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E3RCY7

- MAP21_PYRTT

UniProt

E3RCY7 - MAP21_PYRTT

Protein

Methionine aminopeptidase 2-1

Gene

PTT_01272

Organism
Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus) (Drechslera teres f. teres)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 23 (01 Oct 2014)
      Sequence version 1 (11 Jan 2011)
      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 sitei205 – 2051SubstrateUniRule annotation
    Metal bindingi225 – 2251Divalent metal cation 1UniRule annotation
    Metal bindingi236 – 2361Divalent metal cation 1UniRule annotation
    Metal bindingi236 – 2361Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi305 – 3051Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei313 – 3131SubstrateUniRule annotation
    Metal bindingi338 – 3381Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi433 – 4331Divalent metal cation 1UniRule annotation
    Metal bindingi433 – 4331Divalent 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 2-1UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2-1UniRule annotation
    Short name:
    MetAP 2-1UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    ORF Names:PTT_01272
    OrganismiPyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus) (Drechslera teres f. teres)
    Taxonomic identifieri861557 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaePyrenophora
    ProteomesiUP000001067: 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 – 452452Methionine aminopeptidase 2-1PRO_0000407613Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliE3RCY7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi60 – 667Poly-Lys
    Compositional biasi69 – 724Poly-Lys

    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.

    E3RCY7-1 [UniParc]FASTAAdd to Basket

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    MAAKVADDVA NLKLDDSNTK PASGAAENGD KPTGDAEHDD SDDDNEAEDG    50
    APEAGEGAAK KKKKRKPRKK KKAAGAAGAG GAKVQTAPPR VRIDEVFPND 100
    SYPEGEIQEY VNENAYRTTN EEKRHLDRMN NDFLTEYRKG AEIHREVRQW 150
    AQKWIKPGMG LTEIAEGIED SVRALTGHQG LGNGDAQIAG MGFPTGLSIN 200
    HCAAHYTPNA GNKMVVNYED VMKVDFGVHI NGRIVDSAFT LTFDPVYDNL 250
    INACKAATNA GIKEAGIDVR MSDIGAAIQE VMESYEVEIK GEMLPVKCIR 300
    NLNGHSIGHY TIHGGKTVPI VKGGDQTKME EGETFAIETF GSTGKGYVRD 350
    DMETSHYAMK ADAPKVALRV SSAKTLLSSI TKNFGTLPFC RRYLDRMGHD 400
    KYLLGLNNLV SAGIVEAYPP LCDIKGSYTA QSEHTFVLRP TCKEVLSRGD 450
    DY 452
    Length:452
    Mass (Da):49,147
    Last modified:January 11, 2011 - v1
    Checksum:i70E59100B687B29E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GL531948 Genomic DNA. Translation: EFQ96410.1.
    RefSeqiXP_003295492.1. XM_003295444.1.

    Genome annotation databases

    EnsemblFungiiEFQ96410; EFQ96410; PTT_01272.
    GeneIDi10514792.
    KEGGipte:PTT_01272.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GL531948 Genomic DNA. Translation: EFQ96410.1 .
    RefSeqi XP_003295492.1. XM_003295444.1.

    3D structure databases

    ProteinModelPortali E3RCY7.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFQ96410 ; EFQ96410 ; PTT_01272 .
    GeneIDi 10514792.
    KEGGi pte:PTT_01272.

    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. "A first genome assembly of the barley fungal pathogen Pyrenophora teres f. teres."
      Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S., Oliver R.P., Friesen T.L.
      Genome Biol. 11:R109.1-R109.14(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 0-1.

    Entry informationi

    Entry nameiMAP21_PYRTT
    AccessioniPrimary (citable) accession number: E3RCY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 23 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