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B6H5L5

- MAP21_PENCW

UniProt

B6H5L5 - MAP21_PENCW

Protein

Methionine aminopeptidase 2-1

Gene

Pc14g00010

Organism
Penicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin 54-1255) (Penicillium notatum)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (16 Dec 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 sitei216 – 2161SubstrateUniRule annotation
    Metal bindingi237 – 2371Divalent metal cation 1UniRule annotation
    Metal bindingi248 – 2481Divalent metal cation 1UniRule annotation
    Metal bindingi248 – 2481Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi317 – 3171Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei325 – 3251SubstrateUniRule annotation
    Metal bindingi350 – 3501Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi446 – 4461Divalent metal cation 1UniRule annotation
    Metal bindingi446 – 4461Divalent 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

    Enzyme and pathway databases

    BioCyciPCHR:PC14G00010-MONOMER.

    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:Pc14g00010
    OrganismiPenicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin 54-1255) (Penicillium notatum)
    Taxonomic identifieri500485 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex
    ProteomesiUP000000724: Contig Pc00c14

    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 – 465465Methionine aminopeptidase 2-1PRO_0000407632Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi500485.B6H5L5.

    Structurei

    3D structure databases

    ProteinModelPortaliB6H5L5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    KOiK01265.
    OMAiNNCVAHY.
    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.

    B6H5L5-1 [UniParc]FASTAAdd to Basket

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    MGSKTAENES QGGGNAPPSS TKATATGGEP RGAHWSRDGD GTLGEGEGDD    50
    DADGDNTSCA PAVPLNPQTA PSTNSKKRKK RPKKKTSALK QSSPPRIPLA 100
    DLFPDHQYPH GEAQVYEPGL ENVARTTADE VRHHSRHHIE DDTFLNDYRK 150
    AAEVHRQVRR WTQESVRPGQ TLTEIAMGIE DGVRALLDNA GLDTGQGLIS 200
    GLGFPTGLSL NNCVAHYTPN PGQREVVLDS SDVMKVDFGV HINGWIVDSA 250
    FTMSFDPTYD NLLAAVKDAT NTGIKNAGVD VRISDVSAAI QEAMESYEVD 300
    INGRTFPVKA VRNITGHNIE QYRIHAGKSI PFVKNNDNTK MEEGEIFAIE 350
    TFGTTGRGYL FDGPGVYGYG KDPSAPKRIT SHLASAKSLY QKINENFGSL 400
    VFCRRYLERL GVESYLAGMN NLVSNGYVEV YQPLMDVRGS YSAQFEHTIL 450
    LRESCKEVIS RGDDY 465
    Length:465
    Mass (Da):50,739
    Last modified:December 16, 2008 - v1
    Checksum:iB311D49EC02E3C91
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM920429 Genomic DNA. Translation: CAP74142.1.
    RefSeqiXP_002559996.1. XM_002559950.1.

    Genome annotation databases

    GeneIDi8306312.
    KEGGipcs:Pc14g00010.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM920429 Genomic DNA. Translation: CAP74142.1 .
    RefSeqi XP_002559996.1. XM_002559950.1.

    3D structure databases

    ProteinModelPortali B6H5L5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 500485.B6H5L5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 8306312.
    KEGGi pcs:Pc14g00010.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    KOi K01265.
    OMAi NNCVAHY.
    OrthoDBi EOG7BGHW3.

    Enzyme and pathway databases

    BioCyci PCHR:PC14G00010-MONOMER.

    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: ATCC 28089 / DSM 1075 / Wisconsin 54-1255.

    Entry informationi

    Entry nameiMAP21_PENCW
    AccessioniPrimary (citable) accession number: B6H5L5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 44 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