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Conserved domains on  [gi|2327399340|ref|WP_264990365|]
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Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC [Lysinibacillus piscis]

Protein Classification

aspartyl/glutamyl-tRNA amidotransferase subunit C( domain architecture ID 10002289)

aspartyl/glutamyl-tRNA synthase subunit C (GatC) is part of a heterotrimeric complex that forms correctly charged Gln-tRNA(Gln) or Asn-tRNA(Asn) through the transamidation of misacylated Glu-tRNA(Gln) or Asp-tRNA(Asn)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 3-95 4.57e-40

Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


:

Pssm-ID: 440485 [Multi-domain]  Cd Length: 95  Bit Score: 127.52  E-value: 4.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327399340  3 KLTKEEVKHVANLARLAITEEEAEKFAEQLGKITDFAEQLNELDTTNVEPTTHVLPLVNVMREDVAAEGLARDVMMLNVK 82
Cdd:COG0721    2 SITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANAP 81

                         90
                 ....*....|...
gi 2327399340 83 EQEDGQVKVPAIM 95
Cdd:COG0721   82 ETEDGYFKVPKVI 94
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 3-95 4.57e-40

Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440485 [Multi-domain]  Cd Length: 95  Bit Score: 127.52  E-value: 4.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327399340  3 KLTKEEVKHVANLARLAITEEEAEKFAEQLGKITDFAEQLNELDTTNVEPTTHVLPLVNVMREDVAAEGLARDVMMLNVK 82
Cdd:COG0721    2 SITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANAP 81

                         90
                 ....*....|...
gi 2327399340 83 EQEDGQVKVPAIM 95
Cdd:COG0721   82 ETEDGYFKVPKVI 94
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
3-95 1.92e-34

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 113.37  E-value: 1.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327399340  3 KLTKEEVKHVANLARLAITEEEAEKFAEQLGKITDFAEQLNELDTTNVEPTTHVLPLVNVMREDVAAEGLARDVMMLNVK 82
Cdd:PRK00034   2 AITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTESLPREEALKNAP 81

                         90
                 ....*....|...
gi 2327399340 83 EQEDGQVKVPAIM 95
Cdd:PRK00034  82 ESEDGYFKVPKVI 94
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 4-94 1.15e-32

aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many bacteria charge Gln-tRNA by first misacylating it with Glu and then amidating Glu to Gln. This small protein is part of the amidotransferase heterotrimer and appears to be important to the stability of the amidase subunit encode by gatA, but its function may not be required in every organism that expresses gatA and gatB. The seed alignment for this model does not include any eukaryotic sequence and is not guaranteed to find eukaryotic examples, although it does find some. Saccharomyces cerevisiae, which expresses the amidotransferase for mitochondrial protein translation, seems to lack a gatC ortholog. This model has been revised to remove the candidate sequence from Methanococcus jannaschii, now part of a related model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129241 [Multi-domain]  Cd Length: 93  Bit Score: 108.92  E-value: 1.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327399340  4 LTKEEVKHVANLARLAITEEEAEKFAEQLGKITDFAEQLNELDTTNVEPTTHVLPLVNVMREDVAAEGLARDVMMLNVKE 83
Cdd:TIGR00135  1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDEPEEPLSRDDILKNAPE 80

                         90
                 ....*....|.
gi 2327399340 84 QEDGQVKVPAI 94
Cdd:TIGR00135 81 KEDGFIKVPKI 91
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 22-91 5.67e-25

Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C subunits. The Glu-tRNA Gln amidotransferase enzyme itself is an important translational fidelity mechanism replacing incorrectly charged Glu-tRNAGln with the correct Gln-tRANGln via transmidation of the misacylated Glu-tRNAGln. This activity supplements the lack of glutaminyl-tRNA synthetase activity in gram-positive eubacterteria, cyanobacteria, Archaea, and organelles.


