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A7EZ86

- MAP2_SCLS1

UniProt

A7EZ86 - MAP2_SCLS1

Protein

Methionine aminopeptidase 2

Gene

SS1G_10653

Organism
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (11 Sep 2007)
      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 sitei199 – 1991SubstrateUniRule annotation
    Metal bindingi219 – 2191Divalent metal cation 1UniRule annotation
    Metal bindingi230 – 2301Divalent metal cation 1UniRule annotation
    Metal bindingi230 – 2301Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi299 – 2991Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei307 – 3071SubstrateUniRule annotation
    Metal bindingi332 – 3321Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi427 – 4271Divalent metal cation 1UniRule annotation
    Metal bindingi427 – 4271Divalent 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
    ORF Names:SS1G_10653
    OrganismiSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
    Taxonomic identifieri665079 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia
    ProteomesiUP000001312: 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 – 446446Methionine aminopeptidase 2PRO_0000407668Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi665079.A7EZ86.

    Structurei

    3D structure databases

    ProteinModelPortaliA7EZ86.
    SMRiA7EZ86. Positions 77-446.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    KOiK01265.
    OMAiPVGECHD.
    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.

    A7EZ86-1 [UniParc]FASTAAdd to Basket

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    MAAQVTDALK NLKVKDPNSV IESAAEAKSN GNTQAEAEDS DDEEEEPVNG    50
    EGAGEGGAKK KRKRKKKPKK KAGANPKVQS SPPRVLLSNL FPSGEYPVGE 100
    EVEYRDENNY RTTSEEKRYL DRMNNDFLQE YRQAAEIHRQ VRQYAKANIK 150
    PGQTLTEIAE GIEDSVRALT GHPGLEEGDN IKGGVAFPTG VNLDHIAAHY 200
    SPNAGNKTVL AYENVMKVDF GVHVNGRIVD SAFTIAFDPM YDNLLEAVKQ 250
    ATNTGIKEAG IDARLGEIGE HIQETMESYE VEIKGQTYQV KPIRNLNGHD 300
    ILQWKIHGGK SVPIVKSNDQ TKMEEGEVFA IETFGSTGNG YVRDDLECSH 350
    YAKVADAPNV PLRIASAGKL LNVINKNFGT LPFCRRYLDR LGQDKYLLGL 400
    NALVSHGIVQ DYPPLVDKKG SYTAQFEHTI VLRPNCKEVI SRGDDY 446
    Length:446
    Mass (Da):49,260
    Last modified:September 11, 2007 - v1
    Checksum:i0BC45FC3D04A2AF2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476636 Genomic DNA. Translation: EDN94778.1.
    RefSeqiXP_001588206.1. XM_001588156.1.

    Genome annotation databases

    GeneIDi5484447.
    KEGGissl:SS1G_10653.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476636 Genomic DNA. Translation: EDN94778.1 .
    RefSeqi XP_001588206.1. XM_001588156.1.

    3D structure databases

    ProteinModelPortali A7EZ86.
    SMRi A7EZ86. Positions 77-446.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 665079.A7EZ86.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5484447.
    KEGGi ssl:SS1G_10653.

    Phylogenomic databases

    eggNOGi COG0024.
    KOi K01265.
    OMAi PVGECHD.
    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. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
      Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
      , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
      PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 18683 / 1980 / Ss-1.

    Entry informationi

    Entry nameiMAP2_SCLS1
    AccessioniPrimary (citable) accession number: A7EZ86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 45 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