|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
1-287 |
7.91e-163 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 454.31 E-value: 7.91e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 1 MTDSRYIGRFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQ 80
Cdd:PRK05710 1 MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 81 RHEAYREALTWLGEQGLSYYCTCTRARI-------HAVGGIYDGHCRDLGLGAENA-ALRLRQTRPVLQFSDRLRGTLIA 152
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCSRKEIaaaapapPDGGGIYPGTCRDLLHGPRNPpAWRLRVPDAVIAFDDRLQGRQHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 153 NEPLAREDFIIHRRDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNKLSKQ 232
Cdd:PRK05710 161 DLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490247766 233 NHAPALPEGDPRPEIVRALRFLNQAIPEEWQALSidDLLAQAVANWQPAKIEHSQ 287
Cdd:PRK05710 241 NGAPALDAAGPLPVLAAALRFLGQPPPAADASVE--ELLAQAVAHWDLTRLPRQA 293
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
6-271 |
3.15e-155 |
|
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: 433.89 E-value: 3.15e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 6 YIGRFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQRHEAY 85
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 86 REALTWLGEQGLSYYCTCTRARI---HAVGGIYDGHCRD--LGLGAENAALRLRQTRPVLQFSDRLRGTLIANEPLARED 160
Cdd:TIGR03838 81 QAALDRLLAAGLAYPCQCTRKEIaaaRDGGGIYPGTCRNglPGRPGRPAAWRLRVPDGVIAFDDRLQGPQQQDLAAAVGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 161 FIIHRRDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNKLSKQNHAPALPE 240
Cdd:TIGR03838 161 FVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGAPALDD 240
|
250 260 270
....*....|....*....|....*....|.
gi 490247766 241 GDPRPEIVRALRFLNQAIPEEWQALSIDDLL 271
Cdd:TIGR03838 241 SRPLPALLAALRFLGLPPPPELAAASPAELL 271
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
9-231 |
6.20e-61 |
|
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: 200.02 E-value: 6.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQRHEAYREA 88
Cdd:COG0008 8 RFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIYYEY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 89 LTWLGEQGLSYYCTCT-------RARIHAVGG--IYDGHCRDL-----------GlgaENAALRLRQTRPVLQFSDRLRG 148
Cdd:COG0008 88 AEKLIEKGKAYVCFCTpeelealRETQTAPGKppRYDGRCRDLspeelermlaaG---EPPVLRFKIPEEGVVFDDLVRG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 149 TLIANEPLAReDFIIHRRDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNK 228
Cdd:COG0008 165 EITFPNPNLR-DPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTK 243
|
...
gi 490247766 229 LSK 231
Cdd:COG0008 244 LSK 246
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
9-252 |
8.84e-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: 172.12 E-value: 8.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQRHEAYREA 88
Cdd:pfam00749 5 RFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 89 LTWLGEQGLSYYCTCTRARIHAVGGI-----------YDGHCRDLGLGA--------ENAALRLRQ-TRPVLQFSDRLRG 148
Cdd:pfam00749 85 AEELIKKGKAYVCFCTPEELEEEREEqealgspsrdrYDEENLHLFEEEmkkgsaegGPATVRAKIpMESPYVFRDPVRG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 149 TlIANEPLAREDFIIHRRDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNK 228
Cdd:pfam00749 165 R-IKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLDGTK 243
|
250 260 270
....*....|....*....|....*....|
gi 490247766 229 LSKQNHAPALPE------GDPRPEIVRALR 252
Cdd:pfam00749 244 LSKRKLSWSVDIsqvkgwGDPREATLNGLR 273
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
9-273 |
3.87e-43 |
|
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: 147.73 E-value: 3.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLW--------QSQ 80
Cdd:cd00808 5 RFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVggpygpyrQSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 81 RHEAYREALTWLGEQGlsyyctctrarihavggiydghcrdlglgaenaalrlrqtrpvlqfsdrlrgtlianeplared 160
