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B6HTQ4

- MAP22_PENCW

UniProt

B6HTQ4 - MAP22_PENCW

Protein

Methionine aminopeptidase 2-2

Gene

Pc22g18010

Organism
Penicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin 54-1255) (Penicillium notatum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (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 sitei196 – 1961SubstrateUniRule annotation
    Metal bindingi216 – 2161Divalent metal cation 1UniRule annotation
    Metal bindingi227 – 2271Divalent metal cation 1UniRule annotation
    Metal bindingi227 – 2271Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi296 – 2961Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei304 – 3041SubstrateUniRule annotation
    Metal bindingi329 – 3291Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi424 – 4241Divalent metal cation 1UniRule annotation
    Metal bindingi424 – 4241Divalent 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:PC22G18010-MONOMER.

    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:Pc22g18010
    OrganismiPenicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin 54-1255) (Penicillium notatum)
    Taxonomic identifieri500485 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex
    ProteomesiUP000000724: Contig Pc00c22

    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 – 439439Methionine aminopeptidase 2-2PRO_0000407610Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi500485.B6HTQ4.

    Structurei

    3D structure databases

    ProteinModelPortaliB6HTQ4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi56 – 7419Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    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.
    IPR018349. Pept_M24A_MAP2_BS.
    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.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B6HTQ4-1 [UniParc]FASTAAdd to Basket

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    MAAQTTEKLD QLDLNVQAAP TADQVPAEAE EDSDDAQDEG AAEAGAAGAG    50
    STLADKKKKK KKPKKKSKKK GGAKVQSEPP RVPVSNLFPN GQYPEGEIVE 100
    YLNDNAYRTT NEEKRYLDRM NNDFLQEYRQ GAEVHRQVRQ YAQKNIKPGQ 150
    TLTEIAEGIE DSVRALTGHS GLEEGDNIKG GMGFPCGLSI NHCAAHYTPN 200
    AGNKMVLNEG DVMKVDFGAH LNGRIVDSAF TMTFDPVYDP LLAAVKDATN 250
    TGIREAGIDV RMSDIGAAIQ EAMESYEVEI NGTMHPVKCI RNLNGHNIDQ 300
    HVIHGGKSVP IVKSTDQTKM EEGEVFAIET FGSTGKGYVR EEMETSHYAL 350
    AADAPNVPLR LSSAKNLLNL INKNFGTLPF CRRYIDRLGQ DKYLLGLNNL 400
    VSSGIVQDYP PLCDIKGSYT AQYEHVCFYF GVFSTLIVY 439
    Length:439
    Mass (Da):48,103
    Last modified:December 16, 2008 - v1
    Checksum:i08C432DD67D13107
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM920437 Genomic DNA. Translation: CAP99089.1.
    RefSeqiXP_002565710.1. XM_002565664.1.

    Genome annotation databases

    GeneIDi8312818.
    KEGGipcs:Pc22g18010.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM920437 Genomic DNA. Translation: CAP99089.1 .
    RefSeqi XP_002565710.1. XM_002565664.1.

    3D structure databases

    ProteinModelPortali B6HTQ4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 500485.B6HTQ4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 8312818.
    KEGGi pcs:Pc22g18010.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PCHR:PC22G18010-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 ]
    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.
    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 nameiMAP22_PENCW
    AccessioniPrimary (citable) accession number: B6HTQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 43 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