|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
1-292 |
3.92e-163 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 455.46 E-value: 3.92e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 1 MQESHYVGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQ 80
Cdd:PRK05710 1 MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 81 RHDAYRAALDLLQRQGLSYYCTCTRSRIQ-------HIGGLYDGHCRDLQLGPQGA-AIRLRQTAPVYGFHDRLQGELHA 152
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCSRKEIAaaapappDGGGIYPGTCRDLLHGPRNPpAWRLRVPDAVIAFDDRLQGRQHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 153 DPALAGEDFIIRRRDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANGIKLSKQ 232
Cdd:PRK05710 161 DLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 233 NHAPALPAGDPRPVLIAALKFLRQPLPESWQdlDLPLLLSWAVAHWRLENVPRQEAIPLD 292
Cdd:PRK05710 241 NGAPALDAAGPLPVLAAALRFLGQPPPAADA--SVEELLAQAVAHWDLTRLPRQAEINPA 298
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
6-264 |
5.79e-151 |
|
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: 423.49 E-value: 5.79e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 6 YVGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQRHDAY 85
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 86 RAALDLLQRQGLSYYCTCTRSRIQ---HIGGLYDGHCRDLQLGPQG--AAIRLRQTAPVYGFHDRLQGELHADPALAGED 160
Cdd:TIGR03838 81 QAALDRLLAAGLAYPCQCTRKEIAaarDGGGIYPGTCRNGLPGRPGrpAAWRLRVPDGVIAFDDRLQGPQQQDLAAAVGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 161 FIIRRRDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANGIKLSKQNHAPALPA 240
Cdd:TIGR03838 161 FVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGAPALDD 240
|
250 260
....*....|....*....|....
gi 1398598860 241 GDPRPVLIAALKFLRQPLPESWQD 264
Cdd:TIGR03838 241 SRPLPALLAALRFLGLPPPPELAA 264
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
9-231 |
1.51e-64 |
|
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: 210.03 E-value: 1.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 9 RFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQRHDAYRAA 88
Cdd:COG0008 8 RFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIYYEY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 89 LDLLQRQGLSYYCTCTRSRI------QHIGGL---YDGHCRDL------QLGPQG--AAIRLRQTAPVYGFHDRLQGELH 151
Cdd:COG0008 88 AEKLIEKGKAYVCFCTPEELealretQTAPGKpprYDGRCRDLspeeleRMLAAGepPVLRFKIPEEGVVFDDLVRGEIT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 152 ADPALAGeDFIIRRRDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANGIKLSK 231
Cdd:COG0008 168 FPNPNLR-DPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKLSK 246
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
9-231 |
2.65e-52 |
|
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: 174.04 E-value: 2.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 9 RFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQRHDAYRAA 88
Cdd:pfam00749 5 RFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 89 LDLLQRQGLSYYCTCTRSRIQHIGGL-----------YDGHCRDL----------QLGPqgAAIRLRQ-TAPVYGFHDRL 146
Cdd:pfam00749 85 AEELIKKGKAYVCFCTPEELEEEREEqealgspsrdrYDEENLHLfeeemkkgsaEGGP--ATVRAKIpMESPYVFRDPV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 147 QGELHADPALAGeDFIIRRRDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANG 226
Cdd:pfam00749 163 RGRIKFTPQEIH-DRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLDG 241
|
....*
gi 1398598860 227 IKLSK 231
Cdd:pfam00749 242 TKLSK 246
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
9-231 |
3.26e-41 |
|
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: 142.73 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 9 RFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQV--------IYQSQ 80
Cdd:cd00808 5 RFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPdvggpygpYRQSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 81 RHDAYRAALDLLQRQGlsyyctctrsriqhigglydghcrdlqlgpqgaairlrqtapvygfhdrlqgelhadpalaged 160
Cdd:cd00808 85 RLEIYRKYAEKLLEKG---------------------------------------------------------------- 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598860 161 fiirrrDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANGIKLSK 231
