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C7Z7V7

- MAP22_NECH7

UniProt

C7Z7V7 - MAP22_NECH7

Protein

Methionine aminopeptidase 2-2

Gene

NECHADRAFT_93045

Organism
Nectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI) (Fusarium solani subsp. pisi)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (13 Oct 2009)
      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 sitei211 – 2111SubstrateUniRule annotation
    Metal bindingi232 – 2321Divalent metal cation 1UniRule annotation
    Metal bindingi243 – 2431Divalent metal cation 1UniRule annotation
    Metal bindingi243 – 2431Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi302 – 3021Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei310 – 3101SubstrateUniRule annotation
    Metal bindingi335 – 3351Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi431 – 4311Divalent metal cation 1UniRule annotation
    Metal bindingi431 – 4311Divalent 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 2-2UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2-2UniRule annotation
    Short name:
    MetAP 2-2UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    ORF Names:NECHADRAFT_93045
    OrganismiNectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI) (Fusarium solani subsp. pisi)
    Taxonomic identifieri660122 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium solani species complex
    ProteomesiUP000005206: 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 – 450450Methionine aminopeptidase 2-2PRO_0000407630Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliC7Z7V7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi69 – 8416Lys-richAdd
    BLAST

    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]
    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.

    C7Z7V7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAKISEDHP PQGNGGPLSN DPCSAGGEPR GAHLSRDGDG SVGDKGGDDD    50
    DDDDEGVVGA VSLTEASDKK KKKKRKPKKK KAKKATHQSS PPRVPLSELF 100
    TPGQYPTGEF LEYEDTNTAR TTAAELRALG RKQLEDPAFL DDYRRAAEVH 150
    RQVRQWAQES VKPGQTLRDI ANGIEDGVRA LLGNQGLEPG DGLKSGMGFP 200
    TGLCLNHETA HYTPNPGQKD VVLQYEDVMK VDFGVHINGW IVDSAFTMSF 250
    DPTYDNLLAA VKDATNSGIK VNAAIQEAME SYEVEIAGKT YPVKPVRNIS 300
    AHNIQHYRIH GGKSIPFIKN SDQTKMEEGE VFAIETFGTT GRGRLYDDVG 350
    IYGYKLENGG PSPASLPFAS AKKLHKVIKE NFGNIVFCRR YLERLGQERY 400
    LAGLNCLVSN GLLEAYEPLA DVKGSYSAQF EHTILLRESS KEILSRGSDY 450
    Length:450
    Mass (Da):49,173
    Last modified:October 13, 2009 - v1
    Checksum:i8584AFDFFCEB89B4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GG698911 Genomic DNA. Translation: EEU39759.1.
    RefSeqiXP_003045472.1. XM_003045426.1.

    Genome annotation databases

    EnsemblFungiiNechaT93045; NechaP93045; NechaG93045.
    GeneIDi9672634.
    KEGGinhe:NECHADRAFT_93045.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GG698911 Genomic DNA. Translation: EEU39759.1 .
    RefSeqi XP_003045472.1. XM_003045426.1.

    3D structure databases

    ProteinModelPortali C7Z7V7.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii NechaT93045 ; NechaP93045 ; NechaG93045 .
    GeneIDi 9672634.
    KEGGi nhe:NECHADRAFT_93045.

    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 ]
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI.

    Entry informationi

    Entry nameiMAP22_NECH7
    AccessioniPrimary (citable) accession number: C7Z7V7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: October 13, 2009
    Last modified: October 1, 2014
    This is version 37 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