| Accession | TIGR00135 |
| Name | gatC |
| Function | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit |
| Gene Symbol | gatC |
| Trusted Cutoff | 47.10 |
| Domain Trusted Cutoff | 47.10 |
| Noise Cutoff | 29.35 |
| Domain Noise Cutoff | 29.35 |
| Isology Type | equivalog |
| EC Number | 6.3.5.- |
| HMM Length | 93 |
| Mainrole Category | Protein synthesis |
| Subrole Category | tRNA aminoacylation |
| Gene Ontology Term | GO:0006424: glutamyl-tRNA aminoacylation biological_process |
| | GO:0030956: glutamyl-tRNA(Gln) amidotransferase complex cellular_component |
| | GO:0050567: glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity molecular_function |
| Author | Haft DH |
| Entry Date | Apr 20 1999 2:07PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | 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 HMM 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 HMM has been revised to remove the candidate sequence from Methanococcus jannaschii, now part of a related model. |
| References | DR Proc Natl Acad Sci USA 94, 11819-11826, 1997
SE TIGR
AL clustalw, belvu, seaview
DR HAMAP; MF_00122; 324 of 325 |
| Genome Property | GenProp0188: GatABC aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase complex (HMM) |
| | GenProp0258: tRNA aminoacylation (HMM) |
| | GenProp0258: tRNA aminoacylation (HMM) |
