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Conserved domains on  [gi|1720423901|ref|XP_030098789|]
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nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial isoform X1 [Mus musculus]

Protein Classification

nucleotidyl transferase family protein( domain architecture ID 117)

nucleotidyl transferase (NT) family protein contains a conserved dinucleotide-binding domain; the NT superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and cytidylyltransferases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nt_trans super family cl00015
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 37-139 1.43e-58

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


The actual alignment was detected with superfamily member cd00808:

Pssm-ID: 469580 [Multi-domain]  Cd Length: 239  Bit Score: 191.65  E-value: 1.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRRGGPAGPYC 116
Cdd:cd00808     2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81

                          90       100
                  ....*....|....*....|...
gi 1720423901 117 QSQRLALYAQATEALLRSGAAYP 139
Cdd:cd00808    82 QSERLEIYRKYAEKLLEKGDGFP 104
 
Name Accession Description Interval E-value
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 37-139 1.43e-58

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: 191.65  E-value: 1.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRRGGPAGPYC 116
Cdd:cd00808     2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81

                          90       100
                  ....*....|....*....|...
gi 1720423901 117 QSQRLALYAQATEALLRSGAAYP 139
Cdd:cd00808    82 QSERLEIYRKYAEKLLEKGDGFP 104
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 33-162 4.74e-56

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: 191.93  E-value: 4.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  33 PGAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpa 112
Cdd:COG0008     1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720423901 113 GPYCQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPR 162
Cdd:COG0008    73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPR 122
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 36-199 3.20e-52

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: 181.78  E-value: 3.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPY 115
Cdd:TIGR00464   1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901 116 CQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPRQEEHnkpessaaklyCLHLQEPESKSQSKSFIA 195
Cdd:TIGR00464  73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGR-----------CRNLHEEEIENKLAKGIP 141


                  ....
gi 1720423901 196 YIFR 199
Cdd:TIGR00464 142 PVVR 145
PLN02627 PLN02627
glutamyl-tRNA synthetase
 25-162 6.94e-48

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 171.46  E-value: 6.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  25 REASLGPDPGAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDE 104
Cdd:PLN02627   34 RAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDE 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720423901 105 SPRRGGPAGPYCQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPR 162
Cdd:PLN02627  114 GPDVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPR 171
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 36-199 5.70e-45

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: 158.25  E-value: 5.70e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPY 115
Cdd:pfam00749   1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901 116 CQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKK--EALRSRQTPRQEEHnkpessaaklyCLHLQEPESKSQSKSF 193
Cdd:pfam00749  73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREeqEALGSPSRDRYDEE-----------NLHLFEEEMKKGSAEG 141


                  ....*.
gi 1720423901 194 IAYIFR 199
Cdd:pfam00749 142 GPATVR 147
 
Name Accession Description Interval E-value
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 37-139 1.43e-58

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: 191.65  E-value: 1.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRRGGPAGPYC 116
Cdd:cd00808     2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQERSVPEAEEAILEALKWLGLDWDEGPDVGGPYGPYR 81

                          90       100
                  ....*....|....*....|...
gi 1720423901 117 QSQRLALYAQATEALLRSGAAYP 139
Cdd:cd00808    82 QSERLEIYRKYAEKLLEKGDGFP 104
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 33-162 4.74e-56

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: 191.93  E-value: 4.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  33 PGAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpa 112
Cdd:COG0008     1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDE-------- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720423901 113 GPYCQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPR 162
Cdd:COG0008    73 GPYYQSDRFDIYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPR 122
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 36-199 3.20e-52

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: 181.78  E-value: 3.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPY 115
Cdd:TIGR00464   1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFILRIEDTDLERNIEEAEEAILEGLKWLGISWDE--------GPY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901 116 CQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPRQEEHnkpessaaklyCLHLQEPESKSQSKSFIA 195
Cdd:TIGR00464  73 YQSQRLDIYKKYAKELLEEGLAYRCYCSKERLERLREEQKANKETPRYDGR-----------CRNLHEEEIENKLAKGIP 141


                  ....
gi 1720423901 196 YIFR 199
Cdd:TIGR00464 142 PVVR 145
PLN02627 PLN02627
glutamyl-tRNA synthetase
 25-162 6.94e-48

