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Conserved domains on  [gi|499661185|ref|WP_011341919|]
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Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC [Syntrophotalea carbinolica]

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 ...
 1-95 2.31e-43

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: 136.00  E-value: 2.31e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185  1 MKINREQVEHVARLARLALSEDELASLTDDMDAILGYVEKLNELDTDHIIPTAHAVPVENAFREDCAGSSIGTDKALQNA 80
Cdd:COG0721   1 MSITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANA 80

                        90
                ....*....|....*
gi 499661185 81 PEASDNCFVVPKVIE 95
Cdd:COG0721  81 PETEDGYFKVPKVIE 95
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 1-95 2.31e-43

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: 136.00  E-value: 2.31e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185  1 MKINREQVEHVARLARLALSEDELASLTDDMDAILGYVEKLNELDTDHIIPTAHAVPVENAFREDCAGSSIGTDKALQNA 80
Cdd:COG0721   1 MSITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANA 80

                        90
                ....*....|....*
gi 499661185 81 PEASDNCFVVPKVIE 95
Cdd:COG0721  81 PETEDGYFKVPKVIE 95
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
1-95 2.04e-37

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 120.69  E-value: 2.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185  1 MKINREQVEHVARLARLALSEDELASLTDDMDAILGYVEKLNELDTDHIIPTAHAVPVENAFREDCAGSSIGTDKALQNA 80
Cdd:PRK00034  1 MAITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTESLPREEALKNA 80

                        90
                ....*....|....*
gi 499661185 81 PEASDNCFVVPKVIE 95
Cdd:PRK00034 81 PESEDGYFKVPKVIE 95
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 3-95 1.31e-29

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: 101.22  E-value: 1.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185   3 INREQVEHVARLARLALSEDELASLTDDMDAILGYVEKLNELDTDHIIPTAHAVPVENAFREDCAGSSIGTDKALQNAPE 82
Cdd:TIGR00135  1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDEPEEPLSRDDILKNAPE 80

                         90
                 ....*....|...
gi 499661185  83 ASDNCFVVPKVIE 95
Cdd:TIGR00135 81 KEDGFIKVPKIIE 93
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 21-90 1.94e-25

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: 89.88  E-value: 1.94e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185  21 EDELASLTDDMDAILGYVEKLNELDTDHIIPTAHAVPVENAFREDCAGSSIGTDKALQNAPEASDNCFVV 90
Cdd:pfam02686  1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLTNVLREDEVTESLDREEALANAPETEDGFFKV 70
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 1-95 2.31e-43

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: 136.00  E-value: 2.31e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185  1 MKINREQVEHVARLARLALSEDELASLTDDMDAILGYVEKLNELDTDHIIPTAHAVPVENAFREDCAGSSIGTDKALQNA 80
Cdd:COG0721   1 MSITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANA 80

                        90
                ....*....|....*
gi 499661185 81 PEASDNCFVVPKVIE 95
Cdd:COG0721  81 PETEDGYFKVPKVIE 95
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
1-95 2.04e-37

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 120.69  E-value: 2.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185  1 MKINREQVEHVARLARLALSEDELASLTDDMDAILGYVEKLNELDTDHIIPTAHAVPVENAFREDCAGSSIGTDKALQNA 80
Cdd:PRK00034  1 MAITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTESLPREEALKNA 80

                        90
                ....*....|....*
gi 499661185 81 PEASDNCFVVPKVIE 95
Cdd:PRK00034 81 PESEDGYFKVPKVIE 95
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 3-95 1.31e-29

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: 101.22  E-value: 1.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185   3 INREQVEHVARLARLALSEDELASLTDDMDAILGYVEKLNELDTDHIIPTAHAVPVENAFREDCAGSSIGTDKALQNAPE 82
Cdd:TIGR00135  1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDEPEEPLSRDDILKNAPE 80

                         90
                 ....*....|...
gi 499661185  83 ASDNCFVVPKVIE 95
Cdd:TIGR00135 81 KEDGFIKVPKIIE 93
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 21-90 1.94e-25

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: 89.88  E-value: 1.94e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185  21 EDELASLTDDMDAILGYVEKLNELDTDHIIPTAHAVPVENAFREDCAGSSIGTDKALQNAPEASDNCFVV 90
Cdd:pfam02686  1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLTNVLREDEVTESLDREEALANAPETEDGFFKV 70
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 5-95 3.58e-04

bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 37.66  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185   5 REQVEHVARLARLALSEDELASLTDDMDAILGYVEKLNELDTDHIiPTAHAVPVENAFREDCAG---SSIGTDKALQNAP 81
Cdd:PRK12820 614 EDLIDHLSWVSRIGFAEAERAAIESALADAEELAAQLEDIACDEE-PLFSPAPAANRMGEGLEArecSFAATGEILKNAP 692

                         90
                 ....*....|....
gi 499661185  82 EASDNCFVVPKVIE 95
Cdd:PRK12820 693 AVKGDYFKVAGILD 706
PRK12821 PRK12821
aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional
 2-84 2.14e-03

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


Pssm-ID: 237216 [Multi-domain]  Cd Length: 477  Bit Score: 35.64  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499661185   2 KINREQVEHVARLARLALSEDELASLTDDMDAILGYVEKLNELDTDHIIPTAHavPVENA---FREDCAGSSIGTDKALQ 78
Cdd:PRK12821 388 QLNKDELKKLARLVMFDLDDAELEKLQVEFKDITSSFKQVEKIDTTNVKPMYA--PFSNSptpLRKDKDVVQKHQKILLK 465


                 ....*.
gi 499661185  79 NAPEAS 84
Cdd:PRK12821 466 NCKETL 471
 
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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