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Conserved domains on  [gi|410934677|gb|AFV94040|]
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glutamyl-tRNA synthetase, partial [Bacillus sp. A4(2012b)]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlnS super family cl42988
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-129 2.39e-45

Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis


The actual alignment was detected with superfamily member COG0008:

Pssm-ID: 439779 [Multi-domain]  Cd Length: 467  Bit Score: 152.64  E-value: 2.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410934677   1 VNENRKKLSKRDETIiqFIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLWVN 80
Cdd:COG0008  237 LGPDGTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLN 314

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 410934677  81 NQYMKNLDLDQVAALAMPHLVKAGRvsenpaeeeQDWARKVIALYQEQM 129
Cdd:COG0008  315 GPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERA 354
 
Name Accession Description Interval E-value
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-129 2.39e-45

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: 152.64  E-value: 2.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410934677   1 VNENRKKLSKRDETIiqFIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLWVN 80
Cdd:COG0008  237 LGPDGTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLN 314

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 410934677  81 NQYMKNLDLDQVAALAMPHLVKAGRvsenpaeeeQDWARKVIALYQEQM 129
Cdd:COG0008  315 GPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERA 354
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 1-128 1.43e-43

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: 148.27  E-value: 1.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410934677    1 VNENRKKLSKRDEtiIQFIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLWVN 80
Cdd:TIGR00464 235 LDEDGKKLSKRDG--ATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLN 312

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 410934677   81 NQYMKNLDLDQVAALAMPHLVKAGRVSEnpAEEEQdwARKVIALYQEQ 128
Cdd:TIGR00464 313 AHYIKELPDEELFELLDPHLKSLVNTDT--LNREQ--LAELLLLFKER 356
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 1-86 6.09e-40

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: 133.48  E-value: 6.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410934677   1 VNENRKKLSKRDETiiQFIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLWVN 80
Cdd:cd00808  156 LNPDGKKLSKRKGD--TSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLN 233


                 ....*.
gi 410934677  81 NQYMKN 86
Cdd:cd00808  234 GQYIRE 239
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 1-78 1.56e-31

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: 113.57  E-value: 1.56e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410934677    1 VNENRKKLSKRDETIIQFIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLW 78
Cdd:pfam00749 237 LNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
PLN02627 PLN02627
glutamyl-tRNA synthetase
 3-129 1.10e-30

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 114.07  E-value: 1.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410934677   3 ENRKKLSKRDETIIqfIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLWVNNQ 82
Cdd:PLN02627 289 PDRSKLSKRHGATS--VGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNGQ 366

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 410934677  83 YMKNLDLDQVAALAMPHLVKAGRVsenpAEEEQDWARKVIALYQEQM 129
Cdd:PLN02627 367 HLRLLPEEELVKLVGERWKSAGIL----KESDGSFVKEAVELLKDGI 409
 
Name Accession Description Interval E-value
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 1-129 2.39e-45

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: 152.64  E-value: 2.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410934677   1 VNENRKKLSKRDETIiqFIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLWVN 80
Cdd:COG0008  237 LGPDGTKLSKRKGAV--TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLDRVSRSPAVFDPVKLVWLN 314

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 410934677  81 NQYMKNLDLDQVAALAMPHLVKAGRvsenpaeeeQDWARKVIALYQEQM 129
Cdd:COG0008  315 GPYIRALDDEELAELLAPELPEAGI---------REDLERLVPLVRERA 354
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 1-128 1.43e-43

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: 148.27  E-value: 1.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410934677    1 VNENRKKLSKRDEtiIQFIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLWVN 80
Cdd:TIGR00464 235 LDEDGKKLSKRDG--ATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLNRVSKSPAKFDWKKLQWLN 312

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 410934677   81 NQYMKNLDLDQVAALAMPHLVKAGRVSEnpAEEEQdwARKVIALYQEQ 128
Cdd:TIGR00464 313 AHYIKELPDEELFELLDPHLKSLVNTDT--LNREQ--LAELLLLFKER 356
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 1-86 6.09e-40

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: 133.48  E-value: 6.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410934677   1 VNENRKKLSKRDETiiQFIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLWVN 80
Cdd:cd00808  156 LNPDGKKLSKRKGD--TSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLERVSKSPAIFDPEKLDWLN 233


                 ....*.
gi 410934677  81 NQYMKN 86
Cdd:cd00808  234 GQYIRE 239
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 1-78 1.56e-31

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: 113.57  E-value: 1.56e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410934677    1 VNENRKKLSKRDETIIQFIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLW 78
Cdd:pfam00749 237 LNLDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFDVNRLSKSLEAFDRKKLDW 314
PLN02627 PLN02627
glutamyl-tRNA synthetase
 3-129 1.10e-30

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 114.07  E-value: 1.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410934677   3 ENRKKLSKRDETIIqfIEQYEELGYLPEALFNFIALLGWSPKGEEELFSKEQFIEIFDPERLSKSPAVFDKQKLLWVNNQ 82
Cdd:PLN02627 289 PDRSKLSKRHGATS--VGQFREMGYLPDAMVNYLALLGWNDGTENEIFTLEELVEKFSIDRINKSGAVFDSTKLKWMNGQ 366

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 410934677  83 YMKNLDLDQVAALAMPHLVKAGRVsenpAEEEQDWARKVIALYQEQM 129
Cdd:PLN02627 367 HLRLLPEEELVKLVGERWKSAGIL----KESDGSFVKEAVELLKDGI 409
 
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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