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Q9FV50

- MAP1D_ARATH

UniProt

Q9FV50 - MAP1D_ARATH

Protein

Methionine aminopeptidase 1D, chloroplastic/mitochondrial

Gene

MAP1D

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 95 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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 sitei180 – 1801SubstrateUniRule annotation
    Metal bindingi197 – 1971Divalent metal cation 1UniRule annotation
    Metal bindingi208 – 2081Divalent metal cation 1UniRule annotation
    Metal bindingi208 – 2081Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi271 – 2711Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei278 – 2781SubstrateUniRule annotation
    Metal bindingi303 – 3031Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi334 – 3341Divalent metal cation 1UniRule annotation
    Metal bindingi334 – 3341Divalent 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
    3. response to abscisic acid Source: TAIR

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT4G37040-MONOMER.

    Protein family/group databases

    MEROPSiM24.A06.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1D, chloroplastic/mitochondrialUniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1DUniRule annotation
    Short name:
    MetAP 1DUniRule annotation
    Alternative name(s):
    Peptidase M 1DUniRule annotation
    Gene namesi
    Name:MAP1D
    Ordered Locus Names:At4g37040
    ORF Names:C7A10.320
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G37040.

    Subcellular locationi

    Plastidchloroplast 1 PublicationUniRule annotation. Mitochondrion 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Mitochondrion, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 350Methionine aminopeptidase 1D, chloroplastic/mitochondrialPRO_0000045807
    Initiator methioninei1 – 11RemovedBy similarity
    Transit peptidei2 – ?Chloroplast and mitochondrionUniRule annotation

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9FV50.
    PRIDEiQ9FV50.

    Expressioni

    Tissue specificityi

    Ubiquitous. Preferentially expressed in green tissues.1 Publication

    Gene expression databases

    GenevestigatoriQ9FV50.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT4G37040.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FV50.
    SMRiQ9FV50. Positions 35-348.
    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.
    InParanoidiQ9FV50.
    KOiK01265.
    OMAiFHEEPDV.
    PhylomeDBiQ9FV50.

    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.

    Q9FV50-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGVKSLQPR LISSFLGNNS IRSTQPLIHL FRFDLGRRHV SMQLSRTFSG    50
    LTDLLFNRRN EDEVIDGKRK RLRPGNVSPR RPVPGHITKP PYVDSLQAPG 100
    ISSGLEVHDK KGIECMRASG ILAARVRDYA GTLVKPGVTT DEIDEAVHNM 150
    IIENGAYPSP LGYGGFPKSV CTSVNECICH GIPDSRPLED GDIINIDVTV 200
    YLNGYHGDTS ATFFCGNVDE KAKKLVEVTK ESLDKAISIC GPGVEYKKIG 250
    KVIHDLADKH KYGVVRQFVG HGVGSVFHAD PVVLHFRNNE AGRMVLNQTF 300
    TIEPMLTIGS RNPIMWDDNW TVVTEDASLS AQFEHTILIT KDGAEILTKC 350
    Length:350
    Mass (Da):38,532
    Last modified:March 1, 2001 - v1
    Checksum:i0BB60261008FF99A
    GO

    Sequence cautioni

    The sequence CAB16790.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB80370.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250963 mRNA. Translation: AAG33977.1.
    Z99707 Genomic DNA. Translation: CAB16790.1. Sequence problems.
    AL161590 Genomic DNA. Translation: CAB80370.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86740.1.
    AK118314 mRNA. Translation: BAC42930.1.
    BT005680 mRNA. Translation: AAO64100.1.
    AY085839 mRNA. Translation: AAM63054.1.
    PIRiE85437.
    RefSeqiNP_568014.1. NM_119867.2.
    UniGeneiAt.4646.

    Genome annotation databases

    EnsemblPlantsiAT4G37040.1; AT4G37040.1; AT4G37040.
    GeneIDi829858.
    KEGGiath:AT4G37040.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250963 mRNA. Translation: AAG33977.1 .
    Z99707 Genomic DNA. Translation: CAB16790.1 . Sequence problems.
    AL161590 Genomic DNA. Translation: CAB80370.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86740.1 .
    AK118314 mRNA. Translation: BAC42930.1 .
    BT005680 mRNA. Translation: AAO64100.1 .
    AY085839 mRNA. Translation: AAM63054.1 .
    PIRi E85437.
    RefSeqi NP_568014.1. NM_119867.2.
    UniGenei At.4646.

    3D structure databases

    ProteinModelPortali Q9FV50.
    SMRi Q9FV50. Positions 35-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G37040.1-P.

    Protein family/group databases

    MEROPSi M24.A06.

    Proteomic databases

    PaxDbi Q9FV50.
    PRIDEi Q9FV50.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G37040.1 ; AT4G37040.1 ; AT4G37040 .
    GeneIDi 829858.
    KEGGi ath:AT4G37040.

    Organism-specific databases

    GeneFarmi 2344. 184.
    TAIRi AT4G37040.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030427.
    InParanoidi Q9FV50.
    KOi K01265.
    OMAi FHEEPDV.
    PhylomeDBi Q9FV50.

    Enzyme and pathway databases

    BioCyci ARA:AT4G37040-MONOMER.

    Gene expression databases

    Genevestigatori Q9FV50.

    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. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
      Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
      , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
      Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "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.
    7. "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].

    Entry informationi

    Entry nameiMAP1D_ARATH
    AccessioniPrimary (citable) accession number: Q9FV50
    Secondary accession number(s): Q9SW64
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 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