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Q9FCA2

- DEF2_STRCO

UniProt

Q9FCA2 - DEF2_STRCO

Protein

Peptide deformylase 2

Gene

def2

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      Previous versions | rss
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    Functioni

    Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.UniRule annotation

    Catalytic activityi

    Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.UniRule annotation

    Cofactori

    Binds 1 Fe2+ ion.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi104 – 1041IronUniRule annotation
    Metal bindingi146 – 1461IronUniRule annotation
    Active sitei147 – 1471UniRule annotation
    Metal bindingi150 – 1501IronUniRule annotation

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. peptide deformylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide deformylase 2UniRule annotation (EC:3.5.1.88UniRule annotation)
    Short name:
    PDF 2UniRule annotation
    Alternative name(s):
    Polypeptide deformylase 2UniRule annotation
    Gene namesi
    Name:def2UniRule annotation
    Ordered Locus Names:SCO1211
    ORF Names:2SCG58.11c
    OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    Taxonomic identifieri100226 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    ProteomesiUP000001973: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 179179Peptide deformylase 2PRO_0000082853Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi100226.SCO1211.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FCA2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243508.
    KOiK01462.
    OrthoDBiEOG664CMF.
    PhylomeDBiQ9FCA2.

    Family and domain databases

    Gene3Di3.90.45.10. 1 hit.
    HAMAPiMF_00163. Pep_deformylase.
    InterProiIPR000181. Fmet_deformylase.
    IPR023635. Peptide_deformylase.
    [Graphical view]
    PANTHERiPTHR10458. PTHR10458. 1 hit.
    PfamiPF01327. Pep_deformylase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004749. Pep_def. 1 hit.
    PRINTSiPR01576. PDEFORMYLASE.
    SUPFAMiSSF56420. SSF56420. 1 hit.
    TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9FCA2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRQGSIPGAH GRVRPLGLLG DPVLHARCAE VTDFGPELAA LVEDLFATMY    50
    AAHGVGLAAN QVGEAVRVFV YDCPDDEDER HLGHVVNPRL VETGGVVVRG 100
    PEGCLSLPGL EAGTERYDEA VVTGFTVAGE PVTVRGTGFF ARCLQHECDH 150
    LEGRVYADRL TGRRHRKLMR QVARASWHR 179
    Length:179
    Mass (Da):19,476
    Last modified:September 19, 2002 - v2
    Checksum:i8ABB3827812788F2
    GO

    Sequence cautioni

    The sequence CAC01493.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL939108 Genomic DNA. Translation: CAC01493.1. Different initiation.
    RefSeqiNP_625500.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAC01493; CAC01493; CAC01493.
    GeneIDi1096634.
    KEGGisco:SCO1211.
    PATRICi23731974. VBIStrCoe124346_1210.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL939108 Genomic DNA. Translation: CAC01493.1 . Different initiation.
    RefSeqi NP_625500.1. NC_003888.3.

    3D structure databases

    ProteinModelPortali Q9FCA2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 100226.SCO1211.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC01493 ; CAC01493 ; CAC01493 .
    GeneIDi 1096634.
    KEGGi sco:SCO1211.
    PATRICi 23731974. VBIStrCoe124346_1210.

    Phylogenomic databases

    eggNOGi COG0242.
    HOGENOMi HOG000243508.
    KOi K01462.
    OrthoDBi EOG664CMF.
    PhylomeDBi Q9FCA2.

    Family and domain databases

    Gene3Di 3.90.45.10. 1 hit.
    HAMAPi MF_00163. Pep_deformylase.
    InterProi IPR000181. Fmet_deformylase.
    IPR023635. Peptide_deformylase.
    [Graphical view ]
    PANTHERi PTHR10458. PTHR10458. 1 hit.
    Pfami PF01327. Pep_deformylase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF004749. Pep_def. 1 hit.
    PRINTSi PR01576. PDEFORMYLASE.
    SUPFAMi SSF56420. SSF56420. 1 hit.
    TIGRFAMsi TIGR00079. pept_deformyl. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-471 / A3(2) / M145.

    Entry informationi

    Entry nameiDEF2_STRCO
    AccessioniPrimary (citable) accession number: Q9FCA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 73 of the entry and version 2 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