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Q2U6H2

- MAP2_ASPOR

UniProt

Q2U6H2 - MAP2_ASPOR

Protein

Methionine aminopeptidase 2

Gene

AO090120000238

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (24 Jan 2006)
      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 sitei219 – 2191SubstrateUniRule annotation
    Metal bindingi240 – 2401Divalent metal cation 1UniRule annotation
    Metal bindingi251 – 2511Divalent metal cation 1UniRule annotation
    Metal bindingi251 – 2511Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi320 – 3201Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Metal bindingi353 – 3531Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi449 – 4491Divalent metal cation 1UniRule annotation
    Metal bindingi449 – 4491Divalent 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

    Protein family/group databases

    MEROPSiM24.002.

    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:AO090120000238
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 5

    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 – 468468Methionine aminopeptidase 2PRO_0000407643Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5062.CADAORAP00011158.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2U6H2.
    SMRiQ2U6H2. Positions 93-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi78 – 814Poly-Lys

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    KOiK01265.
    OMAiNNCVAHY.
    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]
    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.

    Q2U6H2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSKTFEGEG QRGGNDPSNS TSPNSAGGEP RGAHLSRDGD GSLGDGDGDD    50
    GADGDEKDGA VTTTPLTEQQ PSSETTSKKK KRRKPKKKIS ALKQSSPPRV 100
    PLDDLFPTGQ FPVGETHEYG SVVEGTARTT SEEVRYLSRN YLQDDSVLTD 150
    YRKAAEIHRQ VRHWTQENVR PGQTLTEIAV GIEDGVRALL DNAGLETGQC 200
    LQSGMGFPTG LALNDCVAHY TPNPGQKDIV LQASDVMKVD FGVHINGWIV 250
    DSAFTMSFDP TYDNLLAAVK DATNTGIKNA GIDVRISDVS AAIQEAMESY 300
    EVEIGGKVFP VKPVRDISGH NINRYQIHGG KSIPFVKNSS QTKMEEGEIF 350
    AIETFGSTGR GSTVEGFGVY GYGKDPNAPK KVSSPLASAR SLYKTINENF 400
    GSIVFCRRYL ERLGVERYLA GMNSLVNNGI VEQYAPLMDM KGSYSAQFEH 450
    TILLRESCKE VVSRGNDY 468
    Length:468
    Mass (Da):50,724
    Last modified:January 24, 2006 - v1
    Checksum:i7290AC2351FFEFF9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007166 Genomic DNA. Translation: BAE62843.1.
    RefSeqiXP_001823976.1. XM_001823924.1.

    Genome annotation databases

    EnsemblFungiiCADAORAT00011390; CADAORAP00011158; CADAORAG00011390.
    GeneIDi5996235.
    KEGGiaor:AOR_1_414094.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007166 Genomic DNA. Translation: BAE62843.1 .
    RefSeqi XP_001823976.1. XM_001823924.1.

    3D structure databases

    ProteinModelPortali Q2U6H2.
    SMRi Q2U6H2. Positions 93-468.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5062.CADAORAP00011158.

    Protein family/group databases

    MEROPSi M24.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00011390 ; CADAORAP00011158 ; CADAORAG00011390 .
    GeneIDi 5996235.
    KEGGi aor:AOR_1_414094.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    KOi K01265.
    OMAi NNCVAHY.
    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 ]
    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. "Genome sequencing and analysis of Aspergillus oryzae."
      Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
      , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
      Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 42149 / RIB 40.

    Entry informationi

    Entry nameiMAP2_ASPOR
    AccessioniPrimary (citable) accession number: Q2U6H2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 59 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