Cdd:cd00808 85 RLEIYRKYAEKLLEKG---------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 161 fiihrrDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNKLSKQNHAPA--- 237
Cdd:cd00808 101 ------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGKKLSKRKGDTSisd 174
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490247766 238 ------LPEGdprpeIVRALRFLNQAIPEEWQALSIDDLLAQ 273
Cdd:cd00808 175 yreegyLPEA-----LLNYLALLGWSPPDGEEFFTLEELIEL 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
1-287 |
7.91e-163 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 454.31 E-value: 7.91e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 1 MTDSRYIGRFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQ 80
Cdd:PRK05710 1 MTMTPYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 81 RHEAYREALTWLGEQGLSYYCTCTRARI-------HAVGGIYDGHCRDLGLGAENA-ALRLRQTRPVLQFSDRLRGTLIA 152
Cdd:PRK05710 81 RHDAYRAALDRLRAQGLVYPCFCSRKEIaaaapapPDGGGIYPGTCRDLLHGPRNPpAWRLRVPDAVIAFDDRLQGRQHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 153 NEPLAREDFIIHRRDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNKLSKQ 232
Cdd:PRK05710 161 DLALAVGDFVLRRADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490247766 233 NHAPALPEGDPRPEIVRALRFLNQAIPEEWQALSidDLLAQAVANWQPAKIEHSQ 287
Cdd:PRK05710 241 NGAPALDAAGPLPVLAAALRFLGQPPPAADASVE--ELLAQAVAHWDLTRLPRQA 293
|
|
| queuosine_YadB |
TIGR03838 |
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ... |
6-271 |
3.15e-155 |
|
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: 433.89 E-value: 3.15e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 6 YIGRFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQRHEAY 85
Cdd:TIGR03838 1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVVYQSQRHALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 86 REALTWLGEQGLSYYCTCTRARI---HAVGGIYDGHCRD--LGLGAENAALRLRQTRPVLQFSDRLRGTLIANEPLARED 160
Cdd:TIGR03838 81 QAALDRLLAAGLAYPCQCTRKEIaaaRDGGGIYPGTCRNglPGRPGRPAAWRLRVPDGVIAFDDRLQGPQQQDLAAAVGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 161 FIIHRRDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNKLSKQNHAPALPE 240
Cdd:TIGR03838 161 FVLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGAPALDD 240
|
250 260 270
....*....|....*....|....*....|.
gi 490247766 241 GDPRPEIVRALRFLNQAIPEEWQALSIDDLL 271
Cdd:TIGR03838 241 SRPLPALLAALRFLGLPPPPELAAASPAELL 271
|
|
| gltX_bact |
TIGR00464 |
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ... |
9-235 |
2.74e-62 |
|
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: 203.74 E-value: 2.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQRHEAYREA 88
Cdd:TIGR00464 5 RFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDEGPYYQSQRLDIYKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 89 LTWLGEQGLSYYCTCTRARIHAVGGI---------YDGHCRDLGlGAENAALRLRQTRPVLQ----------FSDRLRGT 149
Cdd:TIGR00464 85 AKELLEEGLAYRCYCSKERLERLREEqkanketprYDGRCRNLH-EEEIENKLAKGIPPVVRfkipqeavvsFNDQVRGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 150 lIANEPLAREDFIIHRRDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNKL 229
Cdd:TIGR00464 164 -ITFQNSELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGKKL 242
|
....*.
gi 490247766 230 SKQNHA 235
Cdd:TIGR00464 243 SKRDGA 248
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
9-231 |
6.20e-61 |
|
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: 200.02 E-value: 6.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQRHEAYREA 88
Cdd:COG0008 8 RFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIYYEY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 89 LTWLGEQGLSYYCTCT-------RARIHAVGG--IYDGHCRDL-----------GlgaENAALRLRQTRPVLQFSDRLRG 148
Cdd:COG0008 88 AEKLIEKGKAYVCFCTpeelealRETQTAPGKppRYDGRCRDLspeelermlaaG---EPPVLRFKIPEEGVVFDDLVRG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 149 TLIANEPLAReDFIIHRRDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNK 228
Cdd:COG0008 165 EITFPNPNLR-DPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPLILGPDGTK 243
|
...
