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A0L3X7

- FMT_MAGSM

UniProt

A0L3X7 - FMT_MAGSM

Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Magnetococcus sp. (strain MC-1)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (12 Dec 2006)
      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

    BioCyciMSP156889:GH36-144-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:Mmc1_0143
    OrganismiMagnetococcus sp. (strain MC-1)
    Taxonomic identifieri156889 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus
    ProteomesiUP000002586: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 312312Methionyl-tRNA formyltransferasePRO_1000098416Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi156889.Mmc1_0143.

    Structurei

    3D structure databases

    ProteinModelPortaliA0L3X7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni112 – 1154Tetrahydrofolate (THF) bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the Fmt family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0223.
    HOGENOMiHOG000261177.
    KOiK00604.
    OMAiKAQAQNE.
    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.

    A0L3X7-1 [UniParc]FASTAAdd to Basket

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    MTAWRVVFMG TPDFATGTLQ ALLDGPDTVV AVFTQPDKPV GRGMKMQKTP    50
    VKQLAEQHGI PVYQPNRLRE AEAVTALRAL RPDVVVVVAY GQILSREVLE 100
    IPTHGCINVH ASLLPRWRGA APIQRAILAG DAQSGVTIMA MEEGLDTGPM 150
    YSTVVQSIDN HTTGGQLHDQ LMAAGGGLLV ETLARIKHEG LTPQIQPEQG 200
    VTYAAKLKKE EGLVDWSQPA IQIQRAVQAF DPWPCAFTLW QGKPLKLFAA 250
    SVVVGHGTPG EVIEVEKDGF VVACGDGALR VAQVQAAGKK RMSSGEWLRG 300
    HGVKQGERLG EG 312
    Length:312
    Mass (Da):33,499
    Last modified:December 12, 2006 - v1
    Checksum:i65CF1B00BBCB1028
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000471 Genomic DNA. Translation: ABK42670.1.
    RefSeqiYP_864076.1. NC_008576.1.

    Genome annotation databases

    EnsemblBacteriaiABK42670; ABK42670; Mmc1_0143.
    GeneIDi4480997.
    KEGGimgm:Mmc1_0143.
    PATRICi22426740. VBIMagSp23654_0141.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000471 Genomic DNA. Translation: ABK42670.1 .
    RefSeqi YP_864076.1. NC_008576.1.

    3D structure databases

    ProteinModelPortali A0L3X7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 156889.Mmc1_0143.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK42670 ; ABK42670 ; Mmc1_0143 .
    GeneIDi 4480997.
    KEGGi mgm:Mmc1_0143.
    PATRICi 22426740. VBIMagSp23654_0141.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci MSP156889:GH36-144-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: MC-1.

    Entry informationi

    Entry nameiFMT_MAGSM
    AccessioniPrimary (citable) accession number: A0L3X7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 55 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3