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E3L3Q8

- MAP2_PUCGT

UniProt

E3L3Q8 - MAP2_PUCGT

Protein

Methionine aminopeptidase 2

Gene

PGTG_16374

Organism
Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL) (Black stem rust fungus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 24 (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 sitei209 – 2091SubstrateUniRule annotation
    Metal bindingi229 – 2291Divalent metal cation 1UniRule annotation
    Metal bindingi240 – 2401Divalent metal cation 1UniRule annotation
    Metal bindingi240 – 2401Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi309 – 3091Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei317 – 3171SubstrateUniRule annotation
    Metal bindingi343 – 3431Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi437 – 4371Divalent metal cation 1UniRule annotation
    Metal bindingi437 – 4371Divalent 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 involved in protein maturation Source: EnsemblFungi

    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
    ORF Names:PGTG_16374
    OrganismiPuccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL) (Black stem rust fungus)
    Taxonomic identifieri418459 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaPucciniomycotinaPucciniomycetesPuccinialesPucciniaceaePuccinia
    ProteomesiUP000008783: 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 – 456456Methionine aminopeptidase 2PRO_0000407666Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliE3L3Q8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi66 – 7914Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    E3L3Q8-1 [UniParc]FASTAAdd to Basket

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    MTIPVPKPAH PAAPDTNTDG LPNPKVVVPV EADEEEDDDD EEGKEDADGA    50
    VPAASHFSTH ALDGTKKKKK KKKKPKKKKT GEAGAGGQSE PPRVPVSKLF 100
    PNGNYPSGEE SAYLGENSYR TTSSEKRELE RLAAQEDPES AENYNSIRRA 150
    AEVHRQVRRY VQQTVKPGMS MTEIAEMVED GTRALVEVDG LQRGIGFPTG 200
    VSLNHCAAHY TPNAGDTIVL SADDVLKVDF GVQIGGRIVD SAFTMTFNNK 250
    YDKLLEAVRA ATNTGIREAG IDARLSDIGA SIQETMESYE VEVDGKVHKV 300
    KSIRNLTGHN ILPYHIHGGK SVPIVANSDE SAIMEEGDHF AVETFGSTGR 350
    GYVMDDGECS HYAKNPDVNK PIRLARAKTL LNTINKHFDT LPFCKRYLDR 400
    LGESRYYAAL DNLVNLGIVQ AYPPLSDIQG CMTAQYEHTI ILRPTCKEVV 450
    SRGDDY 456
    Length:456
    Mass (Da):49,884
    Last modified:January 11, 2011 - v1
    Checksum:i3E186ACE45D67CED
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS178343 Genomic DNA. Translation: EFP91183.1.
    RefSeqiXP_003335602.1. XM_003335554.1.

    Genome annotation databases

    EnsemblFungiiEFP91183; EFP91183; PGTG_16374.
    GeneIDi10528845.
    KEGGipgr:PGTG_16374.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS178343 Genomic DNA. Translation: EFP91183.1 .
    RefSeqi XP_003335602.1. XM_003335554.1.

    3D structure databases

    ProteinModelPortali E3L3Q8.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFP91183 ; EFP91183 ; PGTG_16374 .
    GeneIDi 10528845.
    KEGGi pgr:PGTG_16374.

    Phylogenomic databases

    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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CRL 75-36-700-3 / race SCCL.

    Entry informationi

    Entry nameiMAP2_PUCGT
    AccessioniPrimary (citable) accession number: E3L3Q8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 24 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