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C4YSA9

- MAP2_CANAW

UniProt

C4YSA9 - MAP2_CANAW

Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Candida albicans (strain WO-1) (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 34 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      Previous versions | rss
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    • Comment

    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 sitei198 – 1981SubstrateUniRule annotation
    Metal bindingi218 – 2181Divalent metal cation 1UniRule annotation
    Metal bindingi229 – 2291Divalent metal cation 1UniRule annotation
    Metal bindingi229 – 2291Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi300 – 3001Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei308 – 3081SubstrateUniRule annotation
    Metal bindingi333 – 3331Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi428 – 4281Divalent metal cation 1UniRule annotation
    Metal bindingi428 – 4281Divalent 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
    Name:MAP2UniRule annotation
    ORF Names:CAWG_04971
    OrganismiCandida albicans (strain WO-1) (Yeast)
    Taxonomic identifieri294748 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000001429: Chromosome 6

    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 – 447447Methionine aminopeptidase 2PRO_0000407645Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliC4YSA9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi71 – 8515Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000226278.
    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.

    C4YSA9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGATEGEDT KVIESKINEL NIDKPKLEDN NEAKGNGNGN ESGGDDDDDK    50
    EDDDDNDEIT EPSTSTSSGD KKKKKNKNKK KKKKKIVSID SSYPEGIFPE 100
    GQWMEYPLED INSYRTTSEE KRYLDRQQNN KWQDFRKGAE IHRRVRHKAQ 150
    SSIRPGMTMI EIANLIEDSV RNYSGNDHTL KAGIGFPTGL SLNHVAAHYT 200
    PNTGDKLILK KDDIMKVDIG VHVNGRICDS AFTMTFNEDG KYDTIMQAVK 250
    EATYTGIKES GIDVRLNDIG AAIQEVMESY EMEENGKTYP IKCIKNLNGH 300
    NIDDFVIHSG KSVPIIANGD MTKMEEGETF AIETFGSTGN GYVLPEGECS 350
    HYAMNKGVEH LKPPSERSKQ LLETIKQNFG TLPWCRRYLE RTGEEKYLFA 400
    LNQLVRHGIV EEYPPIVDKR GSYTAQFEHT ILLHPHKKEV VTKGDDY 447
    Length:447
    Mass (Da):50,409
    Last modified:July 28, 2009 - v1
    Checksum:iEE7A3DE5AC911CD5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM000312 Genomic DNA. Translation: EEQ46612.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CM000312 Genomic DNA. Translation: EEQ46612.1 .

    3D structure databases

    ProteinModelPortali C4YSA9.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOGENOMi HOG000226278.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: WO-1.

    Entry informationi

    Entry nameiMAP2_CANAW
    AccessioniPrimary (citable) accession number: C4YSA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 34 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