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Q9FV49

- MAP21_ARATH

UniProt

Q9FV49 - MAP21_ARATH

Protein

Methionine aminopeptidase 2A

Gene

MAP2A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      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 sitei194 – 1941SubstrateUniRule annotation
    Metal bindingi214 – 2141Divalent metal cation 1UniRule annotation
    Metal bindingi225 – 2251Divalent metal cation 1UniRule annotation
    Metal bindingi225 – 2251Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi294 – 2941Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei302 – 3021SubstrateUniRule annotation
    Metal bindingi327 – 3271Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi422 – 4221Divalent metal cation 1UniRule annotation
    Metal bindingi422 – 4221Divalent 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. N-terminal protein amino acid modification Source: TAIR
    2. protein initiator methionine removal Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT2G44180-MONOMER.

    Protein family/group databases

    MEROPSiM24.A02.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 2AUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2AUniRule annotation
    Short name:
    MetAP 2AUniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:MAP2AUniRule annotation
    Ordered Locus Names:At2g44180
    ORF Names:F6E13.31
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G44180.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441Methionine aminopeptidase 2APRO_0000148970Add
    BLAST

    Proteomic databases

    PaxDbiQ9FV49.
    PRIDEiQ9FV49.

    Expressioni

    Tissue specificityi

    Ubiquitous. Preferentially expressed in roots.1 Publication

    Gene expression databases

    ArrayExpressiQ9FV49.
    GenevestigatoriQ9FV49.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FV49.
    SMRiQ9FV49. Positions 80-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi63 – 7513Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    InParanoidiQ9FV49.
    KOiK01265.
    OMAiERYKLHA.
    PhylomeDBiQ9FV49.

    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.

    Q9FV49-1 [UniParc]FASTAAdd to Basket

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    MAIGNPEVAT MGKENTEAES SNGNESQLSS DLTKSLDLAE VKEDEKDNNQ    50
    EEEDGLKAEA STKKKKKKSK SKKKKSSLQQ TDPPSIPVLE LFPSGDFPQG 100
    EIQQYNDDNL WRTTSEEKRE MERLQKPIYN SLRQAAEVHR QVRKYMRSIL 150
    KPGMLMIDLC ETLENTVRKL ISENGLQAGI AFPTGCSLNN VAAHWTPNSG 200
    DKTVLQYDDV MKLDFGTHID GHIVDSAFTV AFNPMFDPLL AASRDATYTG 250
    IKEAGVDVRL CDVGAAVQEV MESYEVEING KVYQVKSIRN LNGHSIGRYQ 300
    IHAEKSVPNV RGGEQTKMEE GELYAIETFG STGKGYVRED LECSHYMKNY 350
    DVGHVPLRLP RAKQLLATIN KNFSTLAFCR RYLDRLGETK YLMALKNLCD 400
    SGIIEPCPPV CDVKGSYISQ FEHTILLRPT CKEIISKGDD Y 441
    Length:441
    Mass (Da):49,395
    Last modified:January 24, 2006 - v2
    Checksum:iFEC98F6679F0D573
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121G → E in AAG33978. (PubMed:11060042)Curated
    Sequence conflicti51 – 511Missing in AAG33978. (PubMed:11060042)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250964 mRNA. Translation: AAG33978.1.
    AC004005 Genomic DNA. Translation: AAC23422.2.
    CP002685 Genomic DNA. Translation: AEC10386.1.
    BT006476 mRNA. Translation: AAP21284.1.
    PIRiT00698.
    RefSeqiNP_566013.1. NM_129981.4.
    UniGeneiAt.19509.

    Genome annotation databases

    EnsemblPlantsiAT2G44180.1; AT2G44180.1; AT2G44180.
    GeneIDi819025.
    KEGGiath:AT2G44180.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250964 mRNA. Translation: AAG33978.1 .
    AC004005 Genomic DNA. Translation: AAC23422.2 .
    CP002685 Genomic DNA. Translation: AEC10386.1 .
    BT006476 mRNA. Translation: AAP21284.1 .
    PIRi T00698.
    RefSeqi NP_566013.1. NM_129981.4.
    UniGenei At.19509.

    3D structure databases

    ProteinModelPortali Q9FV49.
    SMRi Q9FV49. Positions 80-441.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M24.A02.

    Proteomic databases

    PaxDbi Q9FV49.
    PRIDEi Q9FV49.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G44180.1 ; AT2G44180.1 ; AT2G44180 .
    GeneIDi 819025.
    KEGGi ath:AT2G44180.

    Organism-specific databases

    GeneFarmi 1935. 191.
    TAIRi AT2G44180.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    InParanoidi Q9FV49.
    KOi K01265.
    OMAi ERYKLHA.
    PhylomeDBi Q9FV49.

    Enzyme and pathway databases

    BioCyci ARA:AT2G44180-MONOMER.

    Gene expression databases

    ArrayExpressi Q9FV49.
    Genevestigatori Q9FV49.

    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. "Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms."
      Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.
      EMBO J. 19:5916-5929(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiMAP21_ARATH
    AccessioniPrimary (citable) accession number: Q9FV49
    Secondary accession number(s): O80587
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3