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B6QD96

- MAP22_PENMQ

UniProt

B6QD96 - MAP22_PENMQ

Protein

Methionine aminopeptidase 2-2

Gene

PMAA_077770

Organism
Penicillium marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 1 (16 Dec 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 sitei215 – 2151SubstrateUniRule annotation
    Metal bindingi236 – 2361Divalent metal cation 1UniRule annotation
    Metal bindingi247 – 2471Divalent metal cation 1UniRule annotation
    Metal bindingi247 – 2471Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi316 – 3161Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei324 – 3241SubstrateUniRule annotation
    Metal bindingi349 – 3491Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi444 – 4441Divalent metal cation 1UniRule annotation
    Metal bindingi444 – 4441Divalent 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 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:PMAA_077770
    OrganismiPenicillium marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
    Taxonomic identifieri441960 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeTalaromyces
    ProteomesiUP000001294: 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 – 463463Methionine aminopeptidase 2-2PRO_0000407633Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliB6QD96.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi76 – 794Poly-Lys

    Sequence similaritiesi

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

    Phylogenomic databases

    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.

    B6QD96-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAKTFEGGD NHEDATNALS TKSNAVGGKP RGANMLEDGD GEFGTDDDDD    50
    GDGQDSSLAV VNPEDGSKPK KRKRSKKKKS NKKKPGDGAQ QQTSPPRVPL 100
    SQLFPDGKYP VGQMVKVPAV NLRRTTDEEL RYLSRGTITN DEALSDYRKA 150
    AEVHRQVRHW VHETVHPGQS LTELAVGIED GVRALLGHQG LEPGDSLKGG 200
    MGFPTGLALN NCAAHYTPNP GQKDIILKKE DVMKVDFGVH VNGWIVDSAF 250
    TVTFDPVYDN LLAAVKDATN TGLKCAGVDA RVGEIGGYIQ EAMESYEVEI 300
    NGKVHPVKAI RNITGHDILP YRIHGGKQVP FIKSKDQTKM EEGEVFAIET 350
    FGTTGKGYMM DGPGVYGYSK DPDARNMHLP LASARALLKT INQNFGTIPF 400
    CRRYLDRLGL EKYLLGMNSL ISHGIVHMYP PLVDIPGSYT AQFEHTILIK 450
    SSGNEIISRG DDY 463
    Length:463
    Mass (Da):50,462
    Last modified:December 16, 2008 - v1
    Checksum:i361160DAEC041D14
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS995901 Genomic DNA. Translation: EEA23746.1.
    RefSeqiXP_002147257.1. XM_002147221.1.

    Genome annotation databases

    GeneIDi7026154.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS995901 Genomic DNA. Translation: EEA23746.1 .
    RefSeqi XP_002147257.1. XM_002147221.1.

    3D structure databases

    ProteinModelPortali B6QD96.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 7026154.

    Phylogenomic databases

    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. "The genome sequence of Penicillium marneffei strain ATCC 18224."
      Fedorova N.D., Joardar V.S., Maiti R., Schobel S., Amedeo P., Galens K., Inman J.M., White O.R., Whitty B.R., Wortman J.R., Nierman W.C.
      Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 18224 / CBS 334.59 / QM 7333.

    Entry informationi

    Entry nameiMAP22_PENMQ
    AccessioniPrimary (citable) accession number: B6QD96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 35 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