPAEINSRALE-MLKAVGLEHRANHRPS---------ELSGGERQRVAIARALVNNPRLVL 168
Cdd:TIGR00954 526 MtlgTLRDQIIYPDSSEDMKRRGLSDKDLEqILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1600897103 169 ADEPTGNLDARNADSIFQLLGELnrlqGTAFLVVTHDLQLAKRMSRQLEMrDGR 222
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCREF----GITLFSVSHRKSLWKYHEYLLYM-DGR 654
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-208 |
6.65e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsklsSAAKAelrnQKLGFI--YQFHHLLPD 101
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----------GLAKG----IKLGYFaqHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 FTALENVAmplligKKKPAEINSRALEMLKAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTG--NLDA 178
Cdd:PRK10636 392 ESPLQHLA------RLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNhlDLDM 465
|
170 180 190
....*....|....*....|....*....|
gi 1600897103 179 RNAdsifqLLGELNRLQGtAFLVVTHDLQL 208
Cdd:PRK10636 466 RQA-----LTEALIDFEG-ALVVVSHDRHL 489
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-223 |
7.19e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDViFNGQPMSKLSSAA---KAELRNQKLGFIYQFHHLLP 100
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPQQAwimNATVRGNILFFDEEDAARLA 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 101 DFTALENVamplligkkkpaEINSRALemlkAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
Cdd:PTZ00243 754 DAVRVSQL------------EADLAQL----GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1600897103 181 ADSIFQ--LLGelnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
Cdd:PTZ00243 818 GERVVEecFLG---ALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-226 |
7.98e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 FTALENVAMpllIGKK---KPAEINSRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
Cdd:NF000106 101 FSGRENLYM---IGR*ldlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1600897103 179 RNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLEMRD-GRLTAE 226
Cdd:NF000106 178 RTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDrGRVIAD 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-173 |
1.01e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 14 RYqeGSVQtdVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklSSAAKAELRN------Q 87
Cdd:NF033858 10 RY--GKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPriaympQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 88 KLGfiyqfHHLLPDFTALENVA-MPLLIGKKKpAEINSRALEMLKAVGLEHRANhRPS-ELSGGERQRVAIARALVNNPR 165
Cdd:NF033858 84 GLG-----KNLYPTLSVFENLDfFGRLFGQDA-AERRRRIDELLRATGLAPFAD-RPAgKLSGGMKQKLGLCCALIHDPD 156
|
....*...
gi 1600897103 166 LVLADEPT 173
Cdd:NF033858 157 LLILDEPT 164
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-204 |
1.52e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGlDTPT--SGDVIFNGQpmsKLSSAAKAELRNQKLGFIYQFHHLlpD 101
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTLFGR---RRGSGETIWDIKKHIGYVSSSLHL--D 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 F---TALENVampLLIG--------KKKPAEINSRALEMLKAVGLEHR-ANHRPSELSGGERQRVAIARALVNNPRLVLA 169
Cdd:PRK10938 349 YrvsTSVRNV---ILSGffdsigiyQAVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLIL 425
|
170 180 190
....*....|....*....|....*....|....*
gi 1600897103 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
Cdd:PRK10938 426 DEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-184 |
2.40e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGsvqTD-VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqK 88
Cdd:TIGR00957 1289 NYCLRYRED---LDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLRF-K 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 89 LGFIYQFHHLlpdFTAleNVAMPLLIGKKKPAEINSRALEM--LKAV------GLEHRANHRPSELSGGERQRVAIARAL 160
Cdd:TIGR00957 1362 ITIIPQDPVL---FSG--SLRMNLDPFSQYSDEEVWWALELahLKTFvsalpdKLDHECAEGGENLSVGQRQLVCLARAL 1436
|
170 180
....*....|....*....|....
