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A2QHX0

- MAP22_ASPNC

UniProt

A2QHX0 - MAP22_ASPNC

Protein

Methionine aminopeptidase 2-2

Gene

An04g01330

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      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 sitei184 – 1841SubstrateUniRule annotation
    Metal bindingi204 – 2041Divalent metal cation 1UniRule annotation
    Metal bindingi215 – 2151Divalent metal cation 1UniRule annotation
    Metal bindingi215 – 2151Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi284 – 2841Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei292 – 2921SubstrateUniRule annotation
    Metal bindingi317 – 3171Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi412 – 4121Divalent metal cation 1UniRule annotation
    Metal bindingi412 – 4121Divalent 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 2-2UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2-2UniRule annotation
    Short name:
    MetAP 2-2UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    ORF Names:An04g01330
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 6L

    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 – 431431Methionine aminopeptidase 2-2PRO_0000407602Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00003753.

    Structurei

    3D structure databases

    ProteinModelPortaliA2QHX0.
    SMRiA2QHX0. Positions 62-431.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    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.

    A2QHX0-1 [UniParc]FASTAAdd to Basket

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    MAAQASEKLQ KLDLNGQSGD AEADAPAAGQ TQAGEAEDDS DDDEVEDGNA    50
    AGEGAASGGG AKVQSSPPRV PLSTLFAGKE YPEGEIVEYQ NENSYRTTNE 100
    EKRYLDRMKN DFLQEYRQAA EVHRQVRQYA QKTIKPGQTL TEIAEGIEES 150
    VRALTGHQGL EEGDNLKGGM GFPCGLSINH CAAHYTPNAG NKMVLQQGDV 200
    MKVDFGAHIN GRIVDSAFTV AFDPVYDPLL AAVKDATNTG IREAGIDVRM 250
    SDIGAAIQEA MESYEVEING TMYPVKCIRN LNGHNIDQHI IHGGKSVPIV 300
    KGGDQTKMEE GEVFAIETFG STGKGYVRED METSHYALIP DHSQVPLRLS 350
    SAKNLLNVIN KNFGTLPFCR RYLDRLGQDK YLLGLNNLVS SGIVQDYPPL 400
    CDIKGSYTAQ YEHTIVLRPN VKEVISRGDD Y 431
    Length:431
    Mass (Da):46,964
    Last modified:March 6, 2007 - v1
    Checksum:i3C8063813B50BD68
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270069 Genomic DNA. Translation: CAK38590.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00003842; CADANGAP00003753; CADANGAG00003842.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270069 Genomic DNA. Translation: CAK38590.1 .

    3D structure databases

    ProteinModelPortali A2QHX0.
    SMRi A2QHX0. Positions 62-431.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00003753.

    Protein family/group databases

    MEROPSi M24.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00003842 ; CADANGAP00003753 ; CADANGAG00003842 .

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    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. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
      Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
      , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
      Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CBS 513.88 / FGSC A1513.

    Entry informationi

    Entry nameiMAP22_ASPNC
    AccessioniPrimary (citable) accession number: A2QHX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 50 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