Cdd:cd00808 101 ------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGKKLSK 165
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
1-292 |
3.92e-163 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 455.46 E-value: 3.92e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 1 MQESHYVGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQ 80
Cdd:PRK05710 1 MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 81 RHDAYRAALDLLQRQGLSYYCTCTRSRIQ-------HIGGLYDGHCRDLQLGPQGA-AIRLRQTAPVYGFHDRLQGELHA 152
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCSRKEIAaaapappDGGGIYPGTCRDLLHGPRNPpAWRLRVPDAVIAFDDRLQGRQHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 153 DPALAGEDFIIRRRDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANGIKLSKQ 232
Cdd:PRK05710 161 DLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 233 NHAPALPAGDPRPVLIAALKFLRQPLPESWQdlDLPLLLSWAVAHWRLENVPRQEAIPLD 292
Cdd:PRK05710 241 NGAPALDAAGPLPVLAAALRFLGQPPPAADA--SVEELLAQAVAHWDLTRLPRQAEINPA 298
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
6-264 |
5.79e-151 |
|
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: 423.49 E-value: 5.79e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 6 YVGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQRHDAY 85
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 86 RAALDLLQRQGLSYYCTCTRSRIQ---HIGGLYDGHCRDLQLGPQG--AAIRLRQTAPVYGFHDRLQGELHADPALAGED 160
Cdd:TIGR03838 81 QAALDRLLAAGLAYPCQCTRKEIAaarDGGGIYPGTCRNGLPGRPGrpAAWRLRVPDGVIAFDDRLQGPQQQDLAAAVGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 161 FIIRRRDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANGIKLSKQNHAPALPA 240
Cdd:TIGR03838 161 FVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGAPALDD 240
|
250 260
....*....|....*....|....
gi 1398598860 241 GDPRPVLIAALKFLRQPLPESWQD 264
Cdd:TIGR03838 241 SRPLPALLAALRFLGLPPPPELAA 264
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
9-235 |
4.26e-65 |
|
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: 211.44 E-value: 4.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 9 RFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQRHDAYRAA 88
Cdd:TIGR00464 5 RFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDIYKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 89 LDLLQRQGLSYYCTCTRSRIQHIGGL---------YDGHCRDL------QLGPQGAAIRLRQTAP---VYGFHDRLQGEL 150
Cdd:TIGR00464 85 AKELLEEGLAYRCYCSKERLERLREEqkanketprYDGRCRNLheeeieNKLAKGIPPVVRFKIPqeaVVSFNDQVRGEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 151 HADPALAGeDFIIRRRDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANGIKLS 230
Cdd:TIGR00464 165 TFQNSELD-DFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGKKLS 243
|
....*
gi 1398598860 231 KQNHA 235
Cdd:TIGR00464 244 KRDGA 248
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
9-231 |
1.51e-64 |
|
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: 210.03 E-value: 1.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 9 RFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQRHDAYRAA 88
Cdd:COG0008 8 RFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIYYEY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 89 LDLLQRQGLSYYCTCTRSRI------QHIGGL---YDGHCRDL------QLGPQG--AAIRLRQTAPVYGFHDRLQGELH 151
Cdd:COG0008 88 AEKLIEKGKAYVCFCTPEELealretQTAPGKpprYDGRCRDLspeeleRMLAAGepPVLRFKIPEEGVVFDDLVRGEIT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 152 ADPALAGeDFIIRRRDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANGIKLSK 231
Cdd:COG0008 168 FPNPNLR-DPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTKLSK 246
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
9-231 |
2.65e-52 |
|
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: 174.04 E-value: 2.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 9 RFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQRHDAYRAA 88
Cdd:pfam00749 5 RFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 89 LDLLQRQGLSYYCTCTRSRIQHIGGL-----------YDGHCRDL----------QLGPqgAAIRLRQ-TAPVYGFHDRL 146
