|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
2-281 |
1.01e-170 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 480.44 E-value: 1.01e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 2 SEAPVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAAR 81
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 82 ADRHAEIAHQMLAAGHAYKCYASQDEITAFREAARAEGKSTLYQSPWRDADPATH-----PDAPYVVRLKAPRDGaTVIP 156
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELermlaAGEPPVLRFKIPEEG-VVFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 157 DRVQGDVTWKNDQLDDMVLLRSDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIPLIHGP 236
Cdd:COG0008 160 DLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGP 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2795819396 237 DGKKLSKRHGALGVGEYQAMGYPAAAMRNYLARLGWSHGND-EFFT 281
Cdd:COG0008 240 DGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDqEIFS 285
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
5-281 |
1.59e-135 |
|
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 391.33 E-value: 1.59e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 5 PVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAARADR 84
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 85 HAEIAHQMLAAGHAYKCYASQDEITAFREAARAEGKSTLYQSPWRD--ADPATHPDA---PYVVRLKAPRDGATVIPDRV 159
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNlhEEEIENKLAkgiPPVVRFKIPQEAVVSFNDQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 160 QGDVTWKNDQLDDMVLLRSDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIPLIHGPDGK 239
Cdd:TIGR00464 161 RGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2795819396 240 KLSKRHGALGVGEYQAMGYPAAAMRNYLARLGWSHGND-EFFT 281
Cdd:TIGR00464 241 KLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDqEFFS 283
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-281 |
9.43e-118 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 348.27 E-value: 9.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 2 SEAPVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWD------GE- 74
Cdd:PLN02627 42 KGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdvgGEy 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 75 -PISQAARADRHAEIAHQMLAAGHAYKCYASQDEITAFREAARAEGKSTLYQSPWRDADPATHPDA-----PYVVRLKAP 148
Cdd:PLN02627 122 gPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAElakgtPYTYRFRVP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 149 RDGATVIPDRVQGDVTWKNDQLDDMVLLRSDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFA 228
Cdd:PLN02627 202 KEGSVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFA 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2795819396 229 HIPLIHGPDGKKLSKRHGALGVGEYQAMGYPAAAMRNYLARLGWSHGND-EFFT 281
Cdd:PLN02627 282 HVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTEnEIFT 335
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
5-281 |
1.43e-108 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 316.95 E-value: 1.43e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 5 PVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAARADR 84
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 85 HAEIAHQMLAAGHAYKCYASQDEITAFREAARAEGkstlyqSPWRD-------------ADPATHPDAPYVVRLKAPRDG 151
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEALG------SPSRDrydeenlhlfeeeMKKGSAEGGPATVRAKIPMES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 152 ATVIPDRVQGDVTWKNDQLDDMVLLRSDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIP 231
Cdd:pfam00749 155 PYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEY 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2795819396 232 LIHGPDGKKLSKRHGALGV--GEYQAMGYPAAAMRNYLARLGWS-HGNDEFFT 281
Cdd:pfam00749 235 LRLNLDGTKLSKRKLSWSVdiSQVKGWGDPREATLNGLRRRGWTpEGIREFFT 287
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
6-281 |
6.16e-104 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 302.58 E-value: 6.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDG--------EPIS 77
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 78 QAARADRHAEIAHQMLAAGhaykcyasqdeitafreaaraegkstlyqspwrdadpathpdapyvvrlkaprdgatvipd 157
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 158 rvqgdvtwkndqlddmvllrsDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIPLIHGPD 237
Cdd:cd00808 101 ---------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPD 159
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2795819396 238 GKKLSKRHGALGVGEYQAMGYPAAAMRNYLARLGWSHGND-EFFT 281
Cdd:cd00808 160 GKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGeEFFT 204
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
2-281 |
1.01e-170 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 480.44 E-value: 1.01e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 2 SEAPVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAAR 81
Cdd:COG0008 1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 82 ADRHAEIAHQMLAAGHAYKCYASQDEITAFREAARAEGKSTLYQSPWRDADPATH-----PDAPYVVRLKAPRDGaTVIP 156
Cdd:COG0008 81 FDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYDGRCRDLSPEELermlaAGEPPVLRFKIPEEG-VVFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 157 DRVQGDVTWKNDQLDDMVLLRSDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIPLIHGP 236
