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O58362

- MAP2_PYRHO

UniProt

O58362 - MAP2_PYRHO

Protein

Methionine aminopeptidase

Gene

map

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    • Comment

    Functioni

    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 sitei62 – 621SubstrateUniRule annotation
    Metal bindingi82 – 821Divalent metal cation 1UniRule annotation
    Metal bindingi93 – 931Divalent metal cation 1UniRule annotation
    Metal bindingi93 – 931Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi153 – 1531Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei161 – 1611SubstrateUniRule annotation
    Metal bindingi187 – 1871Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi280 – 2801Divalent metal cation 1UniRule annotation
    Metal bindingi280 – 2801Divalent 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

    BioCyciPHOR70601:GJWR-623-MONOMER.

    Protein family/group databases

    MEROPSiM24.035.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidaseUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAPUniRule annotation
    Short name:
    MetAPUniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:mapUniRule annotation
    Ordered Locus Names:PH0628
    OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
    Taxonomic identifieri70601 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000000752: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 295295Methionine aminopeptidasePRO_0000148979Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi70601.PH0628.

    Structurei

    3D structure databases

    ProteinModelPortaliO58362.
    SMRiO58362. Positions 1-295.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226277.
    KOiK01265.
    OMAiERYKLHA.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_01975. MetAP_2_arc.
    InterProiIPR028595. MetAP_archaeal.
    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]
    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.

    O58362-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDVDKLIEAG KIAKKVREEA VKLAKPGVSL LELAEKIESR IVELGGKPAF    50
    PANLSLNEVA AHYTPYKGDQ TVLKEGDYLK IDLGVHIDGY IADTAVTVRV 100
    GMDFDELMEA AKEALESAIS VARAGVEVKE LGKAIENEIR KRGFNPIVNL 150
    SGHKIERYKL HAGVSIPNIY RPHDNYVLQE GDVFAIEPFA TTGAGQVIEV 200
    PPTLIYMYVR DAPVRMAQAR FLLAKIKREY KTLPFAYRWL QGEMPEGQLK 250
    LALRSLERSG ALYGYPVLRE IRGGMVTQFE HTIIVEKDSV TVTTE 295
    Length:295
    Mass (Da):32,795
    Last modified:August 1, 1998 - v1
    Checksum:iD228F4377CEB2AAC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000001 Genomic DNA. Translation: BAA29717.1.
    PIRiC71107.
    RefSeqiNP_142587.1. NC_000961.1.

    Genome annotation databases

    EnsemblBacteriaiBAA29717; BAA29717; BAA29717.
    GeneIDi1442960.
    KEGGipho:PH0628.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000001 Genomic DNA. Translation: BAA29717.1 .
    PIRi C71107.
    RefSeqi NP_142587.1. NC_000961.1.

    3D structure databases

    ProteinModelPortali O58362.
    SMRi O58362. Positions 1-295.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 70601.PH0628.

    Protein family/group databases

    MEROPSi M24.035.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA29717 ; BAA29717 ; BAA29717 .
    GeneIDi 1442960.
    KEGGi pho:PH0628.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226277.
    KOi K01265.
    OMAi ERYKLHA.

    Enzyme and pathway databases

    BioCyci PHOR70601:GJWR-623-MONOMER.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPi MF_01975. MetAP_2_arc.
    InterProi IPR028595. MetAP_archaeal.
    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 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

    Entry informationi

    Entry nameiMAP2_PYRHO
    AccessioniPrimary (citable) accession number: O58362
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete 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