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Q9FV52

- MAP1B_ARATH

UniProt

Q9FV52 - MAP1B_ARATH

Protein

Methionine aminopeptidase 1B, chloroplastic

Gene

MAP1B

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      Previous versions | rss
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    Functioni

    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 sitei199 – 1991SubstrateUniRule annotation
    Metal bindingi216 – 2161Divalent metal cation 1UniRule annotation
    Metal bindingi227 – 2271Divalent metal cation 1UniRule annotation
    Metal bindingi227 – 2271Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi290 – 2901Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei297 – 2971SubstrateUniRule annotation
    Metal bindingi322 – 3221Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi353 – 3531Divalent metal cation 1UniRule annotation
    Metal bindingi353 – 3531Divalent 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:AT1G13270-MONOMER.
    ARA:GQT-2392-MONOMER.

    Protein family/group databases

    MEROPSiM24.A05.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1B, chloroplasticUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1BUniRule annotation
    Short name:
    MetAP 1BUniRule annotation
    Alternative name(s):
    Peptidase M 1BUniRule annotation
    Gene namesi
    Name:MAP1B
    Ordered Locus Names:At1g13270
    ORF Names:T6J4.3
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G13270.

    Subcellular locationi

    Plastidchloroplast 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. mitochondrion Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5555ChloroplastUniRule annotationAdd
    BLAST
    Chaini56 – 369314Methionine aminopeptidase 1B, chloroplasticPRO_0000045805Add
    BLAST

    Proteomic databases

    PaxDbiQ9FV52.
    PRIDEiQ9FV52.

    Expressioni

    Tissue specificityi

    Ubiquitous. Preferentially expressed in green tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ9FV52.
    GenevestigatoriQ9FV52.

    Interactioni

    Protein-protein interaction databases

    BioGridi23127. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FV52.
    SMRiQ9FV52. Positions 91-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030427.
    InParanoidiQ9FV52.
    KOiK01265.
    OMAiATTYEAM.
    PhylomeDBiQ9FV52.

    Family and domain databases

    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01974. MetAP_1.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 1 hit.
    TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
    PROSITEiPS00680. MAP_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: Q9FV52-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASSVFLSSF SSSSSLQLCS SFHGEYLAPS RCFLGAPVTS SSLSLSGKKN    50
    SYSPRQFHVS AKKVSGLEEA IRIRKMRELE TKSKVRRNPP LRRGRVSPRL 100
    LVPDHIPRPP YVESGVLPDI SSEFQIPGPE GIAKMRAACE LAARVLNYAG 150
    TLVKPSVTTN EIDKAVHDMI IEAGAYPSPL GYGGFPKSVC TSVNECMCHG 200
    IPDSRQLQSG DIINIDVTVY LDGYHGDTSR TFFCGEVDEG FKRLVKVTEE 250
    CLERGIAVCK DGASFKKIGK RISEHAEKFG YNVVERFVGH GVGPVFHSEP 300
    LIYHYRNDEP GLMVEGQTFT IEPILTIGTT ECVTWPDNWT TLTADGGVAA 350
    QFEHTILITR TGSEILTKC 369
    Length:369
    Mass (Da):40,424
    Last modified:January 24, 2006 - v2
    Checksum:i0D28974852F33747
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341L → I in AAG33975. (PubMed:11060042)Curated
    Sequence conflicti243 – 2431R → Q in AAG33975. (PubMed:11060042)Curated
    Sequence conflicti254 – 2541R → K in AAG33975. (PubMed:11060042)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250961 mRNA. Translation: AAG33975.1.
    AC011810 Genomic DNA. Translation: AAG09564.1.
    CP002684 Genomic DNA. Translation: AEE28993.1.
    BT000449 mRNA. Translation: AAN17426.1.
    BT001213 mRNA. Translation: AAN65100.1.
    PIRiC86267.
    RefSeqiNP_172785.1. NM_101198.3. [Q9FV52-1]
    UniGeneiAt.21097.

    Genome annotation databases

    EnsemblPlantsiAT1G13270.1; AT1G13270.1; AT1G13270. [Q9FV52-1]
    GeneIDi837887.
    KEGGiath:AT1G13270.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250961 mRNA. Translation: AAG33975.1 .
    AC011810 Genomic DNA. Translation: AAG09564.1 .
    CP002684 Genomic DNA. Translation: AEE28993.1 .
    BT000449 mRNA. Translation: AAN17426.1 .
    BT001213 mRNA. Translation: AAN65100.1 .
    PIRi C86267.
    RefSeqi NP_172785.1. NM_101198.3. [Q9FV52-1 ]
    UniGenei At.21097.

    3D structure databases

    ProteinModelPortali Q9FV52.
    SMRi Q9FV52. Positions 91-367.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 23127. 1 interaction.

    Protein family/group databases

    MEROPSi M24.A05.

    Proteomic databases

    PaxDbi Q9FV52.
    PRIDEi Q9FV52.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G13270.1 ; AT1G13270.1 ; AT1G13270 . [Q9FV52-1 ]
    GeneIDi 837887.
    KEGGi ath:AT1G13270.

    Organism-specific databases

    GeneFarmi 2345. 184.
    TAIRi AT1G13270.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030427.
    InParanoidi Q9FV52.
    KOi K01265.
    OMAi ATTYEAM.
    PhylomeDBi Q9FV52.

    Enzyme and pathway databases

    BioCyci ARA:AT1G13270-MONOMER.
    ARA:GQT-2392-MONOMER.

    Gene expression databases

    ArrayExpressi Q9FV52.
    Genevestigatori Q9FV52.

    Family and domain databases

    Gene3Di 3.90.230.10. 1 hit.
    HAMAPi MF_01974. MetAP_1.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002467. Pept_M24A_MAP1.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 1 hit.
    TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
    PROSITEi PS00680. MAP_1. 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 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(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.

    Entry informationi

    Entry nameiMAP1B_ARATH
    AccessioniPrimary (citable) accession number: Q9FV52
    Secondary accession number(s): Q9FX70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 96 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