Cdd:pfam00749 85 AEELIKKGKAYVCFCTPEELEEEREEqealgspsrdrYDEENLHLfeeemkkgsaEGGP--ATVRAKIpMESPYVFRDPV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 147 QGELHADPALAGeDFIIRRRDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANG 226
Cdd:pfam00749 163 RGRIKFTPQEIH-DRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLDG 241
|
....*
gi 1398598860 227 IKLSK 231
Cdd:pfam00749 242 TKLSK 246
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
9-231 |
3.26e-41 |
|
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: 142.73 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 9 RFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQV--------IYQSQ 80
Cdd:cd00808 5 RFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPdvggpygpYRQSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 81 RHDAYRAALDLLQRQGlsyyctctrsriqhigglydghcrdlqlgpqgaairlrqtapvygfhdrlqgelhadpalaged 160
Cdd:cd00808 85 RLEIYRKYAEKLLEKG---------------------------------------------------------------- 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598860 161 fiirrrDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANGIKLSK 231
Cdd:cd00808 101 ------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGKKLSK 165
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
7-289 |
5.36e-35 |
|
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: 126.43 E-value: 5.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 7 VGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQRHDAYR 86
Cdd:cd00418 3 VTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 87 AALDLLQRQGlsyyctctrsriqhigglydghcrdlqlgpqgaairlrqtapvygfhdrlqgelhadpalagedfiirrr 166
Cdd:cd00418 83 AYAEELIKKG---------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 167 dGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLALGANGIKLSKQNHAPALPAGDPRPV 246
Cdd:cd00418 93 -GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKLSKRKLNTTLRALRRRGY 171
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1398598860 247 LIAALKFLRQPLPESWQDLDLPLLLSWAVAHWRLENVPRQEAI 289
Cdd:cd00418 172 LPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVERVNSADAT 214
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
9-235 |
2.32e-30 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 119.85 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 9 RFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWD------GQV--IYQSQ 80
Cdd:PLN02627 49 RFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdvgGEYgpYRQSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 81 RHDAYRAALDLLQRQGLSYYCTCT---------RSRIQHIGGLYDGHCRDLQLGPQGAAIRlRQTAPVYGFHDRLQGELH 151
Cdd:PLN02627 129 RNAIYKQYAEKLLESGHVYPCFCTdeeleamkeEAELKKLPPRYTGKWATASDEEVQAELA-KGTPYTYRFRVPKEGSVK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 152 ADPALAGE---------DFIIRRRDGLFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLAL 222
Cdd:PLN02627 208 IDDLIRGEvswntdtlgDFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSLIL 287
|
250
....*....|...
gi 1398598860 223 GANGIKLSKQNHA 235
Cdd:PLN02627 288 APDRSKLSKRHGA 300
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
7-252 |
8.09e-24 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 101.08 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 7 VGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPP--REVPGAAARILSALEHYGLHWDgQVIYQSQRHDA 84
Cdd:PRK04156 103 VMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-EVVIQSDRLEI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 85 -YRAALDLLQRqGLSYYCTCTRSRIqhigglydghcRDLQLgpQGAAIRLRQTAP---VYGFHDRLQGEL---------- 150
Cdd:PRK04156 182 yYEYARKLIEM-GGAYVCTCDPEEF-----------KELRD--AGKPCPHRDKSPeenLELWEKMLDGEYkegeavvrvk 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 151 ----HADPALagEDFIIRR-------RDG-------LfaYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPE 212
Cdd:PRK04156 248 tdleHPNPSV--RDWVAFRivktphpRVGdkyrvwpT--YNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWEY 323
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1398598860 213 PAYVHLPlALGANGIKLSKQNHAPALPAG------DPRPVLIAALK 252
Cdd:PRK04156 324 PETIHYG-RLKIEGFVLSTSKIRKGIEEGeysgwdDPRLPTLRALR 368
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
