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Conserved domains on  [gi|490165356|ref|WP_004064004|]
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MULTISPECIES: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC [Haloferax]

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 ...
6-91 2.20e-31

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: 105.56  E-value: 2.20e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490165356  6 VDADEVRHVAELARVDLDEDEVEEFAAQFADILGYFDALDEVPEVDRE-----DELVNVMRPDEVRDGLTQEEALSNAAE 80
Cdd:COG0721   3 ITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEptahpLDLTNVLREDEVTESLDREEALANAPE 82
                        90
                ....*....|.
gi 490165356 81 TEDGFFKGPRV 91
Cdd:COG0721  83 TEDGYFKVPKV 93
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
6-91 2.20e-31

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: 105.56  E-value: 2.20e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490165356  6 VDADEVRHVAELARVDLDEDEVEEFAAQFADILGYFDALDEVPEVDRE-----DELVNVMRPDEVRDGLTQEEALSNAAE 80
Cdd:COG0721   3 ITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEptahpLDLTNVLREDEVTESLDREEALANAPE 82
                        90
                ....*....|.
gi 490165356 81 TEDGFFKGPRV 91
Cdd:COG0721  83 TEDGYFKVPKV 93
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
6-91 7.91e-26

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 91.42  E-value: 7.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490165356  6 VDADEVRHVAELARVDLDEDEVEEFAAQFADILGYFDALDE-----VPEVDREDELVNVMRPDEVRDGLTQEEALSNAAE 80
Cdd:PRK00034  3 ITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEvdtegVEPTTHPLDMKNVLREDVVTESLPREEALKNAPE 82
                        90
                ....*....|.
gi 490165356 81 TEDGFFKGPRV 91
Cdd:PRK00034 83 SEDGYFKVPKV 93
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
6-91 2.58e-22

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: 82.35  E-value: 2.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490165356   6 VDADEVRHVAELARVDLDEDEVEEFAAQFADILGYFDALDEVPEVDRED-----ELVNVMRPDEVRDGLTQEEALSNAAE 80
Cdd:TIGR00135  1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPmthplEISNVLREDEPEEPLSRDDILKNAPE 80
                         90
                 ....*....|.
gi 490165356  81 TEDGFFKGPRV 91
Cdd:TIGR00135 81 KEDGFIKVPKI 91
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
24-87 1.79e-17

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: 69.46  E-value: 1.79e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490165356  24 EDEVEEFAAQFADILGYFDALDE-----VPEVDREDELVNVMRPDEVRDGLTQEEALSNAAETEDGFFK 87
Cdd:pfam02686  1 EEELEEFAKQLNDILDYVEQLNEvdtegVEPTSHPLDLTNVLREDEVTESLDREEALANAPETEDGFFK 69
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
6-91 2.20e-31

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: 105.56  E-value: 2.20e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490165356  6 VDADEVRHVAELARVDLDEDEVEEFAAQFADILGYFDALDEVPEVDRE-----DELVNVMRPDEVRDGLTQEEALSNAAE 80
Cdd:COG0721   3 ITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEptahpLDLTNVLREDEVTESLDREEALANAPE 82
                        90
                ....*....|.
gi 490165356 81 TEDGFFKGPRV 91
Cdd:COG0721  83 TEDGYFKVPKV 93
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
6-91 7.91e-26

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 91.42  E-value: 7.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490165356  6 VDADEVRHVAELARVDLDEDEVEEFAAQFADILGYFDALDE-----VPEVDREDELVNVMRPDEVRDGLTQEEALSNAAE 80
Cdd:PRK00034  3 ITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEvdtegVEPTTHPLDMKNVLREDVVTESLPREEALKNAPE 82
                        90
                ....*....|.
gi 490165356 81 TEDGFFKGPRV 91
Cdd:PRK00034 83 SEDGYFKVPKV 93
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
6-91 2.58e-22

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: 82.35  E-value: 2.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490165356   6 VDADEVRHVAELARVDLDEDEVEEFAAQFADILGYFDALDEVPEVDRED-----ELVNVMRPDEVRDGLTQEEALSNAAE 80
Cdd:TIGR00135  1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPmthplEISNVLREDEPEEPLSRDDILKNAPE 80
                         90
                 ....*....|.
gi 490165356  81 TEDGFFKGPRV 91
Cdd:TIGR00135 81 KEDGFIKVPKI 91
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
24-87 1.79e-17

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: 69.46  E-value: 1.79e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490165356  24 EDEVEEFAAQFADILGYFDALDE-----VPEVDREDELVNVMRPDEVRDGLTQEEALSNAAETEDGFFK 87
Cdd:pfam02686  1 EEELEEFAKQLNDILDYVEQLNEvdtegVEPTSHPLDLTNVLREDEVTESLDREEALANAPETEDGFFK 69
PRK12821 PRK12821
aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional
9-87 5.24e-05

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


Pssm-ID: 237216 [Multi-domain]  Cd Length: 477  Bit Score: 39.88  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490165356   9 DEVRHVAELARVDLDEDEVEEFAAQFADILGYFDALDEVPEVDRE------DELVNVMRPDEVRDGLTQEEALSNAAETE 82
Cdd:PRK12821 392 DELKKLARLVMFDLDDAELEKLQVEFKDITSSFKQVEKIDTTNVKpmyapfSNSPTPLRKDKDVVQKHQKILLKNCKETL 471

                 ....*
gi 490165356  83 DGFFK 87
Cdd:PRK12821 472 GGFVK 476
 
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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