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Q5B4X6

- MAP21_EMENI

UniProt

Q5B4X6 - MAP21_EMENI

Protein

Methionine aminopeptidase 2-1

Gene

AN4404

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 66 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      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 bindingi301 – 3011Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei309 – 3091SubstrateUniRule annotation
    Metal bindingi334 – 3341Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi429 – 4291Divalent metal cation 1UniRule annotation
    Metal bindingi429 – 4291Divalent 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 2-1UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2-1UniRule annotation
    Short name:
    MetAP 2-1UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    ORF Names:AN4404
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome III

    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 – 448448Methionine aminopeptidase 2-1PRO_0000407606Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00006053.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5B4X6.
    SMRiQ5B4X6. Positions 76-448.
    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.
    KOiK01265.
    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.

    Q5B4X6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQASEKLE KLDLNGQNGE SAAGPAKAGQ ADAGEVEDES DDDADDAGAA    50
    ADGAANGAAK KKKKRKSKKK KKGGAKVQSS PPRVPVSSLF ANGQYPEGEI 100
    VEYKNENSYR TTNEEKRYLD RMNNDFLQEY RQGAEVHRQV RQYAQKNIKP 150
    GQTLTEIAEG IEDSVRALTG HQGLEEGDNI KGGMGFPCGL SINHCAAHYT 200
    PNAGNKMVLQ QGDVMKVDFG AHINGRIVDS AFTMSFDPVY DPLLEAVKDA 250
    TNTGIRSLQE AGIDVRMSDI GAAIQETMES YEIELNGTTY PIKPIRNLNG 300
    HNIDQHVIHG GKSVPIVKGS DQTKMEEGEV FAIETFGSTG KGYVREDMET 350
    SHYALVANAP QVPLRLSSAK SLLNVINKNF GTLPWCRRYL DRLGQDKYLL 400
    GLNNLVQSGI VQDYPPLCDI KGSYTAQFEH TIVLRPTVKE VISRGDDY 448
    Length:448
    Mass (Da):48,898
    Last modified:April 26, 2005 - v1
    Checksum:i51E7D6D1F4AD0298
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000076 Genomic DNA. Translation: EAA60321.1.
    BN001303 Genomic DNA. Translation: CBF77596.1.
    RefSeqiXP_662008.1. XM_656916.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00006053; CADANIAP00006053; CADANIAG00006053.
    GeneIDi2872201.
    KEGGiani:AN4404.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000076 Genomic DNA. Translation: EAA60321.1 .
    BN001303 Genomic DNA. Translation: CBF77596.1 .
    RefSeqi XP_662008.1. XM_656916.1.

    3D structure databases

    ProteinModelPortali Q5B4X6.
    SMRi Q5B4X6. Positions 76-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00006053.

    Protein family/group databases

    MEROPSi M24.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00006053 ; CADANIAP00006053 ; CADANIAG00006053 .
    GeneIDi 2872201.
    KEGGi ani:AN4404.2.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    KOi K01265.
    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: 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 nameiMAP21_EMENI
    AccessioniPrimary (citable) accession number: Q5B4X6
    Secondary accession number(s): C8V8T8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 66 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