gi 1600897103 161 VNNPRLVLADEPTGNLDARNADSI 184
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLI 1460
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-221 |
2.43e-08 |
|
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: 52.19 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 32 VGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSgdvifngqpmsklssaakaelrnqklgfiyqfhhllpdftalENVAMP 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG------------------------------------------DNDEWD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 112 LLIGKKKPAEInsralemlkavglehranhrpsELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL 191
Cdd:cd03222 60 GITPVYKPQYI----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|
gi 1600897103 192 NRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-224 |
3.03e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 6 LQCDNLCKRYQEGSVqtdvLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsKLSSaakaelr 85
Cdd:PRK15064 320 LEVENLTKGFDNGPL----FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSE------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 86 NQKLGFIYQFHHllPDFTALENVaMPLLIGKKKPA--EINSRAL--EMLKAvglEHRANHRPSELSGGERQRVAIARALV 161
Cdd:PRK15064 381 NANIGYYAQDHA--YDFENDLTL-FDWMSQWRQEGddEQAVRGTlgRLLFS---QDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 162 NNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTaFLVVTHDLQ----LAKRMsrqLEMRDGRLT 224
Cdd:PRK15064 455 QKPNVLVMDEPTNHMD---MESIESLNMALEKYEGT-LIFVSHDREfvssLATRI---IEITPDGVV 514
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-211 |
4.03e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPMSKLSSAAKAEL-RNQKLGF--IYQFHHLL 99
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMTNEQDYQGdEEQNVGMknVNEFSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 100 P-----DFTALENVAMPLLIG------------------KKKPAEIN-------------------SRAL------EMLK 131
Cdd:PTZ00265 1263 EggsgeDSTVFKNSGKILLDGvdicdynlkdlrnlfsivSQEPMLFNmsiyenikfgkedatredvKRACkfaaidEFIE 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 132 AVGLEHRANHRP--SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
Cdd:PTZ00265 1343 SLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
..
gi 1600897103 210 KR 211
Cdd:PTZ00265 1423 KR 1424
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
124-210 |
4.44e-08 |
|
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: 53.09 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 124 SRALEMLKAVGLEHRANHRPS-ELSGGERQRVAIARAL---VNNPRLVLADEPTGNLdarNADSIFQLLGELNRL--QGT 197
Cdd:TIGR00630 807 SRKLQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGL---HFDDIKKLLEVLQRLvdKGN 883
|
90
....*....|...
gi 1600897103 198 AFLVVTHDLQLAK 210
Cdd:TIGR00630 884 TVVVIEHNLDVIK 896
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-186 |
6.05e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQFHHL----- 98
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRK-VLGIIPQAPVLfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 99 ---LPDFT---------ALENVAMPLLIGKkkpaeiNSRALEMLKAVGLEHranhrpseLSGGERQRVAIARALVNNPRL 166
Cdd:PLN03130 1330 rfnLDPFNehndadlweSLERAHLKDVIRR------NSLGLDAEVSEAGEN--------FSVGQRQLLSLARALLRRSKI 1395
|
170 180
....*....|....*....|
gi 1600897103 167 VLADEPTGNLDARnADSIFQ 186
Cdd:PLN03130 1396 LVLDEATAAVDVR-TDALIQ 1414
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
124-210 |
9.20e-08 |
|
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: 51.46 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 124 SRALEMLKAVGLEHRANHRPS-ELSGGERQRVAIARALVN---NPRLVLADEPTGNLdarNADSIFQLLGELNRL--QGT 197
Cdd:cd03271 147 ARKLQTLCDVGLGYIKLGQPAtTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGL---HFHDVKKLLEVLQRLvdKGN 223
|
90
....*....|...
gi 1600897103 198 AFLVVTHDLQLAK 210
Cdd:cd03271 224 TVVVIEHNLDVIK 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
10-177 |
1.46e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 51.01 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGSvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSK--LSSAAKA-ELRN 86
Cdd:cd03289 7 DLTAKYTEGG--NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSvpLQKWRKAfGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 87 QKLgFIYQ--FHHLLPDFtalenvamplliGKKKPAEINSRALEmlkaVGLEHRANHRPSE-----------LSGGERQR 153
Cdd:cd03289 84 QKV-FIFSgtFRKNLDPY------------GKWSDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQL 146
|
170 180
....*....|....*....|....
