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B9WJA2

- MAP2_CANDC

UniProt

B9WJA2 - MAP2_CANDC

Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)
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 1 (24 Mar 2009)
      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 sitei203 – 2031SubstrateUniRule annotation
    Metal bindingi223 – 2231Divalent metal cation 1UniRule annotation
    Metal bindingi234 – 2341Divalent metal cation 1UniRule annotation
    Metal bindingi234 – 2341Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi305 – 3051Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei313 – 3131SubstrateUniRule 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
    Name:MAP2UniRule annotation
    ORF Names:CD36_64570
    OrganismiCandida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)
    Taxonomic identifieri573826 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000002605: 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 – 452452Methionine aminopeptidase 2PRO_0000407647Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi573826.CD36_64570.

    Structurei

    3D structure databases

    ProteinModelPortaliB9WJA2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi74 – 9017Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    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.

    B9WJA2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTGVTGTEDT KVIESKINEL NIDKSKPEKT NKVNKSDDVD NDDVDNDDND    50
    DEDNDDDDDE ITESGNSASS SGDKKKKKNK NKNKKKKKKK IISIDSSYPE 100
    GIFPEGQWME YPLEDINSYR ITSEEKRYLD RQQNNKWQDF RKGAEIHRRV 150
    RHKAQSSIKP GMTMIEIANL IEDSIRNYSN NDHTLKSGIG FPTGLSLNHV 200
    AAHYTPNTGD KLILKKDDIM KVDIGIHVNG RICDSAFTMT FNDEGKYDNI 250
    MKAVKEATYT GIKESGIDVR LNDIGAAIQE VMESYEMEEN GKIYPIKCIK 300
    NLNGHNIDDF IIHSGKSVPI IANGDMTKME EGEIFAIETF GSTGNGYVLP 350
    EGECSHYAMN KNIQHLKPPS ERSKQLLESI KQNFGTLPWC RRYLERTGEE 400
    KYLFALNQLV RHGIIEEYPP IVDKRGSYTA QYEHTILLHP HKKEVVTKGD 450
    DY 452
    Length:452
    Mass (Da):51,409
    Last modified:March 24, 2009 - v1
    Checksum:iE9BA5A87E7D7FAF9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FM992693 Genomic DNA. Translation: CAX41324.1.
    RefSeqiXP_002421164.1. XM_002421119.1.

    Genome annotation databases

    GeneIDi8048936.
    KEGGicdu:CD36_64570.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FM992693 Genomic DNA. Translation: CAX41324.1 .
    RefSeqi XP_002421164.1. XM_002421119.1.

    3D structure databases

    ProteinModelPortali B9WJA2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 573826.CD36_64570.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 8048936.
    KEGGi cdu:CD36_64570.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    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: CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841.

    Entry informationi

    Entry nameiMAP2_CANDC
    AccessioniPrimary (citable) accession number: B9WJA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 38 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

    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