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C6HI66

- MAP2_AJECH

UniProt

C6HI66 - MAP2_AJECH

Protein

Methionine aminopeptidase 2

Gene

HCDG_06216

Organism
Ajellomyces capsulatus (strain H143) (Darling's disease fungus) (Histoplasma capsulatum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 31 (01 Oct 2014)
      Sequence version 1 (01 Sep 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 sitei192 – 1921SubstrateUniRule annotation
    Metal bindingi213 – 2131Divalent metal cation 1UniRule annotation
    Metal bindingi224 – 2241Divalent metal cation 1UniRule annotation
    Metal bindingi224 – 2241Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi293 – 2931Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei301 – 3011SubstrateUniRule annotation
    Metal bindingi326 – 3261Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi421 – 4211Divalent metal cation 1UniRule annotation
    Metal bindingi421 – 4211Divalent 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:HCDG_06216
    OrganismiAjellomyces capsulatus (strain H143) (Darling's disease fungus) (Histoplasma capsulatum)
    Taxonomic identifieri544712 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces
    ProteomesiUP000002624: 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 – 440440Methionine aminopeptidase 2PRO_0000407640Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliC6HI66.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi50 – 589Poly-Lys

    Sequence similaritiesi

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

    Phylogenomic databases

    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.

    C6HI66-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSKTPGNHR RDPNESSRPP AIDAINPPKQ AAASGLVHGS LEGESQKRNK    50
    RKKKKKKKNT KELEILQTTP PRVALANIFR SQRYPEAEIV KYSSDNDNLQ 100
    RTTAEELRHL SVLNAMDDEF LNDYRNAAEV HRQVRQYVQT IIKPGIALSQ 150
    LAQEIEDGVR ALTNHQGLET GDALKAGMAF PTGLCLNNIA AHWTPNPGAK 200
    EVILQYDDVL KIDFGVHVNG RIVDSAFTMA FNPVYDNLLA AVKNATNTGL 250
    KEAGIDARIA HISETIQEVM ESYEVELNRK VIPVKAVRNI TGHNILHYKI 300
    HGDKQVPFVK TQTNQRMEEG DVFAIETFGS TGKAYLDDAT GIYGYGYDEN 350
    ASTAGLHHSS AKSLLKTIKE NFGTLVFSRR YLERLGVQRY HLGMRSLVTN 400
    GIVQSYAPLV DVPGSYVAQF EHTVLLRPNC KEVISRGDDY 440
    Length:440
    Mass (Da):48,946
    Last modified:September 1, 2009 - v1
    Checksum:i182797C03B39361E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GG692428 Genomic DNA. Translation: EER39994.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GG692428 Genomic DNA. Translation: EER39994.1 .

    3D structure databases

    ProteinModelPortali C6HI66.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    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: H143.

    Entry informationi

    Entry nameiMAP2_AJECH
    AccessioniPrimary (citable) accession number: C6HI66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 31 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