gi 490247766 229 LSK 231
Cdd:COG0008 244 LSK 246
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
9-252 |
8.84e-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: 172.12 E-value: 8.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQRHEAYREA 88
Cdd:pfam00749 5 RFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIYYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 89 LTWLGEQGLSYYCTCTRARIHAVGGI-----------YDGHCRDLGLGA--------ENAALRLRQ-TRPVLQFSDRLRG 148
Cdd:pfam00749 85 AEELIKKGKAYVCFCTPEELEEEREEqealgspsrdrYDEENLHLFEEEmkkgsaegGPATVRAKIpMESPYVFRDPVRG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 149 TlIANEPLAREDFIIHRRDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNK 228
Cdd:pfam00749 165 R-IKFTPQEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLDGTK 243
|
250 260 270
....*....|....*....|....*....|
gi 490247766 229 LSKQNHAPALPE------GDPRPEIVRALR 252
Cdd:pfam00749 244 LSKRKLSWSVDIsqvkgwGDPREATLNGLR 273
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
9-273 |
3.87e-43 |
|
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: 147.73 E-value: 3.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLW--------QSQ 80
Cdd:cd00808 5 RFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVggpygpyrQSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 81 RHEAYREALTWLGEQGlsyyctctrarihavggiydghcrdlglgaenaalrlrqtrpvlqfsdrlrgtlianeplared 160
Cdd:cd00808 85 RLEIYRKYAEKLLEKG---------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 161 fiihrrDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNKLSKQNHAPA--- 237
Cdd:cd00808 101 ------DGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGKKLSKRKGDTSisd 174
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490247766 238 ------LPEGdprpeIVRALRFLNQAIPEEWQALSIDDLLAQ 273
Cdd:cd00808 175 yreegyLPEA-----LLNYLALLGWSPPDGEEFFTLEELIEL 211
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
9-284 |
1.68e-33 |
|
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: 122.20 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQRHEAYREA 88
Cdd:cd00418 5 RFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLYRAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 89 LTWLGEQGlsyyctctrarihavggiydghcrdlglgaenaalrlrqtrpvlqfsdrlrgtlianeplaredfiihrrdG 168
Cdd:cd00418 85 AEELIKKG-----------------------------------------------------------------------G 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 169 LFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNKLSKQNHAPALPEGDPR---P 245
Cdd:cd00418 94 YPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKLSKRKLNTTLRALRRRgylP 173
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490247766 246 EIVRA-LRFLNQAIPEEWQALSIDDLLAQ---AVANWQPAKIE 284
Cdd:cd00418 174 EALRNyLALIGWSKPDGHELFTLEEMIAAfsvERVNSADATFD 216
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
9-284 |
1.96e-31 |
|
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: 122.62 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDgDVLWQSQRHEAYREA 88
Cdd:TIGR00463 97 RFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWD-EVVYQSDRIETYYDY 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 89 LTWLGEQGLSYYCTCTRARIHAVGGiyDG---HCRDLGLgAENAAL---RLRQTRPVLQFSDRLRGTLIANEPLAReDFI 162
Cdd:TIGR00463 176 TRKLIEMGKAYVCDCRPEEFRELRN--RGeacHCRDRSV-EENLERweeMLEGKEEGGSVVVRVKTDLKHKNPAIR-DWV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 163 I-------HRRDG-----LFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLALNGDGNKLS 230
Cdd:TIGR00463 252 IfrivktpHPRTGdkyrvYPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 231 KQNHAPALPEG------DPRPEIVRALR------------FLNQAIPE-----EWQALS------IDDLLAQAVANWQPA 281
Cdd:TIGR00463 332 TSSARKGILRGeysgwdDPRLPTLRAIRrrgirpeairkfMLSIGVKIndvtmSWKNIYalnrkiIDEEARRYFFIWNPV 411
|
...
gi 490247766 282 KIE 284
Cdd:TIGR00463 412 KIE 414
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
9-235 |
2.54e-30 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 119.46 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWD------GDV--LWQSQ 80
Cdd:PLN02627 49 RFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDegpdvgGEYgpYRQSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 81 RHEAYREALTWLGEQGLSYYCTCT---------RARIHAVGGIYDGHCRDLGLGAENAAL--------RLRQTR-PVLQF 142
Cdd:PLN02627 129 RNAIYKQYAEKLLESGHVYPCFCTdeeleamkeEAELKKLPPRYTGKWATASDEEVQAELakgtpytyRFRVPKeGSVKI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 143 SDRLRGTLIAN-EPLAreDFIIHRRDGLFAYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLA 221
Cdd:PLN02627 209 DDLIRGEVSWNtDTLG--DFVLLRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSLI 286
|
250
....*....|....
