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Conserved domains on  [gi|1084422092|gb|OGM89896|]
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hypothetical protein A2597_00155 [Candidatus Woesebacteria bacterium RIFOXYD1_FULL_46_19]

Protein Classification

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC( domain architecture ID 10002289)

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

CATH:  1.10.20.60
EC:  6.3.5.-
Gene Ontology:  GO:0006450|GO:0050567|GO:0005524
SCOP:  3001870

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 ...
 2-97 1.20e-29

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: 101.71  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084422092   2 SKLTKEEVEHVVKLAKLSISDQELEKYLKQLGEVVNYIGELNEVDTEDTEPTSQTTGLENVTRADELTPqqSLTDESALS 81
Cdd:COG0721     1 MSITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTE--SLDREEALA 78

                          90
                  ....*....|....*.
gi 1084422092  82 GTEAVHNGYFKVEAIL 97
Cdd:COG0721    79 NAPETEDGYFKVPKVI 94
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 2-97 1.20e-29

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: 101.71  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084422092   2 SKLTKEEVEHVVKLAKLSISDQELEKYLKQLGEVVNYIGELNEVDTEDTEPTSQTTGLENVTRADELTPqqSLTDESALS 81
Cdd:COG0721     1 MSITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTE--SLDREEALA 78

                          90
                  ....*....|....*.
gi 1084422092  82 GTEAVHNGYFKVEAIL 97
Cdd:COG0721    79 NAPETEDGYFKVPKVI 94
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
2-97 7.14e-25

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 89.49  E-value: 7.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084422092   2 SKLTKEEVEHVVKLAKLSISDQELEKYLKQLGEVVNYIGELNEVDTEDTEPTSQTTGLENVTRADELTPqqSLTDESALS 81
Cdd:PRK00034    1 MAITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTE--SLPREEALK 78

                          90
                  ....*....|....*.
gi 1084422092  82 GTEAVHNGYFKVEAIL 97
Cdd:PRK00034   79 NAPESEDGYFKVPKVI 94
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 22-93 8.07e-18

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: 71.00  E-value: 8.07e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084422092  22 DQELEKYLKQLGEVVNYIGELNEVDTEDTEPTSQTTGLENVTRADELTPqqSLTDESALSGTEAVHNGYFKV 93
Cdd:pfam02686   1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLTNVLREDEVTE--SLDREEALANAPETEDGFFKV 70
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 4-97 7.68e-16

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: 66.55  E-value: 7.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084422092   4 LTKEEVEHVVKLAKLSISDQELEKYLKQLGEVVNYIGELNEVDTEDTEPTSQTTGLENVTRADEltPQQSLTDESALSGT 83
Cdd:TIGR00135   1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDE--PEEPLSRDDILKNA 78

                          90
                  ....*....|....
gi 1084422092  84 EAVHNGYFKVEAIL 97
Cdd:TIGR00135  79 PEKEDGFIKVPKII 92
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 2-97 1.20e-29

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: 101.71  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084422092   2 SKLTKEEVEHVVKLAKLSISDQELEKYLKQLGEVVNYIGELNEVDTEDTEPTSQTTGLENVTRADELTPqqSLTDESALS 81
Cdd:COG0721     1 MSITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTE--SLDREEALA 78

                          90
                  ....*....|....*.
gi 1084422092  82 GTEAVHNGYFKVEAIL 97
Cdd:COG0721    79 NAPETEDGYFKVPKVI 94
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
2-97 7.14e-25

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 89.49  E-value: 7.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084422092   2 SKLTKEEVEHVVKLAKLSISDQELEKYLKQLGEVVNYIGELNEVDTEDTEPTSQTTGLENVTRADELTPqqSLTDESALS 81
Cdd:PRK00034    1 MAITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTE--SLPREEALK 78

                          90
                  ....*....|....*.
gi 1084422092  82 GTEAVHNGYFKVEAIL 97
Cdd:PRK00034   79 NAPESEDGYFKVPKVI 94
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 22-93 8.07e-18

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: 71.00  E-value: 8.07e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084422092  22 DQELEKYLKQLGEVVNYIGELNEVDTEDTEPTSQTTGLENVTRADELTPqqSLTDESALSGTEAVHNGYFKV 93
Cdd:pfam02686   1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLTNVLREDEVTE--SLDREEALANAPETEDGFFKV 70
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 4-97 7.68e-16

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: 66.55  E-value: 7.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084422092   4 LTKEEVEHVVKLAKLSISDQELEKYLKQLGEVVNYIGELNEVDTEDTEPTSQTTGLENVTRADEltPQQSLTDESALSGT 83
Cdd:TIGR00135   1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDE--PEEPLSRDDILKNA 78

                          90
                  ....*....|....
gi 1084422092  84 EAVHNGYFKVEAIL 97
Cdd:TIGR00135  79 PEKEDGFIKVPKII 92
 
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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