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 171.46  E-value: 6.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  25 REASLGPDPGAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDE 104
Cdd:PLN02627   34 RAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDE 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720423901 105 SPRRGGPAGPYCQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPR 162
Cdd:PLN02627  114 GPDVGGEYGPYRQSERNAIYKQYAEKLLESGHVYPCFCTDEELEAMKEEAELKKLPPR 171
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 36-199 5.70e-45

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: 158.25  E-value: 5.70e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPY 115
Cdd:pfam00749   1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDY--------GPY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901 116 CQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKK--EALRSRQTPRQEEHnkpessaaklyCLHLQEPESKSQSKSF 193
Cdd:pfam00749  73 YQSDRFDIYYKYAEELIKKGKAYVCFCTPEELEEEREeqEALGSPSRDRYDEE-----------NLHLFEEEMKKGSAEG 141


                  ....*.
gi 1720423901 194 IAYIFR 199
Cdd:pfam00749 142 GPATVR 147
PRK05710 PRK05710
tRNA glutamyl-Q(34) synthetase GluQRS;
36-142 1.98e-37

tRNA glutamyl-Q(34) synthetase GluQRS;


Pssm-ID: 235573  Cd Length: 299  Bit Score: 137.67  E-value: 1.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRRggpagpy 115
Cdd:PRK05710    5 PYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLY------- 77

                          90       100
                  ....*....|....*....|....*..
gi 1720423901 116 cQSQRLALYAQATEALLRSGAAYPCFC 142
Cdd:PRK05710   78 -QSQRHDAYRAALDRLRAQGLVYPCFC 103
queuosine_YadB TIGR03838
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ...
 37-142 2.38e-33

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: 126.12  E-value: 2.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESPRrggpagpyC 116
Cdd:TIGR03838   1 YRGRFAPSPSGPLHFGSLVAALGSYLDARAHGGRWLVRIEDLDPPREVPGAADDILRTLEAYGLHWDGEVV--------Y 72

                          90       100
                  ....*....|....*....|....*.
gi 1720423901 117 QSQRLALYAQATEALLRSGAAYPCFC 142
Cdd:TIGR03838  73 QSQRHALYQAALDRLLAAGLAYPCQC 98
GlxRS_core cd00418
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ...
 37-139 4.53e-30

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: 116.03  E-value: 4.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPYC 116
Cdd:cd00418     2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDE--------GPYR 73

                          90       100
                  ....*....|....*....|...
gi 1720423901 117 QSQRLALYAQATEALLRSGaAYP 139
Cdd:cd00418    74 QSDRFDLYRAYAEELIKKG-GYP 95
gltX PRK04156
glutamyl-tRNA synthetase; Provisional
 25-151 1.80e-25

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 235229 [Multi-domain]  Cd Length: 567  Bit Score: 108.79  E-value: 1.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  25 REASLGPDPGA---PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTD--QSRLVPGAAESIEDMLEWAG 99
Cdd:PRK04156   87 EKKGLPPLPNAekgKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDprTKRPDPEAYDMILEDLKWLG 166

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720423901 100 IPPDESprrggpagpYCQSQRLALYAQATEALLRSGAAYPCFCLPQRLELLK 151
Cdd:PRK04156  167 VKWDEV---------VIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELR 209
GluRS_non_core cd09287
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ...
 36-138 4.11e-23

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: 97.42  E-value: 4.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  36 PVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTD--QSRLVPGAAESIEDMLEWAGIPPDESprrggpag 113
Cdd:cd09287     1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDprTKRPDPEAYDMIPEDLEWLGVKWDEV-------- 72

                          90       100
                  ....*....|....*....|....*
gi 1720423901 114 pYCQSQRLALYAQATEALLRSGAAY 138
Cdd:cd09287    73 -VIASDRIELYYEYARKLIEMGGAY 96
gltX_arch TIGR00463
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ...
 37-167 1.60e-22

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: 99.90  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESprrggpagpYC 116
Cdd:TIGR00463  94 VVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEV---------VY 164

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720423901 117 QSQRLALYAQATEALLRSGAAYPCFCLPQRLELLKKEALRSRQTPRQEEHN 167
Cdd:TIGR00463 165 QSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRELRNRGEACHCRDRSVEEN 215
GlnRS_core cd00807
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ...
 37-138 7.15e-14

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: 70.74  E-value: 7.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDESprrggpagpYC 116
Cdd:cd00807     2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKV---------TY 72

