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Q5BGG1

- MAP22_EMENI

UniProt

Q5BGG1 - MAP22_EMENI

Protein

Methionine aminopeptidase 2-2

Gene

AN0369

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 2 (03 May 2011)
      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 sitei209 – 2091SubstrateUniRule annotation
    Metal bindingi230 – 2301Divalent metal cation 1UniRule annotation
    Metal bindingi241 – 2411Divalent metal cation 1UniRule annotation
    Metal bindingi241 – 2411Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi310 – 3101Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei318 – 3181SubstrateUniRule annotation
    Metal bindingi343 – 3431Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi439 – 4391Divalent metal cation 1UniRule annotation
    Metal bindingi439 – 4391Divalent 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:AN0369
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VIII

    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 – 458458Methionine aminopeptidase 2-2PRO_0000407628Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00002334.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5BGG1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    KOiK01265.
    OMAiNNCVAHY.
    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.

    Q5BGG1-1 [UniParc]FASTAAdd to Basket

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    MGSKTPERDG HKGQENTTGP VECPLGGMPR GMHLATDGDG TIGDSGDDDD    50
    GEAHSTALIN ANANGNQKKK RKSKKKGKKK AAKQSSPPRV PLSQLFLQGK 100
    YPIGEVQEYQ PNVENTSRTT AEEVRYKSRS HLEDDSFLND YRKAAEVHRQ 150
    VRKWTQERVK PGQGLMEIAE DIDDGVRALL GHAGLEPGDS LKAGLGFPTG 200
    LSLNNVVAHY TPNPGQKDII LQSSDVMKVD FGVHINGWIV DSAFTMTFDP 250
    VYDNLLAAVK DATNAGLKTA GIDVRISDVS AAIQEAMESY EVEIGGKTFP 300
    VKAVRNITGH NIKHYQIHGG KSVPFVKNSD QTKMEEGEIF AIETFGSTGR 350
    GYIYDDVGVY GYGKSYDAPR QVSLPLASAR SLYKTINENF GTIVFCRRYL 400
    DRLGLQRYLA GMNTLVQHGV VDVYAPLVDI KGSYSAQFEH TVLLRESNKE 450
    VISRGDDY 458
    Length:458
    Mass (Da):50,186
    Last modified:May 3, 2011 - v2
    Checksum:i79A7211808B75D0E
    GO

    Sequence cautioni

    The sequence EAA65775.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000006 Genomic DNA. Translation: EAA65775.1. Sequence problems.
    BN001308 Genomic DNA. Translation: CBF89626.1.
    RefSeqiXP_657973.1. XM_652881.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00002334; CADANIAP00002334; CADANIAG00002334.
    GeneIDi2876145.
    KEGGiani:AN0369.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000006 Genomic DNA. Translation: EAA65775.1 . Sequence problems.
    BN001308 Genomic DNA. Translation: CBF89626.1 .
    RefSeqi XP_657973.1. XM_652881.1.

    3D structure databases

    ProteinModelPortali Q5BGG1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00002334.

    Protein family/group databases

    MEROPSi M24.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00002334 ; CADANIAP00002334 ; CADANIAG00002334 .
    GeneIDi 2876145.
    KEGGi ani:AN0369.2.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    KOi K01265.
    OMAi NNCVAHY.
    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: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    2. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

    Entry informationi

    Entry nameiMAP22_EMENI
    AccessioniPrimary (citable) accession number: Q5BGG1
    Secondary accession number(s): C8VTR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 67 of the entry and version 2 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