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{
    "metadata": {
        "accession": "P00959",
        "id": "SYM_ECOLI",
        "source_organism": {
            "taxId": "83333",
            "scientificName": "Escherichia coli (strain K12)",
            "fullName": "Escherichia coli (strain K12)"
        },
        "name": "Methionine--tRNA ligase",
        "description": [
            "Catalyzes the attachment of L-methionine to tRNA(Met) (PubMed:216545, PubMed:367445, PubMed:4297674, PubMed:4581817, PubMed:7932711). Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (PubMed:216545, PubMed:4581817). MetRS can indeed attach methionine to tRNA(mMet), which supplies methionine for elongation of nascent peptides, and to tRNA(fMet), which supplies formylmethionine for initiation of peptide synthesis (PubMed:216545, PubMed:4581817). However, MetRS charges tRNA(fMet) with a greater efficiency than tRNA(mMet) in several strains of E.coli, suggesting a preference for initiation of new peptides (PubMed:216545). Cannot use D-methionine (PubMed:4297674)",
            "In addition, MetRS can reject misactivated homocysteine by a tRNA-independent hydrolysis of the homocysteinyl-AMP intermediate, preventing incorporation of homocysteine into tRNA and proteins (PubMed:2191291, PubMed:7024910). The homocysteinyl-AMP intermediate undergoes an intramolecular cyclization reaction in which the thiolate side chain of homocysteine displaces the AMP group, forming homocysteine-thiolactone and AMP (PubMed:2191291, PubMed:7024910)"
        ],
        "length": 677,
        "sequence": "MTQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPKLTERAEAFLNTELTWDGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASKEEVKAAAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDAGAKPGHQVK",
        "proteome": "UP000000625",
        "gene": "metG",
        "go_terms": [
            {
                "identifier": "GO:0004825",
                "name": "methionine-tRNA ligase activity",
                "category": {
                    "code": "F",
                    "name": "molecular_function"
                }
            },
            {
                "identifier": "GO:0006431",
                "name": "methionyl-tRNA aminoacylation",
                "category": {
                    "code": "P",
                    "name": "biological_process"
                }
            },
            {
                "identifier": "GO:0000166",
                "name": "nucleotide binding",
                "category": {
                    "code": "F",
                    "name": "molecular_function"
                }
            },
            {
                "identifier": "GO:0004812",
                "name": "aminoacyl-tRNA ligase activity",
                "category": {
                    "code": "F",
                    "name": "molecular_function"
                }
            },
            {
                "identifier": "GO:0005524",
                "name": "ATP binding",
                "category": {
                    "code": "F",
                    "name": "molecular_function"
                }
            },
            {
                "identifier": "GO:0006418",
                "name": "tRNA aminoacylation for protein translation",
                "category": {
                    "code": "P",
                    "name": "biological_process"
                }
            },
            {
                "identifier": "GO:0000049",
                "name": "tRNA binding",
                "category": {
                    "code": "F",
                    "name": "molecular_function"
                }
            }
        ],
        "protein_evidence": 1,
        "source_database": "reviewed",
        "is_fragment": false,
        "in_alphafold": true,
        "in_bfvd": false,
        "ida_accession": "605e59fa9284a45ce9616dfe8a2213f70331198f",
        "counters": {
            "domain_architectures": 13265,
            "entries": 34,
            "isoforms": 0,
            "proteomes": 1,
            "sets": 6,
            "structures": 24,
            "taxa": 1,
            "dbEntries": {
                "ssf": 4,
                "cdd": 3,
                "cathgene3d": 4,
                "pfam": 3,
                "profile": 1,
                "panther": 1,
                "ncbifam": 3,
                "hamap": 1,
                "prosite": 1,
                "prints": 1,
                "interpro": 12
            },
            "proteome": 1,
            "taxonomy": 1,
            "similar_proteins": 13265
        }
    }
}