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Conserved domains on  [gi|2114425|gb|AAB66514|]
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similar to Synechocystis sp. hypothetical protein, encoded by GenBank Accession Number D64006 [Bacillus subtilis subsp. subtilis str. JH642]

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 ...
 4-96 2.63e-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: 135.61  E-value: 2.63e-43
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114425   4 ISIEEVKHVAHLARLAITEEEAKMFTEQLDSIISFAEELNEVNTDNVEPTTHVLKMKNVMREDEAGKGLPVEDVMKNAPD 83
Cdd:COG0721  3 ITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANAPE 82

                       90
               ....*....|...
gi 2114425  84 HKDGYIRVPSILD 96
Cdd:COG0721 83 TEDGYFKVPKVIE 95
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 4-96 2.63e-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: 135.61  E-value: 2.63e-43
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114425   4 ISIEEVKHVAHLARLAITEEEAKMFTEQLDSIISFAEELNEVNTDNVEPTTHVLKMKNVMREDEAGKGLPVEDVMKNAPD 83
Cdd:COG0721  3 ITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANAPE 82

                       90
               ....*....|...
gi 2114425  84 HKDGYIRVPSILD 96
Cdd:COG0721 83 TEDGYFKVPKVIE 95
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 4-96 9.91e-40

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: 126.64  E-value: 9.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114425     4 ISIEEVKHVAHLARLAITEEEAKMFTEQLDSIISFAEELNEVNTDNVEPTTHVLKMKNVMREDEAGKGLPVEDVMKNAPD 83
Cdd:TIGR00135  1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDEPEEPLSRDDILKNAPE 80

                         90
                 ....*....|...
gi 2114425    84 HKDGYIRVPSILD 96
Cdd:TIGR00135 81 KEDGFIKVPKIIE 93
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
2-96 2.42e-39

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 125.70  E-value: 2.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114425    2 SRISIEEVKHVAHLARLAITEEEAKMFTEQLDSIISFAEELNEVNTDNVEPTTHVLKMKNVMREDEAGKGLPVEDVMKNA 81
Cdd:PRK00034  1 MAITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTESLPREEALKNA 80

                        90
                ....*....|....*
gi 2114425   82 PDHKDGYIRVPSILD 96
Cdd:PRK00034 81 PESEDGYFKVPKVIE 95
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 22-91 1.81e-28

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: 97.58  E-value: 1.81e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114425    22 EEEAKMFTEQLDSIISFAEELNEVNTDNVEPTTHVLKMKNVMREDEAGKGLPVEDVMKNAPDHKDGYIRV 91
Cdd:pfam02686  1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLTNVLREDEVTESLDREEALANAPETEDGFFKV 70
 
Name Accession Description Interval E-value
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
 4-96 2.63e-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: 135.61  E-value: 2.63e-43
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114425   4 ISIEEVKHVAHLARLAITEEEAKMFTEQLDSIISFAEELNEVNTDNVEPTTHVLKMKNVMREDEAGKGLPVEDVMKNAPD 83
Cdd:COG0721  3 ITKEEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLTNVLREDEVTESLDREEALANAPE 82

                       90
               ....*....|...
gi 2114425  84 HKDGYIRVPSILD 96
Cdd:COG0721 83 TEDGYFKVPKVIE 95
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
 4-96 9.91e-40

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: 126.64  E-value: 9.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114425     4 ISIEEVKHVAHLARLAITEEEAKMFTEQLDSIISFAEELNEVNTDNVEPTTHVLKMKNVMREDEAGKGLPVEDVMKNAPD 83
Cdd:TIGR00135  1 ISDEEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEISNVLREDEPEEPLSRDDILKNAPE 80

                         90
                 ....*....|...
gi 2114425    84 HKDGYIRVPSILD 96
Cdd:TIGR00135 81 KEDGFIKVPKIIE 93
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
2-96 2.42e-39

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


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 125.70  E-value: 2.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114425    2 SRISIEEVKHVAHLARLAITEEEAKMFTEQLDSIISFAEELNEVNTDNVEPTTHVLKMKNVMREDEAGKGLPVEDVMKNA 81
Cdd:PRK00034  1 MAITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMKNVLREDVVTESLPREEALKNA 80

                        90
                ....*....|....*
gi 2114425   82 PDHKDGYIRVPSILD 96
Cdd:PRK00034 81 PESEDGYFKVPKVIE 95
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
 22-91 1.81e-28

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: 97.58  E-value: 1.81e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114425    22 EEEAKMFTEQLDSIISFAEELNEVNTDNVEPTTHVLKMKNVMREDEAGKGLPVEDVMKNAPDHKDGYIRV 91
Cdd:pfam02686  1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLTNVLREDEVTESLDREEALANAPETEDGFFKV 70
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 7-96 4.86e-05

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


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 40.35  E-value: 4.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114425     7 EEVKHVAHLARLAITEEEAKMFTEQLDSIISFAEELNEVNTDNvEPTTHVLKMKNVMREDEAGKGLPVE---DVMKNAPD 83
Cdd:PRK12820 615 DLIDHLSWVSRIGFAEAERAAIESALADAEELAAQLEDIACDE-EPLFSPAPAANRMGEGLEARECSFAatgEILKNAPA 693

                         90
                 ....*....|...
gi 2114425    84 HKDGYIRVPSILD 96
Cdd:PRK12820 694 VKGDYFKVAGILD 706
gatC_rel TIGR01827
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; This model represents a ...
 26-91 8.24e-03

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; This model represents a family small family related to GatC, the third subunit of an enzyme for completing the charging of tRNA(Gln) by amidating the Glu-tRNA(Gln). The few known archaea that contain a member of this family appear to produce Asn-tRNA(Asn) by an analogous amidotransferase reaction. This protein is proposed to substitute for GatC in the charging of both tRNAs.


Pssm-ID: 130886  Cd Length: 73  Bit Score: 32.22  E-value: 8.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2114425    26 KMFTEQLDSIISFAEELNEVNTdnVEPTTHVLKMKNVMREDEAGKGLP--VEDVMKNAPDHKDGYIRV 91
Cdd:TIGR01827  1 KILKEAEEILEEFSERLEDVDE--EEETYYISDGSNKFREDEEPRCDPefKKKMLENAPVSDDGYVVV 66
 
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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