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C5P8Q4

- MAP2_COCP7

UniProt

C5P8Q4 - MAP2_COCP7

Protein

Methionine aminopeptidase 2

Gene

CPC735_002850

Organism
Coccidioides posadasii (strain C735) (Valley fever fungus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 38 (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 sitei202 – 2021SubstrateUniRule annotation
    Metal bindingi222 – 2221Divalent metal cation 1UniRule annotation
    Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
    Metal bindingi233 – 2331Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi302 – 3021Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei310 – 3101SubstrateUniRule annotation
    Metal bindingi338 – 3381Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi433 – 4331Divalent metal cation 1UniRule annotation
    Metal bindingi433 – 4331Divalent 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:CPC735_002850
    OrganismiCoccidioides posadasii (strain C735) (Valley fever fungus)
    Taxonomic identifieri222929 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides
    ProteomesiUP000009084: 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 – 452452Methionine aminopeptidase 2PRO_0000407650Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi222929.C5P8Q4.

    Structurei

    3D structure databases

    ProteinModelPortaliC5P8Q4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi63 – 7917Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    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.

    C5P8Q4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVQALPEIN KLSVSEEGAA NAAAKGQAAQ GTAGNDDAEN DESDEDKEDE    50
    QEVADGAAAA GGKKKKKKTK KKKKKGTAKV QSDPPRVPLS TLFPNNNYPE 100
    GEIVEYKDDN AYRTTNEEKR YLDRMNNDFL TDYRKSAEIH RQVRQYAQKE 150
    LLKPGRSLTE IAEGIEDSVR ALTGHMGLEE GDSLVAGMGF PTGLNINHCA 200
    AHYSPNAGNK MVLQYGDVMK VDFGVHVNGR IVDSAFTVAF DPVYDNLLNA 250
    VKDATNTGIR EAGIDVRMSD IGAAIQETME SYEVEINGTI YPVKAIRNLN 300
    GHTIGHYLIH GGSTGKSVPI VKGGDQTKME EGETYAIETF GSTGKGFVRD 350
    DMEVSHYAKV PDAPNVPLRL SSAKNLLNVI TKNFGTLPFC RRYLDRLGQE 400
    KYLLGLNNLV SSGLVDAYPP LVDVKGSYTA QFEHTILLRP NVKEVITRGD 450
    DY 452
    Length:452
    Mass (Da):49,394
    Last modified:May 3, 2011 - v2
    Checksum:i9E4A3B36E989C61F
    GO

    Sequence cautioni

    The sequence EER26116.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    ACFW01000030 Genomic DNA. Translation: EER26116.1. Different initiation.
    RefSeqiXP_003068261.1. XM_003068215.1.
    UniGeneiCpo.1088.

    Genome annotation databases

    GeneIDi9693744.
    KEGGicpw:CPC735_002850.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    ACFW01000030 Genomic DNA. Translation: EER26116.1 . Different initiation.
    RefSeqi XP_003068261.1. XM_003068215.1.
    UniGenei Cpo.1088.

    3D structure databases

    ProteinModelPortali C5P8Q4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 222929.C5P8Q4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 9693744.
    KEGGi cpw:CPC735_002850.

    Phylogenomic databases

    eggNOGi COG0024.
    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: C735.

    Entry informationi

    Entry nameiMAP2_COCP7
    AccessioniPrimary (citable) accession number: C5P8Q4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 38 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