Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

C5GLJ6

- MAP22_AJEDR

UniProt

C5GLJ6 - MAP22_AJEDR

Protein

Methionine aminopeptidase 2-2

Gene

BDCG_05228

Organism
Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 32 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • 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 sitei216 – 2161SubstrateUniRule annotation
    Metal bindingi237 – 2371Divalent metal cation 1UniRule annotation
    Metal bindingi248 – 2481Divalent metal cation 1UniRule annotation
    Metal bindingi248 – 2481Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi317 – 3171Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei325 – 3251SubstrateUniRule annotation
    Metal bindingi350 – 3501Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi445 – 4451Divalent metal cation 1UniRule annotation
    Metal bindingi445 – 4451Divalent 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:BDCG_05228
    OrganismiAjellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis)
    Taxonomic identifieri559297 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces
    ProteomesiUP000002039: 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 – 464464Methionine aminopeptidase 2-2PRO_0000407616Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliC5GLJ6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi71 – 8414Lys-richAdd
    BLAST

    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]
    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.

    C5GLJ6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSKTPNDHR RGPNESSPHA AIDTINPPKH AAASGLLHGP LEGETEDGED    50
    EDDDKTGADL KSVGQLNNST KKKNKRKKNK KKKKTLLGGL QTTPPRVALS 100
    SIFYDQRYPE AEIVGYTTNN DNLQRITAEE FRHLCVVNDM DDEFLNDYRK 150
    AAEVHRQVRQ YVQTITKPGI AMSQLAQEIE DGVRALTDHQ GIETGDALKA 200
    GMAFPTGLCL NNIGAHWTPN PGAKEVILQY DDVLKVDFGV HVNGRIVDSA 250
    YTMAFNPVYD DLLTAVKAAT NTGLKEAGID ARIDCISEAI QEVMESYEVE 300
    LNRKIIPVKA VRNITGHNIL RYKIHGDKQV PFVKTHTNQR MEEGDIFAIE 350
    TFGSTGKAYL DDDIGIYGYF CDEHASAAGL HHSSAKSLLK TIKDNFGTLV 400
    FSRRYLERLG VKSYHLGMRS LVSKGIVQSY APLVDVPGSY VAQFEHTVLL 450
    RPNCKEVISR GDDY 464
    Length:464
    Mass (Da):51,414
    Last modified:July 28, 2009 - v1
    Checksum:iE914113CB23390D3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EQ999977 Genomic DNA. Translation: EEQ90108.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EQ999977 Genomic DNA. Translation: EEQ90108.1 .

    3D structure databases

    ProteinModelPortali C5GLJ6.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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 ]
    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. "The genome sequence of Blastomyces dermatitidis strain ER-3."
      Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Klein B., Goldman B., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Heiman D.I., Hepburn T.A., Saif S., Shea T.D., Shenoy N., Sykes S.
      , Galagan J.E., Nusbaum C., Birren B.W.
      Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ER-3 / ATCC MYA-2586.

    Entry informationi

    Entry nameiMAP22_AJEDR
    AccessioniPrimary (citable) accession number: C5GLJ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 32 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