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Conserved domains on  [gi|50978624|ref|NP_789788|]
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glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial [Homo sapiens]

Protein Classification

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC( domain architecture ID 10011107)

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 PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
31-118 5.21e-17

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


:

Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 70.61  E-value: 5.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50978624   31 RITAAVIEHLERLALVDFGSREA---VARLEKAIAFADRLRAVDTDGVEPMESVLeDRCLYLRSDNVVEGNCADELLQNS 107
Cdd:PRK00034   2 AITREEVKHLAKLARLELSEEELekfAGQLNKILDFVEQLNEVDTEGVEPTTHPL-DMKNVLREDVVTESLPREEALKNA 80

                         90
                 ....*....|.
gi 50978624  108 HRVVEEYFVAP 118
Cdd:PRK00034  81 PESEDGYFKVP 91
 
Name Accession Description Interval E-value
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
31-118 5.21e-17

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 70.61  E-value: 5.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50978624   31 RITAAVIEHLERLALVDFGSREA---VARLEKAIAFADRLRAVDTDGVEPMESVLeDRCLYLRSDNVVEGNCADELLQNS 107
Cdd:PRK00034   2 AITREEVKHLAKLARLELSEEELekfAGQLNKILDFVEQLNEVDTEGVEPTTHPL-DMKNVLREDVVTESLPREEALKNA 80

                         90
                 ....*....|.
gi 50978624  108 HRVVEEYFVAP 118
Cdd:PRK00034  81 PESEDGYFKVP 91
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 32-118 8.63e-17

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: 70.13  E-value: 8.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50978624  32 ITAAVIEHLERLALVDFGSREA---VARLEKAIAFADRLRAVDTDGVEPMESVLEDRcLYLRSDNVVEGNCADELLQNSH 108
Cdd:COG0721   3 ITKEEVEHIAKLARLELSEEELerlAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLT-NVLREDEVTESLDREEALANAP 81

                        90
                ....*....|
gi 50978624 109 RVVEEYFVAP 118
Cdd:COG0721  82 ETEDGYFKVP 91
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 32-118 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: 67.32  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50978624    32 ITAAVIEHLERLALVDFGSREA---VARLEKAIAFADRLRAVDTDGVEPMESVLEDrCLYLRSDNVVEGNCADELLQNSH 108
Cdd:TIGR00135   1 ISDEEVKHLAKLARLELSEEEAesfAGDLDKILGFVEQLNEVDTENVEPMTHPLEI-SNVLREDEPEEPLSRDDILKNAP 79

                          90
                  ....*....|
gi 50978624   109 RVVEEYFVAP 118
Cdd:TIGR00135  80 EKEDGFIKVP 89
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 57-116 8.25e-13

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: 59.06  E-value: 8.25e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50978624    57 LEKAIAFADRLRAVDTDGVEPMESVLEDrCLYLRSDNVVEGNCADELLQNSHRVVEEYFV 116
Cdd:pfam02686  11 LNDILDYVEQLNEVDTEGVEPTSHPLDL-TNVLREDEVTESLDREEALANAPETEDGFFK 69
 
Name Accession Description Interval E-value
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
31-118 5.21e-17

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 70.61  E-value: 5.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50978624   31 RITAAVIEHLERLALVDFGSREA---VARLEKAIAFADRLRAVDTDGVEPMESVLeDRCLYLRSDNVVEGNCADELLQNS 107
Cdd:PRK00034   2 AITREEVKHLAKLARLELSEEELekfAGQLNKILDFVEQLNEVDTEGVEPTTHPL-DMKNVLREDVVTESLPREEALKNA 80

                         90
                 ....*....|.
gi 50978624  108 HRVVEEYFVAP 118
Cdd:PRK00034  81 PESEDGYFKVP 91
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 32-118 8.63e-17

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: 70.13  E-value: 8.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50978624  32 ITAAVIEHLERLALVDFGSREA---VARLEKAIAFADRLRAVDTDGVEPMESVLEDRcLYLRSDNVVEGNCADELLQNSH 108
Cdd:COG0721   3 ITKEEVEHIAKLARLELSEEELerlAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLT-NVLREDEVTESLDREEALANAP 81

                        90
                ....*....|
gi 50978624 109 RVVEEYFVAP 118
Cdd:COG0721  82 ETEDGYFKVP 91
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 32-118 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: 67.32  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50978624    32 ITAAVIEHLERLALVDFGSREA---VARLEKAIAFADRLRAVDTDGVEPMESVLEDrCLYLRSDNVVEGNCADELLQNSH 108
Cdd:TIGR00135   1 ISDEEVKHLAKLARLELSEEEAesfAGDLDKILGFVEQLNEVDTENVEPMTHPLEI-SNVLREDEPEEPLSRDDILKNAP 79

                          90
                  ....*....|
gi 50978624   109 RVVEEYFVAP 118
Cdd:TIGR00135  80 EKEDGFIKVP 89
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 57-116 8.25e-13

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: 59.06  E-value: 8.25e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50978624    57 LEKAIAFADRLRAVDTDGVEPMESVLEDrCLYLRSDNVVEGNCADELLQNSHRVVEEYFV 116
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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