Cdd:COG0008 160 DLVRGEITFPNPNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGP 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2795819396 237 DGKKLSKRHGALGVGEYQAMGYPAAAMRNYLARLGWSHGND-EFFT 281
Cdd:COG0008 240 DGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDqEIFS 285
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
5-281 |
1.59e-135 |
|
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273092 [Multi-domain] Cd Length: 470 Bit Score: 391.33 E-value: 1.59e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 5 PVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAARADR 84
Cdd:TIGR00464 1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 85 HAEIAHQMLAAGHAYKCYASQDEITAFREAARAEGKSTLYQSPWRD--ADPATHPDA---PYVVRLKAPRDGATVIPDRV 159
Cdd:TIGR00464 81 YKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGRCRNlhEEEIENKLAkgiPPVVRFKIPQEAVVSFNDQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 160 QGDVTWKNDQLDDMVLLRSDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIPLIHGPDGK 239
Cdd:TIGR00464 161 RGEITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2795819396 240 KLSKRHGALGVGEYQAMGYPAAAMRNYLARLGWSHGND-EFFT 281
Cdd:TIGR00464 241 KLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDqEFFS 283
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
2-281 |
9.43e-118 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 348.27 E-value: 9.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 2 SEAPVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWD------GE- 74
Cdd:PLN02627 42 KGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdvgGEy 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 75 -PISQAARADRHAEIAHQMLAAGHAYKCYASQDEITAFREAARAEGKSTLYQSPWRDADPATHPDA-----PYVVRLKAP 148
Cdd:PLN02627 122 gPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPRYTGKWATASDEEVQAElakgtPYTYRFRVP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 149 RDGATVIPDRVQGDVTWKNDQLDDMVLLRSDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFA 228
Cdd:PLN02627 202 KEGSVKIDDLIRGEVSWNTDTLGDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFA 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2795819396 229 HIPLIHGPDGKKLSKRHGALGVGEYQAMGYPAAAMRNYLARLGWSHGND-EFFT 281
Cdd:PLN02627 282 HVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWNDGTEnEIFT 335
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
5-281 |
1.43e-108 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 316.95 E-value: 1.43e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 5 PVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAARADR 84
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 85 HAEIAHQMLAAGHAYKCYASQDEITAFREAARAEGkstlyqSPWRD-------------ADPATHPDAPYVVRLKAPRDG 151
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEQEALG------SPSRDrydeenlhlfeeeMKKGSAEGGPATVRAKIPMES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 152 ATVIPDRVQGDVTWKNDQLDDMVLLRSDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIP 231
Cdd:pfam00749 155 PYVFRDPVRGRIKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEY 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2795819396 232 LIHGPDGKKLSKRHGALGV--GEYQAMGYPAAAMRNYLARLGWS-HGNDEFFT 281
Cdd:pfam00749 235 LRLNLDGTKLSKRKLSWSVdiSQVKGWGDPREATLNGLRRRGWTpEGIREFFT 287
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
6-281 |
6.16e-104 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 302.58 E-value: 6.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDG--------EPIS 77
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEgpdvggpyGPYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 78 QAARADRHAEIAHQMLAAGhaykcyasqdeitafreaaraegkstlyqspwrdadpathpdapyvvrlkaprdgatvipd 157
Cdd:cd00808 82 QSERLEIYRKYAEKLLEKG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 158 rvqgdvtwkndqlddmvllrsDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIPLIHGPD 237
Cdd:cd00808 101 ---------------------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPD 159
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2795819396 238 GKKLSKRHGALGVGEYQAMGYPAAAMRNYLARLGWSHGND-EFFT 281
Cdd:cd00808 160 GKKLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGeEFFT 204
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
1-273 |
1.33e-86 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 260.55 E-value: 1.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 1 MSEAPVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAA 80
Cdd:PRK05710 1 MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 81 RADRHAEIAHQMLAAGHAYKCYASQDEITAFREAARAEGksTLYqsPWRDADPATHPDAPYVVRLKAPrDGATVIPDRVQ 160
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCSRKEIAAAAPAPPDGG--GIY--PGTCRDLLHGPRNPPAWRLRVP-DAVIAFDDRLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 161 GDVT-WKNDQLDDMVLLRSDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIPLIHGPDGK 239
Cdd:PRK05710 156 GRQHqDLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQ 235
|
250 260 270
....*....|....*....|....*....|....
