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B2VW14

- MAP21_PYRTR

UniProt

B2VW14 - MAP21_PYRTR

Protein

Methionine aminopeptidase 2-1

Gene

PTRG_01376

Organism
Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) (Drechslera tritici-repentis)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (01 Jul 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 sitei210 – 2101SubstrateUniRule annotation
    Metal bindingi231 – 2311Divalent metal cation 1UniRule annotation
    Metal bindingi242 – 2421Divalent metal cation 1UniRule annotation
    Metal bindingi242 – 2421Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi311 – 3111Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei319 – 3191SubstrateUniRule annotation
    Metal bindingi344 – 3441Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi440 – 4401Divalent metal cation 1UniRule annotation
    Metal bindingi440 – 4401Divalent 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:PTRG_01376
    OrganismiPyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) (Drechslera tritici-repentis)
    Taxonomic identifieri426418 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaePyrenophora
    ProteomesiUP000001471: 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 – 459459Methionine aminopeptidase 2-1PRO_0000407634Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliB2VW14.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    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]
    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.

    B2VW14-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSKSPEDHR QGPDGGSADA AVTIINPPKS AAASGLLQGM LEGQDEDGDD    50
    DDDEKTGINV KTYDGAKKKR KRNKKKSKKV AVIQQTFPPR IPLATLFDNQ 100
    PYPEGQIVDH VVKDDNIKRT TTEELRHVAA LNDMDDDFLK DYRKAAEVHR 150
    QVRHHAQTIA KPGVSMTRLA EEIDEGVRAL TGHTGLETGD ALKAGLAFPT 200
    GLCLNHVGAH WTPNAGAKEV ILKHDDVLKV DFGVHVNGRI VDSAFTVAAN 250
    PVYDNLLAAV KAATNTGLGE AGIDARIDHI SEAIQEVMES YEVELNGKTI 300
    PVKAVRNITG HNILRYRIHG DKQVPFVKTK TDQRMEEGDI FAIETFGSTG 350
    KAHLRDDVGV YGYGRNENMS PAVLHQSSAK SLLKTIDANF GTLVFARRQL 400
    ERLPGVEKYH LGMRTLVNSG LVESYAPLVD ITGSYIAQFE HTVLLRPNCK 450
    EIISRGDDY 459
    Length:459
    Mass (Da):50,250
    Last modified:July 1, 2008 - v1
    Checksum:i273AECA2B59CE3E8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS231615 Genomic DNA. Translation: EDU40814.1.
    RefSeqiXP_001931709.1. XM_001931674.1.

    Genome annotation databases

    EnsemblFungiiEDU40814; EDU40814; PTRG_01376.
    GeneIDi6338328.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS231615 Genomic DNA. Translation: EDU40814.1 .
    RefSeqi XP_001931709.1. XM_001931674.1.

    3D structure databases

    ProteinModelPortali B2VW14.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EDU40814 ; EDU40814 ; PTRG_01376 .
    GeneIDi 6338328.

    Phylogenomic databases

    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 ]
    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. "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-repentis, reveals transduplication and the impact of repeat elements on pathogenicity and population divergence."
      Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B., Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H., Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W., Schwartz D.C., Spatafora J.W.
      , Turgeon B.G., Yandava C., Young S., Zhou S., Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.
      G3 (Bethesda) 3:41-63(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Pt-1C-BFP.

    Entry informationi

    Entry nameiMAP21_PYRTR
    AccessioniPrimary (citable) accession number: B2VW14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 39 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