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)

E4ZYY3

- MAP21_LEPMJ

UniProt

E4ZYY3 - MAP21_LEPMJ

Protein

Methionine aminopeptidase 2-1

Gene

Lema_P106830

Organism
Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 23 (01 Oct 2014)
      Sequence version 1 (08 Feb 2011)
      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 sitei212 – 2121SubstrateUniRule annotation
    Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
    Metal bindingi244 – 2441Divalent metal cation 1UniRule annotation
    Metal bindingi244 – 2441Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi313 – 3131Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei321 – 3211SubstrateUniRule annotation
    Metal bindingi346 – 3461Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi441 – 4411Divalent metal cation 1UniRule annotation
    Metal bindingi441 – 4411Divalent 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 2-1UniRule 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:Lema_P106830
    OrganismiLeptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam)
    Taxonomic identifieri985895 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaeLeptosphaeriaceaeLeptosphaeriaLeptosphaeria maculans complex
    ProteomesiUP000002668: Whole genome

    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 – 460460Methionine aminopeptidase 2-1PRO_0000407629Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliE4ZYY3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi77 – 804Poly-Lys

    Sequence similaritiesi

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

    Phylogenomic databases

    OMAiHISECIQ.
    OrthoDBiEOG7BGHW3.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_03175. MetAP_2_euk.
    InterProiIPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    SUPFAMiSSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    E4ZYY3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSKSPNGED RGPNGPSAKK AVASINPPKS AAASGLLRGA LEDQDEDGDD    50
    DEGKIGADMN VSEKTANGTK KRRRNNKKKK SAQAAQQTAP PRVEIATLFH 100
    NRPYPEGEIV EYGINDENLV RTTDEEFRHL AVANNMNDEF LRDYRKAAEV 150
    HRQVRQYAQT IAKPGISMTE LAREIEDGVR ALVGHQGIET GDSLKAGMGF 200
    PTGLCINNVA AHWTPNPGAR EVVLQHDDVL SIDFGVHVNG RIVDSAFTVA 250
    FNPMYDKLLT AVKAATNTGL KESGIDARMD YISETIQEVM ESYEVMINGK 300
    PLPVKALSSL SGHNILRYKI HGDKQVPFVK TRTSQRMEEG DVFAIETFGS 350
    TGIGRTRDDV GVYGYSRNEN VSTAGVHLAS AKSLLKAIDE NFGTLPFSRN 400
    YLERIGVKNY HLGMRSLIAS GVVECYAPLV DTPGSYVAQF EHTVLLRPNC 450
    KEIISRGDDY 460
    Length:460
    Mass (Da):50,338
    Last modified:February 8, 2011 - v1
    Checksum:iAE89CA76466A9747
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FP929129 Genomic DNA. Translation: CBX96418.1.
    RefSeqiXP_003839897.1. XM_003839849.1.

    Genome annotation databases

    EnsemblFungiiCBX96418; CBX96418; LEMA_P106830.1.
    GeneIDi13283230.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FP929129 Genomic DNA. Translation: CBX96418.1 .
    RefSeqi XP_003839897.1. XM_003839849.1.

    3D structure databases

    ProteinModelPortali E4ZYY3.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CBX96418 ; CBX96418 ; LEMA_P106830.1 .
    GeneIDi 13283230.

    Phylogenomic databases

    OMAi HISECIQ.
    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 IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55920. SSF55920. 2 hits.
    TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8.

    Entry informationi

    Entry nameiMAP21_LEPMJ
    AccessioniPrimary (citable) accession number: E4ZYY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 23 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