gi 2795819396 240 KLSKRHGALGVGEyqamGYPAAAMRNYLARLGWS 273
Cdd:PRK05710 236 KLSKQNGAPALDA----AGPLPVLAAALRFLGQP 265
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
6-264 |
2.14e-79 |
|
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ligase, but its purpose is to modify tRNA(Asp) at a queuosine position in the anticodon rather than to charge a tRNA with its cognate amino acid. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274810 Cd Length: 271 Bit Score: 241.29 E-value: 2.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAARADRH 85
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 86 AEIAHQMLAAGHAYKCYASQDEItafreaARAEGKSTLYQSPWRDADPAtHPDAPYVVRLKAPrDGATVIPDRVQGDVTW 165
Cdd:TIGR03838 81 QAALDRLLAAGLAYPCQCTRKEI------AAARDGGGIYPGTCRNGLPG-RPGRPAAWRLRVP-DGVIAFDDRLQGPQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 166 KNDQ-LDDMVLLRSDGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIPLIHGPDGKKLSKR 244
Cdd:TIGR03838 153 DLAAaVGDFVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQ 232
|
250 260
....*....|....*....|
gi 2795819396 245 HGALGVGEYQAMGYPAAAMR 264
Cdd:TIGR03838 233 NGAPALDDSRPLPALLAALR 252
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
6-282 |
4.08e-72 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 221.19 E-value: 4.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAARADRH 85
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 86 AEIAHQMLAAGhaykcyasqdeitafreaaraegkstlyqspwrdadpathpdapyvvrlkaprdgatvipdrvqgdvtw 165
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 166 kndqlddmvllrsdGTPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIPLIHGPDGKKLSKRH 245
Cdd:cd00418 93 --------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKLSKRK 158
|
250 260 270
....*....|....*....|....*....|....*....
gi 2795819396 246 GALGVGEYQAMGYPAAAMRNYLARLGWSH--GNDEFFTD 282
Cdd:cd00418 159 LNTTLRALRRRGYLPEALRNYLALIGWSKpdGHELFTLE 197
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
6-243 |
9.53e-50 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 172.34 E-value: 9.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTD--RARSTPEATEAILTGLRWLGLDWDgEPISQAARAD 83
Cdd:PRK04156 102 VVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLGVKWD-EVVIQSDRLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 84 RHAEIAHQMLAAGHAYKCYASQDEITAFREAARAegkstlyqSPWRDADPATH------------PDAPYVVRLKAprdg 151
Cdd:PRK04156 181 IYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKP--------CPHRDKSPEENlelwekmldgeyKEGEAVVRVKT---- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 152 atvipdrvqgDVTWKNDQLDDMVLLRSDGT------------PTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHA 219
Cdd:PRK04156 249 ----------DLEHPNPSVRDWVAFRIVKTphprvgdkyrvwPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDY 318
|
250 260
....*....|....*....|....*.
gi 2795819396 220 MGWDLPVFAH--IPLIHGPdgkKLSK 243
Cdd:PRK04156 319 FGWEYPETIHygRLKIEGF---VLST 341
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
6-229 |
6.65e-43 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 153.83 E-value: 6.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDgEPISQAARADRH 85
Cdd:TIGR00463 94 VVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-EVVYQSDRIETY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 86 AEIAHQMLAAGHAYKCYASQDEITAFR---EAARAEGKS---TLyqSPWRDADPATHPDAPYVVRLKAprdgatvipdrv 159
Cdd:TIGR00463 173 YDYTRKLIEMGKAYVCDCRPEEFRELRnrgEACHCRDRSveeNL--ERWEEMLEGKEEGGSVVVRVKT------------ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 160 qgDVTWKNDQLDDMVLLRSDGT------------PTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVF 227
Cdd:TIGR00463 239 --DLKHKNPAIRDWVIFRIVKTphprtgdkyrvyPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEF 316
|
..
