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B1L8W7

- FMT_THESQ

UniProt

B1L8W7 - FMT_THESQ

Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Thermotoga sp. (strain RQ2)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      Previous versions | rss
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    Functioni

    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.UniRule annotation

    Catalytic activityi

    10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).UniRule annotation

    GO - Molecular functioni

    1. methionyl-tRNA formyltransferase activity Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    BioCyciTSP126740:GH49-415-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionyl-tRNA formyltransferaseUniRule annotation (EC:2.1.2.9UniRule annotation)
    Gene namesi
    Name:fmtUniRule annotation
    Ordered Locus Names:TRQ2_0409
    OrganismiThermotoga sp. (strain RQ2)
    Taxonomic identifieri126740 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000001687: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Methionyl-tRNA formyltransferasePRO_1000098454Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi126740.TRQ2_0409.

    Structurei

    3D structure databases

    ProteinModelPortaliB1L8W7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni109 – 1124Tetrahydrofolate (THF) bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the Fmt family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0223.
    HOGENOMiHOG000261177.
    KOiK00604.
    OMAiQRFKIYE.
    OrthoDBiEOG6B09WV.

    Family and domain databases

    Gene3Di3.10.25.10. 1 hit.
    3.40.50.170. 1 hit.
    HAMAPiMF_00182. Formyl_trans.
    InterProiIPR005794. Fmt.
    IPR005793. Formyl_trans_C.
    IPR002376. Formyl_transf_N.
    IPR011034. Formyl_transferase_C-like.
    IPR015518. Met_tRNA_Form_TA-like.
    [Graphical view]
    PANTHERiPTHR11138. PTHR11138. 1 hit.
    PfamiPF02911. Formyl_trans_C. 1 hit.
    PF00551. Formyl_trans_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50486. SSF50486. 1 hit.
    SSF53328. SSF53328. 1 hit.
    TIGRFAMsiTIGR00460. fmt. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    B1L8W7-1 [UniParc]FASTAAdd to Basket

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    MRIVFVGTPE FAAEILEHLI KNGFNVVGVV TQPDKPRGRG RKVEPTPVKV    50
    VAEKHRVPFI QPESINKKEA LEFLRSVGPD VIIVASYGKI LGEKVLSLPS 100
    LGCYNIHPSL LPKYRGASPI QRVLENGEER TGVTIYKMVR ELDAGPIALQ 150
    REISIDPFET FDQLEKRLIE LSKEMSIEFL EKLKVGDIEL KEQDHSRATY 200
    APMIKKEDLI VDFSKDAESV KNKIRAYDSR PGARAFLGND EVKLFGVTAI 250
    DSSGDEPGLI HYIDREGAWI GTGKGMVKVK YLQLPGKKKL TFWELRNGRL 300
    IEEGMKLEGR YES 313
    Length:313
    Mass (Da):35,216
    Last modified:April 29, 2008 - v1
    Checksum:i48055C0CDEF4FD92
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000969 Genomic DNA. Translation: ACB08765.1.
    RefSeqiWP_012310526.1. NC_010483.1.
    YP_001738448.1. NC_010483.1.

    Genome annotation databases

    EnsemblBacteriaiACB08765; ACB08765; TRQ2_0409.
    GeneIDi6091814.
    KEGGitrq:TRQ2_0409.
    PATRICi23947331. VBITheSp108950_0414.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000969 Genomic DNA. Translation: ACB08765.1 .
    RefSeqi WP_012310526.1. NC_010483.1.
    YP_001738448.1. NC_010483.1.

    3D structure databases

    ProteinModelPortali B1L8W7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 126740.TRQ2_0409.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB08765 ; ACB08765 ; TRQ2_0409 .
    GeneIDi 6091814.
    KEGGi trq:TRQ2_0409.
    PATRICi 23947331. VBITheSp108950_0414.

    Phylogenomic databases

    eggNOGi COG0223.
    HOGENOMi HOG000261177.
    KOi K00604.
    OMAi QRFKIYE.
    OrthoDBi EOG6B09WV.

    Enzyme and pathway databases

    BioCyci TSP126740:GH49-415-MONOMER.

    Family and domain databases

    Gene3Di 3.10.25.10. 1 hit.
    3.40.50.170. 1 hit.
    HAMAPi MF_00182. Formyl_trans.
    InterProi IPR005794. Fmt.
    IPR005793. Formyl_trans_C.
    IPR002376. Formyl_transf_N.
    IPR011034. Formyl_transferase_C-like.
    IPR015518. Met_tRNA_Form_TA-like.
    [Graphical view ]
    PANTHERi PTHR11138. PTHR11138. 1 hit.
    Pfami PF02911. Formyl_trans_C. 1 hit.
    PF00551. Formyl_trans_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50486. SSF50486. 1 hit.
    SSF53328. SSF53328. 1 hit.
    TIGRFAMsi TIGR00460. fmt. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RQ2.

    Entry informationi

    Entry nameiFMT_THESQ
    AccessioniPrimary (citable) accession number: B1L8W7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 47 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3