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Conserved domains on  [gi|47059159|ref|NP_083921|]
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glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial [Mus musculus]

Protein Classification

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC( domain architecture ID 1369)

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 super family cl00495
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
50-136 1.07e-15

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


The actual alignment was detected with superfamily member TIGR00135:

Pssm-ID: 469792 [Multi-domain]  Cd Length: 93  Bit Score: 67.71  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059159    50 VSPAVIEHLERLALVNFgSREAVDR----LEKAIAFADQLHAVDTDGVEPLESVLEDrCLYLRSDNVAEGSCAEELLQNS 125
Cdd:TIGR00135   1 ISDEEVKHLAKLARLEL-SEEEAESfagdLDKILGFVEQLNEVDTENVEPMTHPLEI-SNVLREDEPEEPLSRDDILKNA 78

                          90
                  ....*....|.
gi 47059159   126 NHVVEEYFVAP 136
Cdd:TIGR00135  79 PEKEDGFIKVP 89
 
Name Accession Description Interval E-value
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 50-136 1.07e-15

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: 67.71  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059159    50 VSPAVIEHLERLALVNFgSREAVDR----LEKAIAFADQLHAVDTDGVEPLESVLEDrCLYLRSDNVAEGSCAEELLQNS 125
Cdd:TIGR00135   1 ISDEEVKHLAKLARLEL-SEEEAESfagdLDKILGFVEQLNEVDTENVEPMTHPLEI-SNVLREDEPEEPLSRDDILKNA 78

                          90
                  ....*....|.
gi 47059159   126 NHVVEEYFVAP 136
Cdd:TIGR00135  79 PEKEDGFIKVP 89
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
55-136 7.88e-15

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 65.61  E-value: 7.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059159   55 IEHLERLALVNFgSREAVDR----LEKAIAFADQLHAVDTDGVEPLESVLeDRCLYLRSDNVAEGSCAEELLQNSNHVVE 130
Cdd:PRK00034   8 VKHLAKLARLEL-SEEELEKfagqLNKILDFVEQLNEVDTEGVEPTTHPL-DMKNVLREDVVTESLPREEALKNAPESED 85


                 ....*.
gi 47059159  131 EYFVAP 136
Cdd:PRK00034  86 GYFKVP 91
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 50-136 1.39e-14

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: 65.12  E-value: 1.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059159  50 VSPAVIEHLERLALVNFGSREA---VDRLEKAIAFADQLHAVDTDGVEPLESVLEDRcLYLRSDNVAEGSCAEELLQNSN 126
Cdd:COG0721   3 ITKEEVEHIAKLARLELSEEELerlAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLT-NVLREDEVTESLDREEALANAP 81

                        90
                ....*....|
gi 47059159 127 HVVEEYFVAP 136
Cdd:COG0721  82 ETEDGYFKVP 91
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 75-134 1.91e-11

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: 56.36  E-value: 1.91e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059159    75 LEKAIAFADQLHAVDTDGVEPLESVLEDrCLYLRSDNVAEGSCAEELLQNSNHVVEEYFV 134
Cdd:pfam02686  11 LNDILDYVEQLNEVDTEGVEPTSHPLDL-TNVLREDEVTESLDREEALANAPETEDGFFK 69
 
Name Accession Description Interval E-value
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 50-136 1.07e-15

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: 67.71  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059159    50 VSPAVIEHLERLALVNFgSREAVDR----LEKAIAFADQLHAVDTDGVEPLESVLEDrCLYLRSDNVAEGSCAEELLQNS 125
Cdd:TIGR00135   1 ISDEEVKHLAKLARLEL-SEEEAESfagdLDKILGFVEQLNEVDTENVEPMTHPLEI-SNVLREDEPEEPLSRDDILKNA 78

                          90
                  ....*....|.
gi 47059159   126 NHVVEEYFVAP 136
Cdd:TIGR00135  79 PEKEDGFIKVP 89
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
55-136 7.88e-15

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 65.61  E-value: 7.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059159   55 IEHLERLALVNFgSREAVDR----LEKAIAFADQLHAVDTDGVEPLESVLeDRCLYLRSDNVAEGSCAEELLQNSNHVVE 130
Cdd:PRK00034   8 VKHLAKLARLEL-SEEELEKfagqLNKILDFVEQLNEVDTEGVEPTTHPL-DMKNVLREDVVTESLPREEALKNAPESED 85


                 ....*.
gi 47059159  131 EYFVAP 136
Cdd:PRK00034  86 GYFKVP 91
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 50-136 1.39e-14

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: 65.12  E-value: 1.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059159  50 VSPAVIEHLERLALVNFGSREA---VDRLEKAIAFADQLHAVDTDGVEPLESVLEDRcLYLRSDNVAEGSCAEELLQNSN 126
Cdd:COG0721   3 ITKEEVEHIAKLARLELSEEELerlAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLT-NVLREDEVTESLDREEALANAP 81

                        90
                ....*....|
gi 47059159 127 HVVEEYFVAP 136
Cdd:COG0721  82 ETEDGYFKVP 91
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 75-134 1.91e-11

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: 56.36  E-value: 1.91e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059159    75 LEKAIAFADQLHAVDTDGVEPLESVLEDrCLYLRSDNVAEGSCAEELLQNSNHVVEEYFV 134
Cdd:pfam02686  11 LNDILDYVEQLNEVDTEGVEPTSHPLDL-TNVLREDEVTESLDREEALANAPETEDGFFK 69
 
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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