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Q6CA79

- MAP2_YARLI

UniProt

Q6CA79 - MAP2_YARLI

Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (16 Aug 2004)
      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 sitei224 – 2241SubstrateUniRule annotation
    Metal bindingi244 – 2441Divalent metal cation 1UniRule annotation
    Metal bindingi255 – 2551Divalent metal cation 1UniRule annotation
    Metal bindingi255 – 2551Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi324 – 3241Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei332 – 3321SubstrateUniRule annotation
    Metal bindingi357 – 3571Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi452 – 4521Divalent metal cation 1UniRule annotation
    Metal bindingi452 – 4521Divalent 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:YALI0D05159g
    OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
    Taxonomic identifieri284591 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
    ProteomesiUP000001300: Chromosome D

    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 – 471471Methionine aminopeptidase 2PRO_0000407673Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi4952.Q6CA79.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6CA79.
    SMRiQ6CA79. Positions 68-471.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi51 – 6414Lys-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.

    Q6CA79-1 [UniParc]FASTAAdd to Basket

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    MAEAIEKVAD KVADLVVDDK PAAVPESTSD HEDGDDNDDA VNEGEAVDGE    50
    KKKKKKKNKK KKKKGPAVQT EPPTVPIDRF FTSGIFPEGE ICEHPHKTFK 100
    PKGTAVDPFA DSEDEREAAE ERAKDDAKHG SDDPLDFNRL RTTNEEKRYL 150
    DREQAAVHNE WRKGAEIHRV VRKYARDNIK AGMTMTSIAE MIEDSVRALS 200
    NEEDSLKGGQ GFPTGVSLNH CAAHYTPNAG DKIVLKEDDV LKVDFGVHVN 250
    GKIIDSAFTH VQNDKWQGLL DAVKAATETG IREAGIDVRL GDIGEAIQET 300
    MESHEVEVDG KVYQVKSIRN LNGHNIAPYE IHGGKSVPIV KSADMTKMEE 350
    GETFAIETFG STGRGYVVTD GECSHYAKNV GVGHVPLRVN KAKQLLATID 400
    KNFGTLPFCR RYLDRLGEEK YLLALKNLVQ SGVVQDYPPL VDQKGCQTAQ 450
    YEHTIYLRPT CKEILSRGDD Y 471
    Length:471
    Mass (Da):52,156
    Last modified:August 16, 2004 - v1
    Checksum:i6990F681D67BBD0D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382130 Genomic DNA. Translation: CAG80621.1.
    RefSeqiXP_502433.1. XM_502433.1.

    Genome annotation databases

    EnsemblFungiiCAG80621; CAG80621; YALI0_D05159g.
    GeneIDi2910974.
    KEGGiyli:YALI0D05159g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382130 Genomic DNA. Translation: CAG80621.1 .
    RefSeqi XP_502433.1. XM_502433.1.

    3D structure databases

    ProteinModelPortali Q6CA79.
    SMRi Q6CA79. Positions 68-471.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4952.Q6CA79.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CAG80621 ; CAG80621 ; YALI0_D05159g .
    GeneIDi 2910974.
    KEGGi yli:YALI0D05159g.

    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_YARLI
    AccessioniPrimary (citable) accession number: Q6CA79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 71 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