gi 1600897103 154 VAIARALVNNPRLVLADEPTGNLD 177
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLD 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-224 |
1.70e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKAeLRNqklGF-----------IY 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI-NNHNANEA-INH---GFalvteerrstgIY 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 94 -----QFHHLLPDFTALENvAMPLLIGKKKPAEINsRALEMLKAVGLEHRANhrPSELSGGERQRVAIARALVNNPRLVL 168
Cdd:PRK10982 339 ayldiGFNSLISNIRNYKN-KVGLLDNSRMKSDTQ-WVIDSMRVKTPGHRTQ--IGSLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1600897103 169 ADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLT 224
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMpELLGITDRILVMSNGLVA 470
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-222 |
2.09e-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: 48.91 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 35 GEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFngqpmsklssaakaelrnqklgfiyqfhhllpdftalenvamplli 114
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 115 gkkkpaeIN-SRALEMLKAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL-----L 188
Cdd:smart00382 36 -------IDgEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1600897103 189 GELNRLQGTAFLVVTHDLQLAKRM------SRQLEMRDGR 222
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPAllrrrfDRRIVLLLIL 148
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-181 |
3.02e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 19 SVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLG----GLDTPTSGDVIFNGQPmsklssaaKAELRNQKLG-FIY 93
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGIT--------PEEIKKHYRGdVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 94 ------QFHHLLPDFTaLENVAM-------PLLIGKKkpAEINSRALEMLKAVGLEHRANHRPSE-----LSGGERQRVA 155
Cdd:TIGR00956 143 naetdvHFPHLTVGET-LDFAARcktpqnrPDGVSRE--EYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVS 219
|
170 180
....*....|....*....|....*.
gi 1600897103 156 IARALVNNPRLVLADEPTGNLDARNA 181
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATA 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-206 |
4.47e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 5 LLQCDNLCKRYQEGsvQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAEL 84
Cdd:PLN03232 1234 SIKFEDVHLRYRPG--LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDL 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RnQKLGFIYQFHHL--------LPDFTALENVAMPLLIGKKKPAEINSRalemlKAVGLEHRANHRPSELSGGERQRVAI 156
Cdd:PLN03232 1309 R-RVLSIIPQSPVLfsgtvrfnIDPFSEHNDADLWEALERAHIKDVIDR-----NPFGLDAEVSEGGENFSVGQRQLLSL 1382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1600897103 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDL 206
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRL 1430
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
25-188 |
1.07e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 25 LHNVSFSVGEGEMMA------------IVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaelrnQKLGFI 92
Cdd:PRK13541 4 LHQLQFNIEQKNLFDlsitflpsaityIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI----------AKPYCT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 93 YQFHHL--LPDFTALENVAMplligkkkPAEINSRALEMLKAV---GLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
Cdd:PRK13541 74 YIGHNLglKLEMTVFENLKF--------WSEIYNSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLW 145
|
170 180
....*....|....*....|.
gi 1600897103 168 LADEPTGNLDARNADSIFQLL 188
Cdd:PRK13541 146 LLDEVETNLSKENRDLLNNLI 166
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-204 |
1.40e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 22 TDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLD--TPTSGDVIFNGQPMSKLSSAAKA---------------EL 84
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAgegifmafqypveipGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 85 RNQ-----KLGFIYQFHHLLP----DFTALENVAMPLLigkKKPAEINSRALEmlkaVGlehranhrpseLSGGERQRVA 155
Cdd:PRK09580 94 SNQfflqtALNAVRSYRGQEPldrfDFQDLMEEKIALL---KMPEDLLTRSVN----VG-----------FSGGEKKRND 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1600897103 156 IARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQG--TAFLVVTH 204
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLD---IDALKIVADGVNSLRDgkRSFIIVTH 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-177 |
2.82e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 23 DVLHNVSFSVGEGEMMAIVGSSGSGKSTLL-----HLLGGLdtPTSGDVI-----FNGQPMSKLSSAAKAELRNQKL--- 89
Cdd:PLN03073 191 DLIVDASVTLAFGRHYGLVGRNGTGKTTFLrymamHAIDGI--PKNCQILhveqeVVGDDTTALQCVLNTDIERTQLlee 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 -GFIYQFHHLLPDFTALENVAMPLLIGKKKPA------EINSRaLEMLKAVGLEHRA--------------NHRPSELSG 148
Cdd:PLN03073 269 eAQLVAQQRELEFETETGKGKGANKDGVDKDAvsqrleEIYKR-LELIDAYTAEARAasilaglsftpemqVKATKTFSG 347
|
170 180
....*....|....*....|....*....
