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O59730

- MAP1_SCHPO

UniProt

O59730 - MAP1_SCHPO

Protein

Methionine aminopeptidase 1

Gene

fma1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      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 bindingi209 – 2091Divalent metal cation 1UniRule annotation
    Metal bindingi220 – 2201Divalent metal cation 1UniRule annotation
    Metal bindingi220 – 2201Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi289 – 2891Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule 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: PomBase

    GO - Biological processi

    1. protein initiator methionine removal involved in protein maturation Source: PomBase

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Protein family/group databases

    MEROPSiM24.017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 1UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 1UniRule annotation
    Short name:
    MetAP 1UniRule annotation
    Alternative name(s):
    Peptidase M 1UniRule annotation
    Gene namesi
    Name:fma1
    ORF Names:SPBC3E7.10
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC3E7.10.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation. Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: PomBase
    2. cytosolic ribosome Source: UniProtKB-HAMAP
    3. nucleolus Source: PomBase
    4. nucleus Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 379379Methionine aminopeptidase 1PRO_0000148972Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei373 – 3731Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO59730.
    PaxDbiO59730.

    Interactioni

    Subunit structurei

    Associates with the 60S ribosomal subunit of the 80S translational complex.UniRule annotation

    Protein-protein interaction databases

    BioGridi277444. 17 interactions.
    MINTiMINT-4675730.
    STRINGi4896.SPBC3E7.10-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO59730.
    SMRiO59730. Positions 72-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni10 – 5344Zinc finger-like; important for proper ribosome associationUniRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000030427.
    KOiK01265.
    OMAiCFKRNWS.
    OrthoDBiEOG78WM23.
    PhylomeDBiO59730.

    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.

    O59730-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATEIAKHIC CGIDCNNEAD RLQCPKCLND GVKSYFCGQE CFRNSWNIHK    50
    HLHRPPNVEK REDGTYNPFP KFHFAGSLKP VYPLSPIRKV PPHIKRPDYA 100
    KTGVSRSEQI EGRSFKLKRL TPKEQEGMRK VCRLGREVLD AAAAAVRPGT 150
    TTDELDSIVH NACIERDCFP STLNYYAFPK SVCTSVNEII CHGIPDQRPL 200
    EDGDIVNIDV SLYHNGFHGD LNETYYVGDK AKANPDLVCL VENTRIALDK 250
    AIAAVKPGVL FQEFGNIIEK HTNSITEKQI SVVRTYCGHG INQLFHCSPS 300
    IPHYSHNKAP GIARPGMTFT IEPMLTLGPA RDITWPDDWT SSTASGRCSA 350
    QFEHTLLVTE TGCEVLTARL PNSPGGPLK 379
    Length:379
    Mass (Da):42,139
    Last modified:August 1, 1998 - v1
    Checksum:iD7A30E2886E3B248
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAA19013.1.
    PIRiT40384.
    RefSeqiNP_596097.1. NM_001022013.2.

    Genome annotation databases

    EnsemblFungiiSPBC3E7.10.1; SPBC3E7.10.1:pep; SPBC3E7.10.
    GeneIDi2540928.
    KEGGispo:SPBC3E7.10.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAA19013.1 .
    PIRi T40384.
    RefSeqi NP_596097.1. NM_001022013.2.

    3D structure databases

    ProteinModelPortali O59730.
    SMRi O59730. Positions 72-373.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 277444. 17 interactions.
    MINTi MINT-4675730.
    STRINGi 4896.SPBC3E7.10-1.

    Protein family/group databases

    MEROPSi M24.017.

    Proteomic databases

    MaxQBi O59730.
    PaxDbi O59730.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC3E7.10.1 ; SPBC3E7.10.1:pep ; SPBC3E7.10 .
    GeneIDi 2540928.
    KEGGi spo:SPBC3E7.10.

    Organism-specific databases

    PomBasei SPBC3E7.10.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000030427.
    KOi K01265.
    OMAi CFKRNWS.
    OrthoDBi EOG78WM23.
    PhylomeDBi O59730.

    Miscellaneous databases

    NextBioi 20802043.
    PROi O59730.

    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. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
      Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
      Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiMAP1_SCHPO
    AccessioniPrimary (citable) accession number: O59730
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3