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)

A6RTU0

- MAP2_BOTFB

UniProt

A6RTU0 - MAP2_BOTFB

Protein

Methionine aminopeptidase 2

Gene

BC1G_04189

Organism
Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (21 Aug 2007)
      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 sitei201 – 2011SubstrateUniRule annotation
    Metal bindingi221 – 2211Divalent metal cation 1UniRule annotation
    Metal bindingi232 – 2321Divalent metal cation 1UniRule annotation
    Metal bindingi232 – 2321Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi301 – 3011Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei309 – 3091SubstrateUniRule annotation
    Metal bindingi334 – 3341Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi429 – 4291Divalent metal cation 1UniRule annotation
    Metal bindingi429 – 4291Divalent 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
    ORF Names:BC1G_04189
    OrganismiBotryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
    Taxonomic identifieri332648 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotrytis

    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 – 448448Methionine aminopeptidase 2PRO_0000407644Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi332648.A6RTU0.

    Structurei

    3D structure databases

    ProteinModelPortaliA6RTU0.
    SMRiA6RTU0. Positions 79-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    KOiK01265.
    OMAiIQICEEL.

    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    A6RTU0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQVTDALK NLKVKDPNAV VESAAEAKAN GNAQPEAEAE DSDDDDEEPV    50
    NGEGAGEGGA KKKRKRKKKP KKKAGANPKV QSSPPRVLLS NLFPSGEYPV 100
    GEEVEYRDEN NYRTTSEEKR YLDRMNNDFL QEYRQGAEIH RQVRQYAKAN 150
    IKPGQTLTEI AEGIEDSVRA LTGHPGLEEG DNIKGGVAFP TGVNLDHIAA 200
    HYSPNAGNKT VLAYENVMKV DFGVHINGRI VDSAFTIAFD PMYDNLLEAV 250
    KQATNTGIKE AGIDARLGEI GEHIQETMES YEVEIKGQTY QVKPIRNLNG 300
    HDILQWKIHG GKSVPIVKSN DQTKMEEGEV FAIETFGSTG NGYVRDDLEC 350
    SHYAKVADAP NVPLRIASAG KLLNVINKNF GTLPFCRRYL DRLGQDKYLL 400
    GLNALVSHGI VQDYPPLVDK KGSYTAQFEH TIVLRPNCKE VISRGDDY 448
    Length:448
    Mass (Da):49,382
    Last modified:August 21, 2007 - v1
    Checksum:iBAE7123D8B732BAB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476856 Genomic DNA. Translation: EDN21182.1.
    RefSeqiXP_001557579.1. XM_001557529.1.

    Genome annotation databases

    GeneIDi5438178.
    KEGGibfu:BC1G_04189.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476856 Genomic DNA. Translation: EDN21182.1 .
    RefSeqi XP_001557579.1. XM_001557529.1.

    3D structure databases

    ProteinModelPortali A6RTU0.
    SMRi A6RTU0. Positions 79-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 332648.A6RTU0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5438178.
    KEGGi bfu:BC1G_04189.

    Phylogenomic databases

    eggNOGi COG0024.
    KOi K01265.
    OMAi IQICEEL.

    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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
      Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
      , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
      PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: B05.10.

    Entry informationi

    Entry nameiMAP2_BOTFB
    AccessioniPrimary (citable) accession number: A6RTU0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 50 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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