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)

B2B738

- MAP2_PODAN

UniProt

B2B738 - MAP2_PODAN

Protein

Methionine aminopeptidase 2

Gene

PODANS_2_9800

Organism
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (20 May 2008)
      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 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 bindingi298 – 2981Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei306 – 3061SubstrateUniRule annotation
    Metal bindingi331 – 3311Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi426 – 4261Divalent metal cation 1UniRule annotation
    Metal bindingi426 – 4261Divalent 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 2UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2UniRule annotation
    Short name:
    MetAP 2UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Ordered Locus Names:PODANS_2_9800
    OrganismiPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
    Taxonomic identifieri515849 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora
    ProteomesiUP000001197: Chromosome 2

    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 – 445445Methionine aminopeptidase 2PRO_0000407665Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliB2B738.
    SMRiB2B738. Positions 77-445.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi61 – 7313Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01265.

    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.

    B2B738-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQAPVDEI AQLSVSDAAT TKPKPGLDSA TATNGNLNRD SDDSDDDAEN    50
    AAPGAETGAA KKKKKRKPKK KKKNPTAQSD PPRVLISQLF PDKVYPKGEE 100
    VEYVNENRYR TTNEEKRHLD NLKNDFYNDY RHAAEAHRQT RQWAQKNIKP 150
    GWSLTDIANG IEDSVRALVG HQGLEEGDAL KAGMGFPTGL SLNHCAAHYN 200
    PNAGNKMVLQ QDDVLKVDIG VHVNGNIVDS AFTLAFNPRY DPLLEACKAA 250
    TNEGLKQAGI DARLGEIGGY IQEVMESYEV ELDGNTYQVK PIRNLNGHTI 300
    LPYNIHGGKS VPIVKSNDQT KMEEGDVFAI ETFGSTGNGY VHEEGEISHY 350
    AKRMDAPKVD LRLSSAKSLL NVINKNFGTL PFCRRYLDRL GQDKYLLGLN 400
    SLVANGVVES YPPLVDKKGS YTAQFEHTIL IRPTVKEVIS RGDDY 445
    Length:445
    Mass (Da):49,022
    Last modified:May 20, 2008 - v1
    Checksum:iD4973E6DC966821E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU640366 Genomic DNA. Translation: CAP73616.1.
    RefSeqiXP_001911788.1. XM_001911753.1.

    Genome annotation databases

    GeneIDi6196226.
    KEGGipan:PODANSg8833.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU640366 Genomic DNA. Translation: CAP73616.1 .
    RefSeqi XP_001911788.1. XM_001911753.1.

    3D structure databases

    ProteinModelPortali B2B738.
    SMRi B2B738. Positions 77-445.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6196226.
    KEGGi pan:PODANSg8833.

    Phylogenomic databases

    KOi K01265.

    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: S / ATCC MYA-4624 / DSM 980 / FGSC 10383.

    Entry informationi

    Entry nameiMAP2_PODAN
    AccessioniPrimary (citable) accession number: B2B738
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 42 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