gi 2795819396 228 AH 229
Cdd:TIGR00463 317 IH 318
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
5-271 |
1.70e-37 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 132.47 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 5 PVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTD--RARSTPEATEAILTGLRWLGLDWDgEPISQAARA 82
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDprTKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 83 DRHAEIAHQMLAAGHAYkcyasqdeitafreaaraegkstlyqspwrdadpaTHPDA--PYVVrlkaprdgatvipdrvq 160
Cdd:cd09287 80 ELYYEYARKLIEMGGAY-----------------------------------VHPRTgsKYRV----------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 161 gdvtWkndqlddmvllrsdgtPTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDLPVFAHIPLIHGPDGK- 239
Cdd:cd09287 108 ----W----------------PTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRLKIEGGKl 167
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2795819396 240 KLSKRHGALGVGEY-----------QAM---GYPAAAMRNYLARLG 271
Cdd:cd09287 168 STSKIRKGIESGEYegwddprlptlRALrrrGIRPEAIRDFIIEVG 213
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
6-201 |
2.04e-21 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 93.63 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAARADRH 85
Cdd:PRK14703 32 VVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHLYYASDYFERM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 86 AEIAHQMLAAGHAYKCYASQDEITAFREAARAEGKstlyQSPWRDADPATHPDapYVVRLKAPR--DGATVIpdRVQGDV 163
Cdd:PRK14703 112 YAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGT----PSPYRDRSVEENLD--LFRRMRAGEfpDGAHVL--RAKIDM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2795819396 164 TWKNDQLDDMVLLR---------SDG---TPTYMLAVVVDDFDMGVTHVI 201
Cdd:PRK14703 184 SSPNMKLRDPLLYRirhahhyrtGDEwciYPMYDFAHPLEDAIEGVTHSI 233
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
6-99 |
2.30e-19 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 84.61 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGepISQAARA-DR 84
Cdd:cd00807 2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYK--VTYASDYfDQ 79
|
90
....*....|....*
gi 2795819396 85 HAEIAHQMLAAGHAY 99
Cdd:cd00807 80 LYEYAEQLIKKGKAY 94
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
6-244 |
8.92e-19 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 85.83 E-value: 8.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLdwdgEPISQAARADRH 85
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEI----KPDSVSFTSDYF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 86 AEI---AHQMLAAGHAYKCYASQDEITAFReAARAEGKSTlYQSP------WRDADPATHPDAPYVVRLKAprdgatvip 156
Cdd:PLN03233 88 EPIrcyAIILIEEGLAYMDDTPQEEMKKER-ADRAESKHR-NQSPeealemFKEMCSGKEEGGAWCLRAKI--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 157 drvqgDVTWKNDQLDDMVLLRSDGT------------PTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMGWDL 224
Cdd:PLN03233 157 -----DMQSDNGTLRDPVLFRQNTTphhrsgtaykayPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRR 231
|
250 260
....*....|....*....|...
