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Q0CL94

- MAP22_ASPTN

UniProt

Q0CL94 - MAP22_ASPTN

Protein

Methionine aminopeptidase 2-2

Gene

ATEG_05540

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
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 (17 Oct 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 sitei198 – 1981SubstrateUniRule annotation
    Metal bindingi218 – 2181Divalent metal cation 1UniRule annotation
    Metal bindingi229 – 2291Divalent metal cation 1UniRule annotation
    Metal bindingi229 – 2291Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi298 – 2981Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei306 – 3061SubstrateUniRule annotation
    Metal bindingi331 – 3311Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi426 – 4261Divalent metal cation 1UniRule annotation
    Metal bindingi426 – 4261Divalent 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

    Protein family/group databases

    MEROPSiM24.002.

    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:ATEG_05540
    OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
    Taxonomic identifieri341663 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000007963: 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 – 445445Methionine aminopeptidase 2-2PRO_0000407603Add
    BLAST

    Proteomic databases

    PRIDEiQ0CL94.

    Interactioni

    Protein-protein interaction databases

    STRINGi33178.CADATEAP00004684.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0CL94.
    SMRiQ0CL94. Positions 76-445.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi60 – 7617Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    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.

    Q0CL94-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQASEDLK KLDLNGQAGD SKAAAATAGQ AEAGEAEDDS DDDEVDGNAA    50
    PEGAASGAAK KKKKRKPKKK KKGGAKVQSS PPRVPISQLF PNNQYPEGEI 100
    VEYKNENSYR TTNEEKRYLD RMNNDFLQEY RQGAEVHRQV RQYAQKNIKP 150
    GQTLTEIAEG IEDAVRALTG HQGLEEGDNL KGGMGFPCGL SINHCAAHYT 200
    PNAGNKMVLQ QGDVMKVDFG AHLNGRIVDS AFTMAFDPVY DPLLEAVKDA 250
    TNTGIREAGI DVRMSDIGAA IQETMESYEV EINGQMHPVK CIRNLNGHNI 300
    DQHVIHGGKS VPIVKGGDQT KMEEGEVFAI ETFGSTGKGY VREDMETSHY 350
    ALVPNATPVP LRLSSAKNLL NVINKNFGTL PFCRRYLDRL GQDKYLLGLN 400
    NLVSSGIVQD YPPLCDIKGS YTAQFEHTIV LRPTVKEVIS RGDDY 445
    Length:445
    Mass (Da):48,627
    Last modified:October 17, 2006 - v1
    Checksum:i6F5D7F18DF1AE822
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476600 Genomic DNA. Translation: EAU34609.1.
    RefSeqiXP_001214718.1. XM_001214718.1.

    Genome annotation databases

    EnsemblFungiiCADATEAT00004684; CADATEAP00004684; CADATEAG00004684.
    GeneIDi4320577.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476600 Genomic DNA. Translation: EAU34609.1 .
    RefSeqi XP_001214718.1. XM_001214718.1.

    3D structure databases

    ProteinModelPortali Q0CL94.
    SMRi Q0CL94. Positions 76-445.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 33178.CADATEAP00004684.

    Protein family/group databases

    MEROPSi M24.002.

    Proteomic databases

    PRIDEi Q0CL94.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADATEAT00004684 ; CADATEAP00004684 ; CADATEAG00004684 .
    GeneIDi 4320577.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    OMAi IQICEEL.
    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: NIH 2624 / FGSC A1156.

    Entry informationi

    Entry nameiMAP22_ASPTN
    AccessioniPrimary (citable) accession number: Q0CL94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: October 17, 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