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A8QBZ2

- MAP2_MALGO

UniProt

A8QBZ2 - MAP2_MALGO

Protein

Methionine aminopeptidase 2

Gene

MGL_3955

Organism
Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (15 Jan 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 sitei200 – 2001SubstrateUniRule annotation
    Metal bindingi220 – 2201Divalent metal cation 1UniRule annotation
    Metal bindingi231 – 2311Divalent metal cation 1UniRule annotation
    Metal bindingi231 – 2311Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi300 – 3001Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei308 – 3081SubstrateUniRule annotation
    Metal bindingi334 – 3341Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi429 – 4291Divalent metal cation 1UniRule annotation
    Metal bindingi429 – 4291Divalent 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
    ORF Names:MGL_3955
    OrganismiMalassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus)
    Taxonomic identifieri425265 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaExobasidiomycetesMalassezialesMalasseziaceaeMalassezia
    ProteomesiUP000008837: 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 – 448448Methionine aminopeptidase 2PRO_0000407657Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliA8QBZ2.
    SMRiA8QBZ2. Positions 77-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi54 – 7320Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    A8QBZ2-1 [UniParc]FASTAAdd to Basket

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    MPATAEAADA ATQATDAFST KLEENKLPEG QERGPEEEED DDDDETPAPG    50
    DAEKKKKKKK KSGAKKKKSK TAKAVMEQTE PPSIGLTKMF PNGVFPVGEV 100
    QQYDETKFDE SRKRVTGEEL RERERLIQEK DGFNYNFIRR AAEVHRQVRQ 150
    YAQRTIKPGM SMTEIANMIE DGTRALVEVN GFESGIGFPT GLSLNEVAAH 200
    YTPNAGDKRI LQSGDVLKVD FGVQVKGRIV DSAFTMNFEP TYDPLLAAVR 250
    AATNTGVKEA GIDARLGEVG AAIQEVMESH EFEAEGKTHQ VKCIRNLQGH 300
    DIAPYRIHGG KSVPIVAVPN LDVKMEEGET FAIETFGSTG RGYVVDSGEC 350
    SHYARQANPP HVSLRINSAR QLLYTINKNF GSLPFCRRYL DRLGEQNYLL 400
    GLRHLVSQGV VQDYPPLADV PGCMTAQFEH TILLRPTCKE VVSRGDDY 448
    Length:448
    Mass (Da):49,566
    Last modified:January 15, 2008 - v1
    Checksum:i12878A2062411469
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAYY01000016 Genomic DNA. Translation: EDP41747.1.
    RefSeqiXP_001728961.1. XM_001728909.1.

    Genome annotation databases

    GeneIDi5853267.
    KEGGimgl:MGL_3955.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAYY01000016 Genomic DNA. Translation: EDP41747.1 .
    RefSeqi XP_001728961.1. XM_001728909.1.

    3D structure databases

    ProteinModelPortali A8QBZ2.
    SMRi A8QBZ2. Positions 77-448.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5853267.
    KEGGi mgl:MGL_3955.

    Phylogenomic databases

    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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4612 / CBS 7966.

    Entry informationi

    Entry nameiMAP2_MALGO
    AccessioniPrimary (citable) accession number: A8QBZ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 45 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