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D4DE65

- MAP2_TRIVH

UniProt

D4DE65 - MAP2_TRIVH

Protein

Methionine aminopeptidase 2

Gene

TRV_05431

Organism
Trichophyton verrucosum (strain HKI 0517)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 32 (01 Oct 2014)
      Sequence version 2 (03 May 2011)
      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 bindingi335 – 3351Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi430 – 4301Divalent metal cation 1UniRule annotation
    Metal bindingi430 – 4301Divalent 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 Source: UniProtKB-HAMAP

    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:TRV_05431
    OrganismiTrichophyton verrucosum (strain HKI 0517)
    Taxonomic identifieri663202 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton
    ProteomesiUP000008383: 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 – 449449Methionine aminopeptidase 2PRO_0000407670Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliD4DE65.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi61 – 7616Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01265.
    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.

    D4DE65-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQAAPELA KLDLNKNTGS VEANAVSAGG SEKEEAENEG DSEDDRDDEQ    50
    AGGSAEVNAE KKKKKKRPKK KKKTAKVQSS PPRIPLTTLF PNNNFPEGEI 100
    VEYLNENSYR TTNEEKRHLD RMNNDFLTEY RQAAEIHRQV RQYAQKELIK 150
    PGATLTDIAE GIEDGVRHLT GHMGLEEGDS LVAGMGFPTG LNINHCAAHY 200
    SPNAGNKVVL QHGDVMKVDF GVHINGRIVD SAFTVAFDPV FDPLLTAVKE 250
    ATNTGIKEAG IDVRMSDIGA AIQETMESYE LELNGTSYPI KAIRNLNGHT 300
    IGQYEIHGGV NGKSVPIVKG GDQTKMEEGE TYAIETFGST GKGYVRDDME 350
    TSHYAKVPNA PSVPLRLSSA KNLYSLINKN FGTLPFCRRY LDRLGQEKYL 400
    LGLNNLVSSG LVDAYPPLCD VKGSYTAQFE HTILLRPNVK EVISRGDDY 449
    Length:449
    Mass (Da):49,232
    Last modified:May 3, 2011 - v2
    Checksum:i7CB3434189AF910B
    GO

    Sequence cautioni

    The sequence EFE39847.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    ACYE01000286 Genomic DNA. Translation: EFE39847.1. Sequence problems.
    RefSeqiXP_003020465.1. XM_003020419.1.

    Genome annotation databases

    GeneIDi9584204.
    KEGGitve:TRV_05431.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    ACYE01000286 Genomic DNA. Translation: EFE39847.1 . Sequence problems.
    RefSeqi XP_003020465.1. XM_003020419.1.

    3D structure databases

    ProteinModelPortali D4DE65.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 9584204.
    KEGGi tve:TRV_05431.

    Phylogenomic databases

    KOi K01265.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HKI 0517.

    Entry informationi

    Entry nameiMAP2_TRIVH
    AccessioniPrimary (citable) accession number: D4DE65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 32 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete 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