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PIMT_SCHPO
ID   PIMT_SCHPO              Reviewed;         230 AA.
AC   Q9URZ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable protein-L-isoaspartate O-methyltransferase {ECO:0000250|UniProtKB:P23506};
DE            Short=PIMT;
DE            EC=2.1.1.77 {ECO:0000250|UniProtKB:P23506};
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
DE   AltName: Full=Protein L-isoaspartyl methyltransferase;
DE   AltName: Full=Protein-beta-aspartate methyltransferase;
GN   Name=pcm2; ORFNames=SPAC869.08;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Initiates the repair of damaged proteins by catalyzing methyl
CC       esterification of L-isoaspartyl and D-aspartyl residues produced by
CC       spontaneous isomerization and racemization of L-aspartyl and L-
CC       asparaginyl residues in aging peptides and proteins.
CC       {ECO:0000250|UniProtKB:P23506}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-L-isoaspartate + S-adenosyl-L-methionine =
CC         [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:12705, Rhea:RHEA-COMP:12143, Rhea:RHEA-
CC         COMP:12144, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90596,
CC         ChEBI:CHEBI:90598; EC=2.1.1.77;
CC         Evidence={ECO:0000250|UniProtKB:P23506};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12706;
CC         Evidence={ECO:0000250|UniProtKB:P23506};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P22061}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:16823372}.
CC       Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB60018.1; -; Genomic_DNA.
DR   PIR; T39119; T39119.
DR   RefSeq; NP_595011.1; NM_001020442.2.
DR   AlphaFoldDB; Q9URZ1; -.
DR   SMR; Q9URZ1; -.
DR   BioGRID; 279805; 10.
DR   STRING; 4896.SPAC869.08.1; -.
DR   PaxDb; Q9URZ1; -.
DR   EnsemblFungi; SPAC869.08.1; SPAC869.08.1:pep; SPAC869.08.
DR   GeneID; 2543383; -.
DR   KEGG; spo:SPAC869.08; -.
DR   PomBase; SPAC869.08; pcm2.
DR   VEuPathDB; FungiDB:SPAC869.08; -.
DR   eggNOG; KOG1661; Eukaryota.
DR   HOGENOM; CLU_055432_0_2_1; -.
DR   InParanoid; Q9URZ1; -.
DR   OMA; TISAIHM; -.
DR   PhylomeDB; Q9URZ1; -.
DR   Reactome; R-SPO-5676934; Protein repair.
DR   PRO; PR:Q9URZ1; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; ISS:PomBase.
DR   GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR   GO; GO:0030091; P:protein repair; IC:PomBase.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR000682; PCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11579; PTHR11579; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00080; pimt; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..230
FT                   /note="Probable protein-L-isoaspartate O-methyltransferase"
FT                   /id="PRO_0000316247"
FT   ACT_SITE        60
FT                   /evidence="ECO:0000250|UniProtKB:Q27869"
FT   BINDING         57..60
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P22061"
FT   BINDING         65
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P22061"
FT   BINDING         89
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P22061"
FT   BINDING         110..111
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P22061"
FT   BINDING         148..149
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P22061"
FT   BINDING         221
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P22061"
SQ   SEQUENCE   230 AA;  25333 MW;  A38C89901812F792 CRC64;
     MFWSFNLSSN AALVQHLVES KFLTNQRAIK AMNATSRSFY CPLSPYMDSP QSIGYGVTIS
     APHMHATALQ ELEPVLQPGC SALDIGSGSG YLVAAMARMV APNGTVKGIE HIPQLVETSK
     KNLLKDINHD EVLMEMYKEK RLQINVGDGR MGTSEDEKFD AIHVGASASE LPQKLVDQLK
     SPGKILIPIG TYSQNIYLIE KNEQGKISKR TLFPVRYVPL TDSPDDSSDY
 
 
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