SPM_000260
  | Uniprot: A0A037UKU8
Description: methionyl-tRNA formyltransferase EC number: 2.1.2.9 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS00325839}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by: (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP. {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS00381977}. Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): fmt Gene names (synonym): Mass: 35,844 Subunit structure [CC]: Gene ontology (GO): methionyl-tRNA formyltransferase activity [GO:0004479] Gene ontology IDs: GO:0004479 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the Fmt family. {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS00569886}. Protein families: Fmt family Coiled coil: Domain [FT]: DOMAIN 5 172 Formyl_trans_N. {ECO:0000259|Pfam:PF00551}.; DOMAIN 206 306 Formyl_trans_C. {ECO:0000259|Pfam:PF02911}. Motif: Region: REGION 112 115 Tetrahydrofolate (THF) binding. {ECO:0000256|HAMAP-Rule:MF_00182}. EMBL: AGBZ02000001 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI92549 UniPathway: CDD: Gene3D: HAMAP: 3.10.25.10;3.40.50.170 InterPro: MF_00182 PANTHER: IPR005794;IPR005793;IPR002376;IPR011034;IPR001555 PIRSF: PRINTS: PROSITE: Pfam: PS00373 ProDom: PF02911;PF00551 SMART: SUPFAM: TIGRFAMs: SSF50486;SSF53328 |
51353-52313(-) >nucleotide sequence ATCAGTTGCTTTTTTACCTTCGCGTTGTAAACGCGTAATTAATAAATAACCATCTTCAAC TTTAACTTTAATCCCTAATTTTGAAATATCAATAATTGTTCCATTTACAAAATCAGCGTC TTTTTCAGCTAATGGTTCTAAGGTAATCACTGCTTGATGCAATTTATAATGAATATTATT AACAGTTGTGTAAGCAATTGGTCATGCATATAAACCACGAATTTGATCAACAATTTTTTG TTTTGGTAAAAATCAATTCACTTTTTCTTCATCGCGGGTAATGTTATAAGCAAATGTTGC TTGACTATCATCTTGTGGTGTTCCCTTAATTTTGCCAGTAATAATATCTAATAAATGCTT TTCAATCATTGTTCCTGCTAAAACCATTAAACGGTCATGCAAAGATGAAGCTGTTTCCGT TGGACTAATTGGAATTGCTGTTTGAACATACATTTCGCCCGCATCCATTTTTTTAATCAT TTGCATTAGCGTAATCCCAGTTTCTTGTTCACCATAAATAATAGCTTTATGAATGGGAGC ACCACCACGTAATTTTGGTAATAACGAAGCATGAACATTAATACAATTAATCCGGGCTAA TTTTAAAATTCGCTCTGGAATAAACTGCCCATAAGCACATGTCACAATAACATCTGGTTG CAAAGTGACTAACTCTGCATAAAGATCATTAATTTTTTCTGGTTGAAAAACAGGAATTTG ATTTGTTAAAGCAAATTCTTTTACTGGGGAAAATTGAACAAGTTGTTGCCGTCCAATTTT TCGATCAGGTTGGGTAACAATCCCAATTATTTCAATTGTTGGACTTAACTTTTGCAAAGC CTTTAAAACAGCTGTCGCAAAGATTGGTGTTCCCATAAAAATCACTCTATATTTTTGCAT >protein sequence QIPVFQPEKINDLYAELVTLQPDVIVTCAYGQFIPERILKLARINCINVHASLLPKLRGG APIHKAIIYGEQETGITLMQMIKKMDAGEMYVQTAIPISPTETASSLHDRLMVLAGTMIE KHLLDIITGKIKGTPQDDSQATFAYNITRDEEKVNWFLPKQKIVDQIRGLYAWPIAYTTV NNIHYKLHQAVITLEPLAEKDADFVNGTIIDISKLGIKVKVEDGYLLITRLQREGKKATD AKNYYHNASSEIIVGNIFI |
© Fisunov Lab of Proteomics, 2016.