gi 1600897103 149 GERQRVAIARALVNNPRLVLADEPTGNLD 177
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-177 |
3.42e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.60 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 10 NLCKRYQEGSvqTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTpTSGDVIFNGQPMSKLSsaakAELRNQKL 89
Cdd:TIGR01271 1222 GLTAKYTEAG--RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVT----LQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 90 GFIYQFHHLLPDfTALENVamplligkkKPAEINSRAlEMLKA---VGLEHRANHRPSE-----------LSGGERQRVA 155
Cdd:TIGR01271 1295 GVIPQKVFIFSG-TFRKNL---------DPYEQWSDE-EIWKVaeeVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMC 1363
|
170 180
....*....|....*....|..
gi 1600897103 156 IARALVNNPRLVLADEPTGNLD 177
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLD 1385
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
113-207 |
3.57e-06 |
|
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: 47.32 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 113 LIGKKKPAEINSRaLEMLKAVGLEHRANHRPSE-LSGGERQRVAIARALvnNPRLV----LADEPTGNLDARNADsifQL 187
Cdd:TIGR00630 456 KIAEEVLKEIRER-LGFLIDVGLDYLSLSRAAGtLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHQRDNR---RL 529
|
90 100
....*....|....*....|..
gi 1600897103 188 LGELNRL--QGTAFLVVTHDLQ 207
Cdd:TIGR00630 530 INTLKRLrdLGNTLIVVEHDED 551
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-228 |
8.18e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTL-LHLLG---GldTPTSGDVIFNGQPMSkLSSAAKA---------ELRNQkLG 90
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrsyG--RNISGTVFKDGKEVD-VSTVSDAidaglayvtEDRKG-YG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 91 FIyqfhhlLPDfTALENVAMPLLIGKKKPAEINSRAlEMLKAVGLEHRANHR-PS------ELSGGERQRVAIARALVNN 163
Cdd:NF040905 351 LN------LID-DIKRNITLANLGKVSRRGVIDENE-EIKVAEEYRKKMNIKtPSvfqkvgNLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 164 PRLVLADEPTGNLD--ARnadsiFQLLGELNRL--QGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
Cdd:NF040905 423 PDVLILDEPTRGIDvgAK-----YEIYTIINELaaEGKGVIVISSELPELLGMCdRIYVMNEGRITGELP 487
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-218 |
8.29e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 127 LEMLKAVGLEHRANHRP-SELSGGERQRVAIARALVN---NPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVV 202
Cdd:PRK00635 790 IHALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVII 868
|
90
....*....|....*.
gi 1600897103 203 THDLQLAKRMSRQLEM 218
Cdd:PRK00635 869 EHNMHVVKVADYVLEL 884
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
24-210 |
9.11e-06 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 45.05 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 24 VLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfnGQPMSKLSSAAKAelrnqklgfiyqfhHLLPDFT 103
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFI--GLRGDALPLGANS--------------FILPGLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 104 ALENVAMPLLIGKKKPAEINSRALEMLKavgLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDarNADS 183
Cdd:PRK15177 66 GEENARMMASLYGLDGDEFSHFCYQLTQ---LEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGD--NATQ 140
|
170 180
....*....|....*....|....*..
gi 1600897103 184 IFQLLGELNRLQGTAFLVVTHDLQLAK 210
Cdd:PRK15177 141 LRMQAALACQLQQKGLIVLTHNPRLIK 167
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
122-208 |
6.96e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 122 INSRaLEMLKAVGLEHRANHRP-SELSGGERQRVAIARAL---VNNPRLVLaDEPTGNLDARNADSIFQLLGELnRLQGT 197
Cdd:PRK00635 453 LKSR-LSILIDLGLPYLTPERAlATLSGGEQERTALAKHLgaeLIGITYIL-DEPSIGLHPQDTHKLINVIKKL-RDQGN 529
|
90
....*....|.
gi 1600897103 198 AFLVVTHDLQL 208
Cdd:PRK00635 530 TVLLVEHDEQM 540
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
125-206 |
1.22e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 125 RALEMLKAVGLE-----HRANhrpsELSGGERQRVAIARALV---NNPRLVLADEPTGNLdarNADSIFQLLGELNRL-- 194
Cdd:COG0178 805 RKLQTLQDVGLGyiklgQPAT----TLSGGEAQRVKLASELSkrsTGKTLYILDEPTTGL---HFHDIRKLLEVLHRLvd 877
|
90
....*....|..
