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Q6BVB8

- MAP2_DEBHA

UniProt

Q6BVB8 - MAP2_DEBHA

Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 2 (04 Nov 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 sitei172 – 1721SubstrateUniRule annotation
    Metal bindingi192 – 1921Divalent metal cation 1UniRule annotation
    Metal bindingi203 – 2031Divalent metal cation 1UniRule annotation
    Metal bindingi203 – 2031Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi272 – 2721Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei280 – 2801SubstrateUniRule annotation
    Metal bindingi305 – 3051Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi400 – 4001Divalent metal cation 1UniRule annotation
    Metal bindingi400 – 4001Divalent 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
    Ordered Locus Names:DEHA2C03894g
    OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
    Taxonomic identifieri284592 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
    ProteomesiUP000000599: Chromosome C

    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 – 419419Methionine aminopeptidase 2PRO_0000407651Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi4959.Q6BVB8.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6BVB8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi48 – 6013Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    KOiK01265.
    OMAiIQICEEL.
    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.

    Q6BVB8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTNSSNPNE VMEKVQDLKI DDSKPKVDSE EQPEAESDGE SATDGAQKKK    50
    KKKKSKKKKK ITAIDNSYPD GVFPEGEWQE YPLDVNSYRT TSEEKRYLDR 100
    QQNNHWQDFR KGAEIHRRVR HKAQSSIRPG MNMTEIADLI ENSVRSYANN 150
    DHTLKAGIGF PTGLSLNHVA AHYTPNAGDK TVLNYEDVMK VDIGVHVNGH 200
    IVDSAFTLTF DDKYDSLLKA VKEATNTGVK EAGIDVRLND IGEAIQEVME 250
    SYEMELNGKT YPIKCIRNLN GHNIGDYLIH SGKTVPIVPN GDMTKMEEGE 300
    TFAIETFGST GNGYVLPQGE CSHYAKNPGT DDIVVPGDKA KSLLNVINEN 350
    FGTLPWCRRY LDRLGQDKYL LALNQLVRAG IVQDYPPIVD IKGSYTAQFE 400
    HTILLHPHKK EVVSRGDDY 419
    Length:419
    Mass (Da):46,948
    Last modified:November 4, 2008 - v2
    Checksum:iFF3366D553F7D758
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382135 Genomic DNA. Translation: CAG85896.2.
    RefSeqiXP_457851.2. XM_457851.1.

    Genome annotation databases

    GeneIDi2900504.
    KEGGidha:DEHA2C03894g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382135 Genomic DNA. Translation: CAG85896.2 .
    RefSeqi XP_457851.2. XM_457851.1.

    3D structure databases

    ProteinModelPortali Q6BVB8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4959.Q6BVB8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2900504.
    KEGGi dha:DEHA2C03894g.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    KOi K01265.
    OMAi IQICEEL.
    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...

    Entry informationi

    Entry nameiMAP2_DEBHA
    AccessioniPrimary (citable) accession number: Q6BVB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 69 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