gi 2795819396 225 P---VFAHIPLIHgpdgKKLSKR 244
Cdd:PLN03233 232 PrihAFARMNFMN----TVLSKR 250
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
6-130 |
4.36e-18 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 83.61 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPisqaaradRH 85
Cdd:PRK05347 30 VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWSGEL--------RY 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2795819396 86 A--------EIAHQMLAAGHAYKCYASQDEITAFREAARAEGKstlyQSPWRD 130
Cdd:PRK05347 102 AsdyfdqlyEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGK----NSPYRD 150
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
3-226 |
4.74e-17 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 80.78 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 3 EAPVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWDGEPISQAARA 82
Cdd:PTZ00402 50 EGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 83 DRHAEIAHQMLAAGHAYKCYASQDEI---------TAFREAARAEGKSTlyqspWRDADPATHPDAPYVVRLKAPRDGat 153
Cdd:PTZ00402 130 DLMYEKAEELIKKGLAYCDKTPREEMqkcrfdgvpTKYRDISVEETKRL-----WNEMKKGSAEGQETCLRAKISVDN-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 154 vipdrvqgdvtwKNDQLDDMVLLRSDGT------------PTYMLAVVVDDFDMGVTHVIRGDDHLANAARQMQIYHAMG 221
Cdd:PTZ00402 203 ------------ENKAMRDPVIYRVNLTpharqgtkykayPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALG 270
|
....*
gi 2795819396 222 WDLPV 226
Cdd:PTZ00402 271 IRKPI 275
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
6-130 |
1.28e-16 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 79.80 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 6 VVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGldWdgEPISQAARADRH 85
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--W--EPFKITYTSDYF 340
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2795819396 86 AEI---AHQMLAAGHAYKCYASQDEITAFREAARaegkstlyQSPWRD 130
Cdd:PLN02859 341 QELyelAVELIRRGHAYVDHQTPEEIKEYREKKM--------NSPWRD 380
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
3-72 |
2.18e-14 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 72.83 E-value: 2.18e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 3 EAPVVTRFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDRARSTPEATEAILTGLRWLGLDWD 72
Cdd:PLN02907 211 EGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD 280
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
9-130 |
4.72e-14 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 71.94 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 9 RFAPSPTGYLHIGGARTALFNWLYARGRGGKFLLRIEDTDrarstPEATE-----AILTGLRWLGldWDGEPISQAARA- 82
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTN-----PETEEqvyidAIMEMVKWMG--WKPDWVTFSSDYf 127
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2795819396 83 DRHAEIAHQMLAAGHAYKCYASQDEITAFREaARAEgkstlyqSPWRD 130
Cdd:PTZ00437 128 DQLHEFAVQLIKDGKAYVDHSTPDELKQQRE-QRED-------SPWRN 167
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
150-246 |
4.56e-07 |
|
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439789 [Multi-domain] Cd Length: 574 Bit Score: 50.53 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 150 DGATVIpdrvqgDVTwKNDQLDDMVLLRSDGTPTYM---LAVVVDDF-DMGVTHVIR--GDDHLANAARQMQIYHAMGWD 223
Cdd:COG0018 287 DGALWV------RLT-EFGDDKDRVLVKSDGTYTYFttdIAYHLYKFeRYGFDRVIYvvGADQHGHFKRLFAALKALGYD 359
|
90 100
....*....|....*....|....*.
gi 2795819396 224 LP-VFAHIP--LIHGPDGKKLSKRHG 246
Cdd:COG0018 360 PAkDLEHLLfgMVNLRDGEKMSTRAG 385
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
150-246 |
4.02e-06 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 46.79 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 150 DGATVIpdrvqgDVTwKNDQLDDMVLLRSDGTPTYM---LAVVVDDFDMGVTHVIR--GDDHLANAARQMQIYHAMGWDL 224
Cdd:cd00671 115 DGALWL------DLT-EFGDDKDRVLVRSDGTYTYFtrdIAYHLDKFERGADKIIYvvGADHHGHFKRLFAALELLGYDE 187
|
90 100
....*....|....*....|....*
gi 2795819396 225 PVFAHI---PLIHGPDGKKLSKRHG 246
Cdd:cd00671 188 AKKLEHllyGMVNLPKEGKMSTRAG 212
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
150-246 |
2.91e-05 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 45.15 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2795819396 150 DGATVIpdrvqgDVTwKNDQLDDMVLLRSDGTPTYM---LAVVVD---DFDmgvtHVIR--GDDHlANAARQMQ-IYHAM 220
Cdd:PRK01611 230 DGALWV------RLT-EFGDDKDRVLIKSDGTYTYFtrdIAYHLYkfeRFD----RVIYvvGADH-HGHFKRLKaALKAL 297
|
90 100 110
....*....|....*....|....*....|.
gi 2795819396 221 GWD---LPVFAHIP--LIHGPDGKKLSKRHG 246
Cdd:PRK01611 298 GYDpdaLEVLLHQMvgLVRGGEGVKMSTRAG 328
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
7-54 |
3.56e-03 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 37.07 E-value: 3.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2795819396 7 VTRFAPSPTGYLHIGGART-----ALFNWLYARGRGGKFLLRIEDTDRARSTP 54
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTivtfdFLAQAYRKLGYKVRCIALIDDAGGLIGDP 53
|
|
| |
