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Q0UTI9

- MAP2_PHANO

UniProt

Q0UTI9 - MAP2_PHANO

Protein

Methionine aminopeptidase 2

Gene

SNOG_04925

Organism
Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).UniRule annotation

    Catalytic activityi

    Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

    Cofactori

    Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei199 – 1991SubstrateUniRule annotation
    Metal bindingi219 – 2191Divalent metal cation 1UniRule annotation
    Metal bindingi230 – 2301Divalent metal cation 1UniRule annotation
    Metal bindingi230 – 2301Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi299 – 2991Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei307 – 3071SubstrateUniRule annotation
    Metal bindingi332 – 3321Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi427 – 4271Divalent metal cation 1UniRule annotation
    Metal bindingi427 – 4271Divalent metal cation 2; catalyticUniRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-HAMAP
    2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. protein initiator methionine removal involved in protein maturation Source: EnsemblFungi

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2UniRule annotation
    Short name:
    MetAP 2UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    ORF Names:SNOG_04925
    OrganismiPhaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum)
    Taxonomic identifieri321614 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePhaeosphaeriaceaeParastagonospora
    ProteomesiUP000001055: Unassembled WGS sequence

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 435435Methionine aminopeptidase 2PRO_0000407662Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ0UTI9.
    SMRiQ0UTI9. Positions 77-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi55 – 617Poly-Lys
    Compositional biasi64 – 674Poly-Lys

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.UniRule annotation

    Phylogenomic databases

    KOiK01265.
    OMAiIQICEEL.
    OrthoDBiEOG7BGHW3.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_03175. MetAP_2_euk.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q0UTI9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQVADGVA DLKLDDTKSK PTNGTTQNGD AEHEDSDDDN EGEEGAAEGG    50
    EGAAKKKKKR KPRKKKKAGA AGASGPKTQT KPPRVPVHEI FLNDSYPEGE 100
    IHEYLNENSY RTTSEEKRHL DRMNNDFLTD YRRGAEIHRT VRQWARDWIK 150
    PGMSLTEIAE GIEDSVRALT GHQGLEDGDA QIAGMGFPTG LSINHCAAHY 200
    TPNAGNKMVV NYEDVMKVDF GVHINGRIVD SAFTLTFDPV YDNLVEACKA 250
    ATNAGIKEAG IDVRMSDIGA AIQEVMESYE VEIKGETFPV KCIRNLNGHS 300
    IGHYTIHGGK TVPIVKGGDQ TKMEEGETFA IETFGSTGKG YVRDDMETSH 350
    YAKRSDAPKV ALRVSSAKTL LNSITKNFGT LPFCRRYLDR LGHDKYLLGL 400
    NNLVSAGIVE AYPPLCDIKG SYTAQSEHVS FFPSV 435
    Length:435
    Mass (Da):47,572
    Last modified:September 5, 2006 - v1
    Checksum:i769B7666F52B14E4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH445331 Genomic DNA. Translation: EAT87316.1.
    RefSeqiXP_001795338.1. XM_001795286.1.

    Genome annotation databases

    EnsemblFungiiSNOT_04925; SNOT_04925; SNOG_04925.
    GeneIDi5972213.
    KEGGipno:SNOG_04925.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH445331 Genomic DNA. Translation: EAT87316.1 .
    RefSeqi XP_001795338.1. XM_001795286.1.

    3D structure databases

    ProteinModelPortali Q0UTI9.
    SMRi Q0UTI9. Positions 77-430.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SNOT_04925 ; SNOT_04925 ; SNOG_04925 .
    GeneIDi 5972213.
    KEGGi pno:SNOG_04925.

    Phylogenomic databases

    KOi K01265.
    OMAi IQICEEL.
    OrthoDBi EOG7BGHW3.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPi MF_03175. MetAP_2_euk.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10804:SF9. PTHR10804:SF9. 1 hit.
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 2 hits.
    TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
    PROSITEi PS01202. MAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum."
      Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P.
      Plant Cell 19:3347-3368(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

    Entry informationi

    Entry nameiMAP2_PHANO
    AccessioniPrimary (citable) accession number: Q0UTI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3