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Q56Y85

- MAP22_ARATH

UniProt

Q56Y85 - MAP22_ARATH

Protein

Methionine aminopeptidase 2B

Gene

MAP2B

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 78 (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 sitei192 – 1921SubstrateUniRule annotation
    Metal bindingi212 – 2121Divalent metal cation 1UniRule annotation
    Metal bindingi223 – 2231Divalent metal cation 1UniRule annotation
    Metal bindingi223 – 2231Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi292 – 2921Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei300 – 3001SubstrateUniRule annotation
    Metal bindingi325 – 3251Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi420 – 4201Divalent metal cation 1UniRule annotation
    Metal bindingi420 – 4201Divalent 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
    2. protein processing Source: TAIR

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT3G59990-MONOMER.
    ARA:GQT-1753-MONOMER.
    ARA:GQT-2672-MONOMER.
    ARA:GQT-2673-MONOMER.

    Protein family/group databases

    MEROPSiM24.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 2BUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2BUniRule annotation
    Short name:
    MetAP 2BUniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:MAP2BUniRule annotation
    Ordered Locus Names:At3g59990
    ORF Names:F24G16.26
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G59990.

    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 – 439439Methionine aminopeptidase 2BPRO_0000148971Add
    BLAST

    Proteomic databases

    PaxDbiQ56Y85.
    PRIDEiQ56Y85.

    Expressioni

    Tissue specificityi

    Ubiquitous. Preferentially expressed in roots.1 Publication

    Gene expression databases

    GenevestigatoriQ56Y85.

    Structurei

    3D structure databases

    ProteinModelPortaliQ56Y85.
    SMRiQ56Y85. Positions 78-439.
    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

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    InParanoidiQ56Y85.
    KOiK01265.
    OMAiIQICEEL.
    PhylomeDBiQ56Y85.

    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.

    Q56Y85-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASESPDVAV VAPVVENGGA ESSNGKEEQL ESELSKKLEI AEDGQEENDG    50
    EEGSKAETST KKKKKKNKSK KKKELPQQTD PPSIPVVELF PSGEFPEGEI 100
    QEYKDDNLWR TTSEEKRELE RFEKPIYNSV RRAAEVHRQV RKYVRSIVKP 150
    GMLMTDICET LENTVRKLIS ENGLQAGIAF PTGCSLNWVA AHWTPNSGDK 200
    TVLQYDDVMK LDFGTHIDGH IIDCAFTVAF NPMFDPLLAA SREATYTGIK 250
    EAGIDVRLCD IGAAIQEVME SYEVEINGKV FQVKSIRNLN GHSIGPYQIH 300
    AGKSVPIVKG GEQTKMEEGE FYAIETFGST GKGYVREDLE CSHYMKNFDA 350
    GHVPLRLPRA KQLLATINKN FSTLAFCRRY LDRIGETKYL MALKNLCDSG 400
    IVQPYPPLCD VKGSYVSQFE HTILLRPTCK EVLSKGDDY 439
    Length:439
    Mass (Da):49,060
    Last modified:January 24, 2006 - v2
    Checksum:iEC1C79EA1B49D3BF
    GO

    Sequence cautioni

    The sequence BAD94472.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAB75818.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti270 – 2701E → K in AAL38337. (PubMed:14593172)Curated
    Sequence conflicti270 – 2701E → K in AAN15382. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF300880 mRNA. Translation: AAG34551.1.
    AL138647 Genomic DNA. Translation: CAB75818.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE79996.1.
    CP002686 Genomic DNA. Translation: AEE79997.1.
    CP002686 Genomic DNA. Translation: AEE79998.1.
    CP002686 Genomic DNA. Translation: AEE79999.1.
    AY065161 mRNA. Translation: AAL38337.1.
    BT000063 mRNA. Translation: AAN15382.1.
    AY084710 mRNA. Translation: AAM61284.1.
    AK221438 mRNA. Translation: BAD94472.1. Different initiation.
    PIRiT47823.
    RefSeqiNP_001030898.1. NM_001035821.1.
    NP_001190139.1. NM_001203210.1.
    NP_567089.1. NM_115862.3.
    NP_850725.1. NM_180394.1.
    UniGeneiAt.16912.

    Genome annotation databases

    EnsemblPlantsiAT3G59990.1; AT3G59990.1; AT3G59990.
    AT3G59990.2; AT3G59990.2; AT3G59990.
    AT3G59990.3; AT3G59990.3; AT3G59990.
    AT3G59990.4; AT3G59990.4; AT3G59990.
    GeneIDi825169.
    KEGGiath:AT3G59990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF300880 mRNA. Translation: AAG34551.1 .
    AL138647 Genomic DNA. Translation: CAB75818.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE79996.1 .
    CP002686 Genomic DNA. Translation: AEE79997.1 .
    CP002686 Genomic DNA. Translation: AEE79998.1 .
    CP002686 Genomic DNA. Translation: AEE79999.1 .
    AY065161 mRNA. Translation: AAL38337.1 .
    BT000063 mRNA. Translation: AAN15382.1 .
    AY084710 mRNA. Translation: AAM61284.1 .
    AK221438 mRNA. Translation: BAD94472.1 . Different initiation.
    PIRi T47823.
    RefSeqi NP_001030898.1. NM_001035821.1.
    NP_001190139.1. NM_001203210.1.
    NP_567089.1. NM_115862.3.
    NP_850725.1. NM_180394.1.
    UniGenei At.16912.

    3D structure databases

    ProteinModelPortali Q56Y85.
    SMRi Q56Y85. Positions 78-439.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M24.002.

    Proteomic databases

    PaxDbi Q56Y85.
    PRIDEi Q56Y85.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G59990.1 ; AT3G59990.1 ; AT3G59990 .
    AT3G59990.2 ; AT3G59990.2 ; AT3G59990 .
    AT3G59990.3 ; AT3G59990.3 ; AT3G59990 .
    AT3G59990.4 ; AT3G59990.4 ; AT3G59990 .
    GeneIDi 825169.
    KEGGi ath:AT3G59990.

    Organism-specific databases

    GeneFarmi 1944. 191.
    TAIRi AT3G59990.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    InParanoidi Q56Y85.
    KOi K01265.
    OMAi IQICEEL.
    PhylomeDBi Q56Y85.

    Enzyme and pathway databases

    BioCyci ARA:AT3G59990-MONOMER.
    ARA:GQT-1753-MONOMER.
    ARA:GQT-2672-MONOMER.
    ARA:GQT-2673-MONOMER.

    Miscellaneous databases

    PROi Q56Y85.

    Gene expression databases

    Genevestigatori Q56Y85.

    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. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      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.
    5. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-439.
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiMAP22_ARATH
    AccessioniPrimary (citable) accession number: Q56Y85
    Secondary accession number(s): Q8VZ89, Q9FPV8, Q9M1X7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 78 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