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C5M8M4

- MAP2_CANTT

UniProt

C5M8M4 - MAP2_CANTT

Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 32 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      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 sitei183 – 1831SubstrateUniRule annotation
    Metal bindingi203 – 2031Divalent metal cation 1UniRule annotation
    Metal bindingi214 – 2141Divalent metal cation 1UniRule annotation
    Metal bindingi214 – 2141Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi285 – 2851Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei293 – 2931SubstrateUniRule annotation
    Metal bindingi318 – 3181Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi413 – 4131Divalent metal cation 1UniRule annotation
    Metal bindingi413 – 4131Divalent 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
    ORF Names:CTRG_02746
    OrganismiCandida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
    Taxonomic identifieri294747 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000002037: 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 – 432432Methionine aminopeptidase 2PRO_0000407648Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliC5M8M4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi57 – 7115Lys-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.
    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.

    C5M8M4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTASVDTKTV EGQINDLKID STESSTTIPN NGKQESDNED DEVDESSTTQ    50
    LSSTGDKKKK KKKNNKKKKK KIVSIDSSYP DGVFPEGQWM EYPLEINSYR 100
    TTSEEKRYLD RQENNKWEDF RKGAEIHRRV RHKAQSSIKP GMSMIEIADL 150
    IEDSVRNYAA ADHTLKAGIG FPTGLSLNHV AAHYTPNTGD KLVLNKDDIM 200
    KVDIGVHVNG RICDSAFTMT FNEEGKYDKI MEAVREATYT GIKEAGIDVR 250
    LNDIGEAIQE VMESYEMEEN GKILPIKCIK NLNGHNIGDY VIHSGKTVPI 300
    VANGDMTKME EGETFAIETF GSTGNGYVLP EGECSHYAMN TGVEHLKAPS 350
    ERSKQLLQNI KDNFGTLPWC RRYLERAGEE KYLFALNQLV RHGIVEEYPP 400
    IVDKRGSYTA QYEHTILLHP HKKEVVTKGD DY 432
    Length:432
    Mass (Da):48,681
    Last modified:July 28, 2009 - v1
    Checksum:i5D96C6A42548FB08
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GG692397 Genomic DNA. Translation: EER33928.1.
    RefSeqiXP_002548449.1. XM_002548403.1.

    Genome annotation databases

    GeneIDi8298308.
    KEGGictp:CTRG_02746.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GG692397 Genomic DNA. Translation: EER33928.1 .
    RefSeqi XP_002548449.1. XM_002548403.1.

    3D structure databases

    ProteinModelPortali C5M8M4.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 8298308.
    KEGGi ctp:CTRG_02746.

    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.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-3404 / T1.

    Entry informationi

    Entry nameiMAP2_CANTT
    AccessioniPrimary (citable) accession number: C5M8M4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 32 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