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Conserved domains on  [gi|1701533660|ref|WP_142081311|]
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Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC [Roseinatronobacter monicus]

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 ...
 2-96 3.90e-37

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: 120.20  E-value: 3.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701533660  2 SEIDLETARKVAHLARIAVPEDNLPALAQELSQILTFMEELNEVDVEGVEPMTSVTPMRLKRRKDGVTDGDMQAKILSNA 81
Cdd:COG0721    1 MSITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANA 80

                         90
                 ....*....|....*
gi 1701533660 82 PDAREGFFAVPKVVE 96
Cdd:COG0721   81 PETEDGYFKVPKVIE 95
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 2-96 3.90e-37

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: 120.20  E-value: 3.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701533660  2 SEIDLETARKVAHLARIAVPEDNLPALAQELSQILTFMEELNEVDVEGVEPMTSVTPMRLKRRKDGVTDGDMQAKILSNA 81
Cdd:COG0721    1 MSITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANA 80

                         90
                 ....*....|....*
gi 1701533660 82 PDAREGFFAVPKVVE 96
Cdd:COG0721   81 PETEDGYFKVPKVIE 95
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
2-96 2.69e-35

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 115.68  E-value: 2.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701533660  2 SEIDLETARKVAHLARIAVPEDNLPALAQELSQILTFMEELNEVDVEGVEPMTSVTPMRLKRRKDGVTDGDMQAKILSNA 81
Cdd:PRK00034   1 MAITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTESLPREEALKNA 80

                         90
                 ....*....|....*
gi 1701533660 82 PDAREGFFAVPKVVE 96
Cdd:PRK00034  81 PESEDGYFKVPKVIE 95
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 4-96 7.94e-27

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: 93.90  E-value: 7.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701533660  4 IDLETARKVAHLARIAVPEDNLPALAQELSQILTFMEELNEVDVEGVEPMTSVTPMRLKRRKDGVTDGDMQAKILSNAPD 83
Cdd:TIGR00135  1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDEPEEPLSRDDILKNAPE 80

                         90
                 ....*....|...
gi 1701533660 84 AREGFFAVPKVVE 96
Cdd:TIGR00135 81 KEDGFIKVPKIIE 93
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 22-91 3.23e-22

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: 81.79  E-value: 3.23e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701533660 22 EDNLPALAQELSQILTFMEELNEVDVEGVEPMTSVTPMRLKRRKDGVTDGDMQAKILSNAPDAREGFFAV 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 ...
 2-96 3.90e-37

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: 120.20  E-value: 3.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701533660  2 SEIDLETARKVAHLARIAVPEDNLPALAQELSQILTFMEELNEVDVEGVEPMTSVTPMRLKRRKDGVTDGDMQAKILSNA 81
Cdd:COG0721    1 MSITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANA 80

                         90
                 ....*....|....*
gi 1701533660 82 PDAREGFFAVPKVVE 96
Cdd:COG0721   81 PETEDGYFKVPKVIE 95
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
2-96 2.69e-35

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 115.68  E-value: 2.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701533660  2 SEIDLETARKVAHLARIAVPEDNLPALAQELSQILTFMEELNEVDVEGVEPMTSVTPMRLKRRKDGVTDGDMQAKILSNA 81
Cdd:PRK00034   1 MAITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTESLPREEALKNA 80

                         90
                 ....*....|....*
gi 1701533660 82 PDAREGFFAVPKVVE 96
Cdd:PRK00034  81 PESEDGYFKVPKVIE 95
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 4-96 7.94e-27

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: 93.90  E-value: 7.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701533660  4 IDLETARKVAHLARIAVPEDNLPALAQELSQILTFMEELNEVDVEGVEPMTSVTPMRLKRRKDGVTDGDMQAKILSNAPD 83
Cdd:TIGR00135  1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDEPEEPLSRDDILKNAPE 80

                         90
                 ....*....|...
gi 1701533660 84 AREGFFAVPKVVE 96
Cdd:TIGR00135 81 KEDGFIKVPKIIE 93
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 22-91 3.23e-22

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: 81.79  E-value: 3.23e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701533660 22 EDNLPALAQELSQILTFMEELNEVDVEGVEPMTSVTPMRLKRRKDGVTDGDMQAKILSNAPDAREGFFAV 91
Cdd:pfam02686  1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLTNVLREDEVTESLDREEALANAPETEDGFFKV 70
 
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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