gi 490247766 222 LNGDGNKLSKQNHA 235
Cdd:PLN02627 287 LAPDRSKLSKRHGA 300
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
9-252 |
6.75e-27 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 109.56 E-value: 6.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPP--REVPGAADTILRQLDHYGLHWDgDVLWQSQRHEAYR 86
Cdd:PRK04156 105 RFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRtkRPDPEAYDMILEDLKWLGVKWD-EVVIQSDRLEIYY 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 87 EALTWLGEQGLSYYCTCTRARIHAV--GGIYDgHCRDLGLgAENAALrlrqtrpvlqFSDRLRGTLIANEPLAR------ 158
Cdd:PRK04156 184 EYARKLIEMGGAYVCTCDPEEFKELrdAGKPC-PHRDKSP-EENLEL----------WEKMLDGEYKEGEAVVRvktdle 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 159 ------EDFII-------HRRDG-------LfaYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHL 218
Cdd:PRK04156 252 hpnpsvRDWVAfrivktpHPRVGdkyrvwpT--YNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWEYPETIHY 329
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490247766 219 PlALNGDGNKLSKQNHAPALPEG------DPRPEIVRALR 252
Cdd:PRK04156 330 G-RLKIEGFVLSTSKIRKGIEEGeysgwdDPRLPTLRALR 368
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
9-262 |
1.78e-25 |
|
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: 101.27 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDP--PREVPGAADTILRQLDHYGLHWDgDVLWQSQRHEAYR 86
Cdd:cd09287 5 RFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWD-EVVIASDRIELYY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 87 EALTWLGEQGLSYyctctrarIHAVGGiydghcrdlglgaenaalrlrqtrpvlqfsDRLRGTlianePLaredfiihrr 166
Cdd:cd09287 84 EYARKLIEMGGAY--------VHPRTG------------------------------SKYRVW-----PT---------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 167 dglfaYNLAVVVDDHFQGITEIVRGADLIEPTVRQISLYQHFGWQAPDYLHLPLaLNGDGNKLSKQNHAPALPEG----- 241
Cdd:cd09287 111 -----LNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGR-LKIEGGKLSTSKIRKGIESGeyegw 184
|
250 260
....*....|....*....|....*
gi 490247766 242 -DPRPEIVRALR---FLNQAIPEEW 262
Cdd:cd09287 185 dDPRLPTLRALRrrgIRPEAIRDFI 209
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
5-99 |
3.23e-08 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 54.25 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 5 RYIGRFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDgDVLWQSQRHEA 84
Cdd:PLN03233 11 QIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPD-SVSFTSDYFEP 89
|
90
....*....|....*
gi 490247766 85 YREALTWLGEQGLSY 99
Cdd:PLN03233 90 IRCYAIILIEEGLAY 104
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
9-72 |
1.20e-05 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 46.64 E-value: 1.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWD 72
Cdd:PLN02907 217 RFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYD 280
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
5-99 |
5.29e-05 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 44.57 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 5 RYIGRFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQRHEA 84
Cdd:PTZ00402 52 KVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDL 131
|
90
....*....|....*
gi 490247766 85 YREALTWLGEQGLSY 99
Cdd:PTZ00402 132 MYEKAEELIKKGLAY 146
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
4-99 |
6.50e-05 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 44.33 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490247766 4 SRYIGRFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWDGDVLWQSQRHE 83
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGEHLYYASDYFE 109
|
90
....*....|....*.
gi 490247766 84 AYREALTWLGEQGLSY 99
Cdd:PRK14703 110 RMYAYAEQLIKMGLAY 125
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
9-72 |
2.10e-04 |
|
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: 41.85 E-value: 2.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490247766 9 RFAPSPSGELHFGSLIAALGSYLQARANQGIWRVRIEDIDPPREVPGAADTILRQLDHYGLHWD 72
Cdd:cd00807 5 RFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY 68
|
|
| |
