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Q2GYA8

- MAP22_CHAGB

UniProt

Q2GYA8 - MAP22_CHAGB

Protein

Methionine aminopeptidase 2-2

Gene

CHGG_07046

Organism
Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (21 Mar 2006)
      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 bindingi212 – 2121Divalent metal cation 1UniRule annotation
    Metal bindingi223 – 2231Divalent metal cation 1UniRule annotation
    Metal bindingi223 – 2231Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi292 – 2921Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei300 – 3001SubstrateUniRule annotation
    Metal bindingi325 – 3251Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi420 – 4201Divalent metal cation 1UniRule annotation
    Metal bindingi420 – 4201Divalent 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 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:CHGG_07046
    OrganismiChaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus)
    Taxonomic identifieri306901 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeChaetomium
    ProteomesiUP000001056: 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 – 439439Methionine aminopeptidase 2-2PRO_0000407604Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ2GYA8.
    SMRiQ2GYA8. Positions 72-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi55 – 617Poly-Lys
    Compositional biasi64 – 674Poly-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]
    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.

    Q2GYA8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQAPPTDE LSKLSVEDAD NKPQPDASNG NLNHDEDDSE DDAEDASAPA    50
    AGGAKKKKKR KPRKKKKNPT QQSDPPRVLI SQLFPDKQYP KGEEVEYLNE 100
    NSYRTTNEEK RHLDNLKSEF LNDYRHAAEA HRQVRQWAAK NIKPGQSLTD 150
    IANGIEDSVR ALVGHQGLEE GDALIAGMGF PTGLSINHCA AHYTPNAGNK 200
    MILQQDDVMK IDFGVQVNGN IVDSAFTMAF NPRYDPLLEA VKAATNAGIK 250
    EAGIDVRLGE IGGVIQEVME SYEVEIDGTT YPVKPIRNLN GHTILPYNIH 300
    GGKSVPIVKS NDTTKMEEGD VFAIETFGST GGGHVIEDGE VSHYAKRTDA 350
    PKVDLRLSSA KSLLSVINKN FGTLPWCRRY LDRLGQEKYL LGLNNLVSNG 400
    IVEAYPPLVD KKGSYTAQFE HTILIRPTVK EVISRGDDF 439
    Length:439
    Mass (Da):48,244
    Last modified:March 21, 2006 - v1
    Checksum:iE1E54ED5023BDB67
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH408033 Genomic DNA. Translation: EAQ85793.1.
    RefSeqiXP_001224702.1. XM_001224701.1.

    Genome annotation databases

    GeneIDi4393147.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH408033 Genomic DNA. Translation: EAQ85793.1 .
    RefSeqi XP_001224702.1. XM_001224701.1.

    3D structure databases

    ProteinModelPortali Q2GYA8.
    SMRi Q2GYA8. Positions 72-439.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4393147.

    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 ]
    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 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970.

    Entry informationi

    Entry nameiMAP22_CHAGB
    AccessioniPrimary (citable) accession number: Q2GYA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 51 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