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A5DR89

- MAP2_PICGU

UniProt

A5DR89 - MAP2_PICGU

Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      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 sitei210 – 2101SubstrateUniRule annotation
    Metal bindingi230 – 2301Divalent metal cation 1UniRule annotation
    Metal bindingi241 – 2411Divalent metal cation 1UniRule annotation
    Metal bindingi241 – 2411Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi312 – 3121Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei320 – 3201SubstrateUniRule annotation
    Metal bindingi345 – 3451Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi440 – 4401Divalent metal cation 1UniRule annotation
    Metal bindingi440 – 4401Divalent 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:PGUG_05790
    OrganismiMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
    Taxonomic identifieri294746 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeMeyerozyma
    ProteomesiUP000001997: 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 – 459459Methionine aminopeptidase 2PRO_0000407663Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi4929.A5DR89.

    Structurei

    3D structure databases

    ProteinModelPortaliA5DR89.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi89 – 9810Poly-Lys

    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.

    A5DR89-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKTRTNSET VSILHTLHTN QKAPGARVYR VFRFSHHPKM RSNMSQDKEA    50
    NEIAVNTTET VVSTPTDVTT AETKTDGSPE TNAAPAAAKK KKNKKKKKIT 100
    SIDSSYPDGV FPEGEWQEYP LEINSYRTSS EELRYLDNQR NNHWQDFRKG 150
    AEIHRRVRHK AQSSIRPGMT MTEIADLIEN SVRSYAAADH TLKAGIGFPT 200
    GLSLNEIAAH YTPNAGDKLV LGKDDVMKVD IGVHVNGHIV DSAFTMTFDD 250
    DHKYDNLLKA VKEATNTGVR EAGIDVRLND IGAAVQEVME SYEMEIGGKT 300
    YPIKCIRNLN GHNIGDYVIH SGKTVPIVAN GDMTKMEEGE TFAIETFGST 350
    GNGYVIPTGE CSHYALSEEY KQARVGTDRA KQLLKTIESN FGTLPWCRRY 400
    LDRVGEEKYL LALNQLVRAG AVQDYPPITD RAGSYTAQFE HTILLHPHKK 450
    EVVSRGDDY 459
    Length:459
    Mass (Da):51,166
    Last modified:July 22, 2008 - v2
    Checksum:iBD5FDC3013D74BC1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH408162 Genomic DNA. Translation: EDK41692.2.
    RefSeqiXP_001482027.1. XM_001481977.1.

    Genome annotation databases

    GeneIDi5123876.
    KEGGipgu:PGUG_05790.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH408162 Genomic DNA. Translation: EDK41692.2 .
    RefSeqi XP_001482027.1. XM_001481977.1.

    3D structure databases

    ProteinModelPortali A5DR89.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4929.A5DR89.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5123876.
    KEGGi pgu:PGUG_05790.

    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: ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324.

    Entry informationi

    Entry nameiMAP2_PICGU
    AccessioniPrimary (citable) accession number: A5DR89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 48 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, 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