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Q6XMH6

- MAP2_ENCHA

UniProt

Q6XMH6 - MAP2_ENCHA

Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Encephalitozoon hellem (strain ATCC 50504) (Microsporidian parasite)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (05 Jul 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).1 PublicationUniRule 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

    Enzyme regulationi

    Irreversibly inhibited by the fungal metabolite fumagillin and the fumagillin analog TNP470, antiangiogenic drugs.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091SubstrateUniRule annotation
    Metal bindingi130 – 1301Divalent metal cation 1UniRule annotation
    Metal bindingi141 – 1411Divalent metal cation 1UniRule annotation
    Metal bindingi141 – 1411Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi210 – 2101Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei218 – 2181SubstrateUniRule annotation
    Metal bindingi243 – 2431Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi339 – 3391Divalent metal cation 1UniRule annotation
    Metal bindingi339 – 3391Divalent 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

    Enzyme and pathway databases

    BRENDAi3.4.11.18. 8141.

    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:EHEL_100750
    OrganismiEncephalitozoon hellem (strain ATCC 50504) (Microsporidian parasite)
    Taxonomic identifieri907965 [NCBI]
    Taxonomic lineageiEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon
    ProteomesiUP000010086: Chromosome X

    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 – 358358Methionine aminopeptidase 2PRO_0000148986Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ6XMH6.
    SMRiQ6XMH6. Positions 4-358.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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.
    InterProiIPR000994. 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]
    SUPFAMiSSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6XMH6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFILMNQAA ELPIEFLPRD GAYRKGRLLD SKNAEVENTT ESDILQDARR    50
    AAEAHRRVRY KVQSIIKPGM TLLEIVKSIE DSTRILLSGE RNNGIGFPAG 100
    MSMNSCAAHY SVNPGEKDII LTENDVLKID FGTHSNGRIM DSAFTIAFKE 150
    EFEPLLMAAK EGTETGIRSL GIDARVCDIG RDINEVISSY EMEVDGKKWA 200
    IRPVSDLHGH SISQFKIHGG ISIPAVNNRD PTRITGDTFY AVETFATTGE 250
    GFINDRSPCS HFMINTHKSR KLYNKDLIKV YEFVRDSFGT LPFSPRHLDY 300
    YNLVEGSALK SVNLLTMMGL FTPYPPLNDI DGSKVAQFEH TVYLSESGKE 350
    ILTRGDDY 358
    Length:358
    Mass (Da):40,071
    Last modified:July 5, 2004 - v1
    Checksum:i1EF1C9B28E0E8C39
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY224694 Genomic DNA. Translation: AAP51023.1.
    CP002723 Genomic DNA. Translation: AFM99168.1.
    AY339780 Genomic DNA. Translation: AAR04554.1.
    RefSeqiXP_003888149.1. XM_003888100.1.

    Genome annotation databases

    GeneIDi13466604.
    KEGGiehe:EHEL_100750.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY224694 Genomic DNA. Translation: AAP51023.1 .
    CP002723 Genomic DNA. Translation: AFM99168.1 .
    AY339780 Genomic DNA. Translation: AAR04554.1 .
    RefSeqi XP_003888149.1. XM_003888100.1.

    3D structure databases

    ProteinModelPortali Q6XMH6.
    SMRi Q6XMH6. Positions 4-358.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 13466604.
    KEGGi ehe:EHEL_100750.

    Phylogenomic databases

    KOi K01265.
    OrthoDBi EOG7BGHW3.

    Enzyme and pathway databases

    BRENDAi 3.4.11.18. 8141.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPi MF_03175. MetAP_2_euk.
    InterProi 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 ]
    SUPFAMi SSF55920. SSF55920. 2 hits.
    TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
    PROSITEi PS01202. MAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Investigations into microsporidian methionine aminopeptidase type 2: a therapeutic target for microsporidiosis."
      Zhang H., Huang H., Cali A., Takvorian P.M., Feng X., Zhou G., Weiss L.M.
      Folia Parasitol. 52:182-192(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Gain and loss of multiple functionally related, horizontally transferred genes in the reduced genomes of two microsporidian parasites."
      Pombert J.-F., Selman M., Burki F., Bardell F.T., Farinelli L., Solter L.F., Whitman D.W., Weiss L.M., Corradi N., Keeling P.J.
      Proc. Natl. Acad. Sci. U.S.A. 109:12638-12643(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 50504.
    3. "Phylogenetic relationships of methionine aminopeptidase 2 among Encephalitozoon species and genotypes of microsporidia."
      Pandrea I., Mittleider D., Brindley P.J., Didier E.S., Robertson D.L.
      Mol. Biochem. Parasitol. 140:141-152(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-343.
      Strain: ATCC 50504.
    4. "Microsporidian methionine aminopeptidase type 2."
      Weiss L.M., Costa S.F., Zhang H.
      J. Eukaryot. Microbiol. 48:88S-90S(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.

    Entry informationi

    Entry nameiMAP2_ENCHA
    AccessioniPrimary (citable) accession number: Q6XMH6
    Secondary accession number(s): I6UP09, Q6VH16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 63 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

    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