7-217 |
3.34e-23 |
|
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: 99.51 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 7 VGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDgQVIYQSQRHDAYR 86
Cdd:TIGR00463 95 VMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-EVVYQSDRIETYY 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 87 AALDLLQRQGLSYYCTCTRSRIQHIGGlyDG---HCRDlqlgpqgaaIRLRQTAPVygFHDRLQGEL------------- 150
Cdd:TIGR00463 174 DYTRKLIEMGKAYVCDCRPEEFRELRN--RGeacHCRD---------RSVEENLER--WEEMLEGKEeggsvvvrvktdl 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 151 -HADPALagEDFIIRR-------RDG-----LFAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVH 217
Cdd:TIGR00463 241 kHKNPAI--RDWVIFRivktphpRTGdkyrvYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIH 318
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
7-283 |
2.45e-20 |
|
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: 87.79 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 7 VGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDP--PREVPGAAARILSALEHYGLHWDgQVIYQSQRHDA 84
Cdd:cd09287 3 VMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 85 YraaldllqrqglsyyctctrsriqhigglYDgHCRDLqLGPQGAAIRlrqtapvygfhdrlqgelhadpALAGEDFIIR 164
Cdd:cd09287 82 Y-----------------------------YE-YARKL-IEMGGAYVH----------------------PRTGSKYRVW 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 165 RrdglfAYNLAVVIDDHFQGVTEIVRGADLIEPTVRQIALYRQLQAPEPAYVHLPLaLGANGIKLSKQNHAPALPAG--- 241
Cdd:cd09287 109 P-----TLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGR-LKIEGGKLSTSKIRKGIESGeye 182
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1398598860 242 ---DPRPVLIAALKfLRQPLPESWQDLDLPLLLSWAVAHWRLENV 283
Cdd:cd09287 183 gwdDPRLPTLRALR-RRGIRPEAIRDFIIEVGVKQTDATISWENL 226
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
2-109 |
2.59e-09 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 58.05 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 2 QESHYVGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQR 81
Cdd:PTZ00402 49 EEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDY 128
|
90 100
....*....|....*....|....*....
gi 1398598860 82 HD-AYRAALDLLQRqGLSYYCTCTRSRIQ 109
Cdd:PTZ00402 129 MDlMYEKAEELIKK-GLAYCDKTPREEMQ 156
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
9-110 |
4.89e-07 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 50.88 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 9 RFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDgQVIYQSqrhDAYRAA 88
Cdd:PLN02907 217 RFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD-AVTYTS---DYFPQL 292
|
90 100
....*....|....*....|....*
gi 1398598860 89 LDL---LQRQGLSYYCTCTRSRIQH 110
Cdd:PLN02907 293 MEMaekLIKEGKAYVDDTPREQMRK 317
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
7-99 |
1.44e-06 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 49.24 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 7 VGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDgQVIYQSQRHDAYR 86
Cdd:PLN03233 13 VTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPD-SVSFTSDYFEPIR 91
|
90
....*....|...
gi 1398598860 87 AALDLLQRQGLSY 99
Cdd:PLN03233 92 CYAIILIEEGLAY 104
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
7-99 |
2.74e-06 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 48.56 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 7 VGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDGQVIYQSQRHDAYR 86
Cdd:PRK14703 33 VTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHLYYASDYFERMY 112
|
90
....*....|...
gi 1398598860 87 AALDLLQRQGLSY 99
Cdd:PRK14703 113 AYAEQLIKMGLAY 125
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
7-99 |
1.07e-05 |
|
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: 45.71 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598860 7 VGRFAPSPSGDLHFGSLIAALGSYLQARAQRGQWLVRIEDIDPPREVPGAAARILSALEHYGLHWDgQVIYQSQRHDA-Y 85
Cdd:cd00807 3 VTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQlY 81
|
90
....*....|....
gi 1398598860 86 RAALDLLqRQGLSY 99
Cdd:cd00807 82 EYAEQLI-KKGKAY 94
|
|
| |
