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E5R4J3

- MAP22_LEPMJ

UniProt

E5R4J3 - MAP22_LEPMJ

Protein

Methionine aminopeptidase 2-2

Gene

Lema_P046670

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
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    • History
      Entry version 22 (01 Oct 2014)
      Sequence version 1 (08 Feb 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 sitei204 – 2041SubstrateUniRule annotation
    Metal bindingi224 – 2241Divalent metal cation 1UniRule annotation
    Metal bindingi235 – 2351Divalent metal cation 1UniRule annotation
    Metal bindingi235 – 2351Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi304 – 3041Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei312 – 3121SubstrateUniRule annotation
    Metal bindingi337 – 3371Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi432 – 4321Divalent metal cation 1UniRule annotation
    Metal bindingi432 – 4321Divalent 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:Lema_P046670
    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 – 451451Methionine aminopeptidase 2-2PRO_0000407607Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliE5R4J3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi60 – 667Poly-Lys
    Compositional biasi69 – 724Poly-Lys

    Sequence similaritiesi

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

    Phylogenomic databases

    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.

    E5R4J3-1 [UniParc]FASTAAdd to Basket

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    MAAQVEDDVA NLKLDDSTTK PTNGTSQPDS KLSAEAEDSD DDAEGDGNGT    50
    GEAGADGAAK KKKKRKPRKK KKAGTSATAG AKSQTSPPRV LISDLFPNDS 100
    YPEGEICEYR DENSYRTTNE EKRHLDRMNN DFLTDYRKGA EIHRQVRQWA 150
    ANWIKPGMTL TEIAEGIEDS VRALTGHQGL EEGDAQKAGM GFPTGLSINH 200
    CAAHYTPNAG NKVVVNYEDV MKVDFGVHIN GRIVDSAFTK TFDPVYDPLV 250
    EACKAATNAG IKEAGIDVRM SDIGAAIQEV MESYEVEIGG KMLPVKCIRN 300
    LNGHSIGHYT IHGGKTVPIV KGSDQTKMEE GETFAIETFG STGKGYVRDD 350
    METSHYALRP DAPKVALRIS SAKSLLASIT KNFGTLPFCR RYLDRLGHDK 400
    YLLGLNNLVS SGIVEAYPPL CDIKGSWTAQ SEHTFVLRPT CKEVLSRGDD 450
    Y 451
    Length:451
    Mass (Da):49,158
    Last modified:February 8, 2011 - v1
    Checksum:i08407BBF6A063CA3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FP929083 Genomic DNA. Translation: CBX91961.1.
    RefSeqiXP_003835326.1. XM_003835278.1.

    Genome annotation databases

    EnsemblFungiiCBX91961; CBX91961; LEMA_P046670.1.
    GeneIDi13284777.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FP929083 Genomic DNA. Translation: CBX91961.1 .
    RefSeqi XP_003835326.1. XM_003835278.1.

    3D structure databases

    ProteinModelPortali E5R4J3.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CBX91961 ; CBX91961 ; LEMA_P046670.1 .
    GeneIDi 13284777.

    Phylogenomic databases

    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: JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8.

    Entry informationi

    Entry nameiMAP22_LEPMJ
    AccessioniPrimary (citable) accession number: E5R4J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 22 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