Pssm-ID: 460651 [Multi-domain]  Cd Length: 70  Bit Score: 88.72  E-value: 5.67e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327399340 22 EEEAEKFAEQLGKITDFAEQLNELDTTNVEPTTHVLPLVNVMREDVAAEGLARDVMMLNVKEQEDGQVKV 91
Cdd:pfam02686  1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLTNVLREDEVTESLDREEALANAPETEDGFFKV 70
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 3-95 4.57e-40

Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440485 [Multi-domain]  Cd Length: 95  Bit Score: 127.52  E-value: 4.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327399340  3 KLTKEEVKHVANLARLAITEEEAEKFAEQLGKITDFAEQLNELDTTNVEPTTHVLPLVNVMREDVAAEGLARDVMMLNVK 82
Cdd:COG0721    2 SITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANAP 81

                         90
                 ....*....|...
gi 2327399340 83 EQEDGQVKVPAIM 95
Cdd:COG0721   82 ETEDGYFKVPKVI 94
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
3-95 1.92e-34

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 113.37  E-value: 1.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327399340  3 KLTKEEVKHVANLARLAITEEEAEKFAEQLGKITDFAEQLNELDTTNVEPTTHVLPLVNVMREDVAAEGLARDVMMLNVK 82
Cdd:PRK00034   2 AITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTESLPREEALKNAP 81

                         90
                 ....*....|...
gi 2327399340 83 EQEDGQVKVPAIM 95
Cdd:PRK00034  82 ESEDGYFKVPKVI 94
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 4-94 1.15e-32

aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many bacteria charge Gln-tRNA by first misacylating it with Glu and then amidating Glu to Gln. This small protein is part of the amidotransferase heterotrimer and appears to be important to the stability of the amidase subunit encode by gatA, but its function may not be required in every organism that expresses gatA and gatB. The seed alignment for this model does not include any eukaryotic sequence and is not guaranteed to find eukaryotic examples, although it does find some. Saccharomyces cerevisiae, which expresses the amidotransferase for mitochondrial protein translation, seems to lack a gatC ortholog. This model has been revised to remove the candidate sequence from Methanococcus jannaschii, now part of a related model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129241 [Multi-domain]  Cd Length: 93  Bit Score: 108.92  E-value: 1.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327399340  4 LTKEEVKHVANLARLAITEEEAEKFAEQLGKITDFAEQLNELDTTNVEPTTHVLPLVNVMREDVAAEGLARDVMMLNVKE 83
Cdd:TIGR00135  1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDEPEEPLSRDDILKNAPE 80

                         90
                 ....*....|.
gi 2327399340 84 QEDGQVKVPAI 94
Cdd:TIGR00135 81 KEDGFIKVPKI 91
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 22-91 5.67e-25

Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C subunits. The Glu-tRNA Gln amidotransferase enzyme itself is an important translational fidelity mechanism replacing incorrectly charged Glu-tRNAGln with the correct Gln-tRANGln via transmidation of the misacylated Glu-tRNAGln. This activity supplements the lack of glutaminyl-tRNA synthetase activity in gram-positive eubacterteria, cyanobacteria, Archaea, and organelles.


Pssm-ID: 460651 [Multi-domain]  Cd Length: 70  Bit Score: 88.72  E-value: 5.67e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327399340 22 EEEAEKFAEQLGKITDFAEQLNELDTTNVEPTTHVLPLVNVMREDVAAEGLARDVMMLNVKEQEDGQVKV 91
Cdd:pfam02686  1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLTNVLREDEVTESLDREEALANAPETEDGFFKV 70
PRK12821 PRK12821
aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional
 3-91 2.31e-06

aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional


Pssm-ID: 237216 [Multi-domain]  Cd Length: 477  Bit Score: 43.73  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327399340   3 KLTKEEVKHVANLARLAITEEEAEKFAEQLGKITDFAEQLNELDTTNVEPTTHVLPLV-NVMREDVAAEGLARDVMMLNV 81
Cdd:PRK12821  388 QLNKDELKKLARLVMFDLDDAELEKLQVEFKDITSSFKQVEKIDTTNVKPMYAPFSNSpTPLRKDKDVVQKHQKILLKNC 467

                          90
                  ....*....|
gi 2327399340  82 KEQEDGQVKV 91
Cdd:PRK12821  468 KETLGGFVKV 477
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 6-69 3.06e-03

bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 34.96  E-value: 3.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2327399340   6 KEEVKHVANLARLAITEEEAEKFAEQLGKITDFAEQLNELDTtNVEPTTHVLPLVNVMREDVAA 69
Cdd:PRK12820  614 EDLIDHLSWVSRIGFAEAERAAIESALADAEELAAQLEDIAC-DEEPLFSPAPAANRMGEGLEA 676
 
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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