gi 1600897103 195 QGTAFLVVTHDL 206
Cdd:COG0178 878 KGNTVVVIEHNL 889
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
39-206 |
1.26e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 39 AIVGSSGSGKSTLLH----LLGGldtPTSGDVIFNGQPMSKLSSAAKAEL------------RNQklGFIYQFHHLLPD- 101
Cdd:COG0419 27 LIVGPNGAGKSTILEairyALYG---KARSRSKLRSDLINVGSEEASVELefehggkryrieRRQ--GEFAEFLEAKPSe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 102 -FTALENV--AMPLLIGKKKPAEINSRALEMLKAVGLEHRANHR----------PSELSGGERQRVAIARALvnnpRLVL 168
Cdd:COG0419 102 rKEALKRLlgLEIYEELKERLKELEEALESALEELAELQKLKQEilaqlsgldpIETLSGGERLRLALADLL----SLIL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1600897103 169 aDepTGNLDARNADSIFQLLGELNrlqgtaflVVTHDL 206
Cdd:COG0419 178 -D--FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
127-188 |
1.29e-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: 39.53 E-value: 1.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600897103 127 LEMLKAVGLEHRANHRPSELSGGERQR---VAIARALV----------NNPRLVLADEPTGNLDARNADSIFQLL 188
Cdd:pfam13558 14 VEVRDEDGSEVETYRRSGGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-205 |
1.61e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 121 EINSRaLEMLKAVGLEHRANHRPSE-LSGGERQRV----AIARALVNnprlVL--ADEPTGNLDARNADsifQLLGELNR 193
Cdd:COG0178 461 EIRSR-LGFLVDVGLDYLTLDRSAGtLSGGEAQRIrlatQIGSGLVG----VLyvLDEPSIGLHQRDND---RLIETLKR 532
|
90
....*....|....
gi 1600897103 194 L--QGTAFLVVTHD 205
Cdd:COG0178 533 LrdLGNTVIVVEHD 546
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
153-214 |
2.57e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1600897103 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL--NRLQGTAF--LVVTHDLQLAKRMSR 214
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIikSRSQQRNFqlLVITHDEDFVELLGR 1278
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
121-205 |
5.14e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 121 EINSRaLEMLKAVGLEHRANHRPSE-LSGGERQRVaiaralvnnpRL-------------VLaDEPTGNLDARNADsifQ 186
Cdd:PRK00349 465 EIRER-LKFLVDVGLDYLTLSRSAGtLSGGEAQRI----------RLatqigsgltgvlyVL-DEPSIGLHQRDND---R 529
|
90 100
....*....|....*....|.
gi 1600897103 187 LLGELNRLQ--GTAFLVVTHD 205
Cdd:PRK00349 530 LIETLKHLRdlGNTLIVVEHD 550
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
26-69 |
1.91e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 1.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1600897103 26 HNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPtSGDVIFN 69
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP-AKRARFN 55
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
142-217 |
7.52e-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: 36.48 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600897103 142 RP-SELSGGERQRVAIARAL--------VNNPRL--VLADEPTGNLDARN---ADSIFQLLGELNRLQGtaflVVTHDLQ 207
Cdd:cd03279 119 RPvSTLSGGETFLASLSLALalsevlqnRGGARLeaLFIDEGFGTLDPEAleaVATALELIRTENRMVG----VISHVEE 194
|
90
....*....|
gi 1600897103 208 LAKRMSRQLE 217
Cdd:cd03279 195 LKERIPQRLE 204
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
39-66 |
9.29e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 35.39 E-value: 9.29e-03
10 20
....*....|....*....|....*...
gi 1600897103 39 AIVGSSGSGKSTLLHLLGGLDTPTSGDV 66
Cdd:cd11383 1 GLMGKTGAGKSSLCNALFGTEVAAVGDR 28
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
39-66 |
9.75e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.22 E-value: 9.75e-03
10 20
....*....|....*....|....*....
gi 1600897103 39 AIVGSSGSGKSTLL-HLLGGLDTPTsGDV 66
Cdd:cd01854 89 VLVGQSGVGKSTLLnALLPELVLAT-GEI 116
|
|
| |