                          90       100
                  ....*....|....*....|....*
gi 1720423901 117 QS---QRLALYAqatEALLRSGAAY 138
Cdd:cd00807    73 ASdyfDQLYEYA---EQLIKKGKAY 94
PTZ00402 PTZ00402
glutamyl-tRNA synthetase; Provisional
 10-138 1.74e-10

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 240404 [Multi-domain]  Cd Length: 601  Bit Score: 62.67  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  10 LAEPHVVALGHRVGRREASLGPDPGAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAE 89
Cdd:PTZ00402   26 LSNTYFTAANANEENDKLQLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQ 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720423901  90 SIEDMLEWAGIPPDesprrggpAGPYCQSQRLALYAQATEALLRSGAAY 138
Cdd:PTZ00402  106 AILDDLATLGVSWD--------VGPTYSSDYMDLMYEKAEELIKKGLAY 146
PLN02907 PLN02907
glutamate-tRNA ligase
 33-104 1.85e-10

glutamate-tRNA ligase


Pssm-ID: 215492 [Multi-domain]  Cd Length: 722  Bit Score: 62.82  E-value: 1.85e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720423901  33 PGAP---VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDE 104
Cdd:PLN02907  207 PGAEegkVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKYDA 281
PLN03233 PLN03233
putative glutamate-tRNA ligase; Provisional
 34-103 1.68e-08

putative glutamate-tRNA ligase; Provisional


Pssm-ID: 178772 [Multi-domain]  Cd Length: 523  Bit Score: 56.56  E-value: 1.68e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720423901  34 GAPVRV--RFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPD 103
Cdd:PLN03233    7 AIAGQIvtRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPD 78
PTZ00437 PTZ00437
glutaminyl-tRNA synthetase; Provisional
 34-103 1.59e-07

glutaminyl-tRNA synthetase; Provisional


Pssm-ID: 240418 [Multi-domain]  Cd Length: 574  Bit Score: 53.45  E-value: 1.59e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  34 GAPVrVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPD 103
Cdd:PTZ00437   50 GKPY-FRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPD 118
PLN02859 PLN02859
glutamine-tRNA ligase
 34-164 1.75e-07

glutamine-tRNA ligase


Pssm-ID: 178450 [Multi-domain]  Cd Length: 788  Bit Score: 53.61  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  34 GAPVRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDqsrlvPGAAES-----IEDMLEWAGIPPDESprr 108
Cdd:PLN02859  262 GGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTN-----PEAEKKeyidhIEEIVEWMGWEPFKI--- 333

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720423901 109 ggpagPYCQSQRLALYAQATEaLLRSGAAYPCFCLPQRLELLKKEALRS--RQTPRQE 164
Cdd:PLN02859  334 -----TYTSDYFQELYELAVE-LIRRGHAYVDHQTPEEIKEYREKKMNSpwRDRPIEE 385
PRK14703 PRK14703
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
 37-138 2.44e-06

glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional


Pssm-ID: 237793 [Multi-domain]  Cd Length: 771  Bit Score: 49.72  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDTDQSRLVPGAAESIEDMLEWAGIPPDEsprrggpaGPYC 116
Cdd:PRK14703   32 VVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDWGE--------HLYY 103

                          90       100
                  ....*....|....*....|..
gi 1720423901 117 QSQRLALYAQATEALLRSGAAY 138
Cdd:PRK14703  104 ASDYFERMYAYAEQLIKMGLAY 125
PRK05347 PRK05347
glutaminyl-tRNA synthetase; Provisional
 37-141 2.30e-03

glutaminyl-tRNA synthetase; Provisional


Pssm-ID: 235424 [Multi-domain]  Cd Length: 554  Bit Score: 40.09  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423901  37 VRVRFAPSPTGFLHLGGLRTALYNYIFAKKHQGSFILRLEDT-----DQsRLVpgaaESIEDMLEWAGIPPDESPRRggp 111
Cdd:PRK05347   30 VHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTnpekeDQ-EYV----DSIKEDVRWLGFDWSGELRY--- 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 1720423901 112 AGPYCQSqrlaLYAQAtEALLRSGAAYPCF 141
Cdd:PRK05347  102 ASDYFDQ----LYEYA-VELIKKGKAYVDD 126
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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