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B0Y5N4

- MAP22_ASPFC

UniProt

B0Y5N4 - MAP22_ASPFC

Protein

Methionine aminopeptidase 2-2

Gene

AFUB_064000

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 2 (03 May 2011)
      Previous versions | rss
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    • Comment

    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 sitei225 – 2251SubstrateUniRule annotation
    Metal bindingi245 – 2451Divalent metal cation 1UniRule annotation
    Metal bindingi256 – 2561Divalent metal cation 1UniRule annotation
    Metal bindingi256 – 2561Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi325 – 3251Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei333 – 3331SubstrateUniRule annotation
    Metal bindingi358 – 3581Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi453 – 4531Divalent metal cation 1UniRule annotation
    Metal bindingi453 – 4531Divalent 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:AFUB_064000
    OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
    Taxonomic identifieri451804 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000001699: 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 – 472472Methionine aminopeptidase 2-2PRO_0000407599Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliB0Y5N4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi88 – 9912Poly-LysAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000226278.
    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.

    B0Y5N4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQVSEKLQ DLHLNGLNGD AKSNATVIGQ TEAGEAEDDS DDEKEDGNTA    50
    PEAGAGGGAY LHVWVIFEMP VSQALGMLAY NSRIPAAKKK KRKSKKKKKG 100
    GAKVQSSPPR VPVSNLFPNN QYPEGEIVEY KNENSYRTTN EEKRYLDRMN 150
    NNFLQEYRQA AEVHRQVRQY AQKTIKPGQT LTEIAEGIED AVRALTGHQG 200
    LEEGDNLKGG MGFPCGLSIN HCAAHYTPNA GNKMVLQQGD VMKVDFGAHI 250
    NGRIVDSAFT MTFDPVYDPL LEAVKDATNT GIREAGIDVR MSDIGAAIQE 300
    AMESYEVELN GTMYPVKCIR NLNGHNIDRH IIHGGKSVPI VKGSDQTKME 350
    EGETFAIETF GSTGKGYVRE DMETSHYALI PDAPSVPLRL SSAKNLLNVI 400
    NKNFGTLPFC RRYLDRLGQE KYLLGLNNLV SSGIVQDYPP LCDVKGSYTA 450
    QFEHTILLRP TVKEVISRGD DY 472
    Length:472
    Mass (Da):51,959
    Last modified:May 3, 2011 - v2
    Checksum:i07C2C43062731656
    GO

    Sequence cautioni

    The sequence EDP50069.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499598 Genomic DNA. Translation: EDP50069.1. Sequence problems.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499598 Genomic DNA. Translation: EDP50069.1 . Sequence problems.

    3D structure databases

    ProteinModelPortali B0Y5N4.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOGENOMi HOG000226278.
    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: CEA10 / CBS 144.89 / FGSC A1163.

    Entry informationi

    Entry nameiMAP22_ASPFC
    AccessioniPrimary (citable) accession number: B0Y5N4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 44 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

    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