ID   PIMT_WHEAT              Reviewed;         230 AA.
AC   Q43209;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase;
DE            Short=PIMT;
DE            EC=2.1.1.77;
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
DE   AltName: Full=Protein L-isoaspartyl methyltransferase;
DE   AltName: Full=Protein-beta-aspartate methyltransferase;
GN   Name=PCM;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=cv. Augusta;
RX   PubMed=8198620; DOI=10.1021/bi00092a020;
RA   Mudgett M.B., Clarke S.;
RT   "Characterization of plant L-isoaspartyl methyltransferases that may be
RT   involved in seed survival: purification, cloning, and sequence analysis of
RT   the wheat germ enzyme.";
RL   Biochemistry 32:11100-11111(1993).
CC   -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues
CC       in peptides and proteins that result from spontaneous decomposition of
CC       normal L-aspartyl and L-asparaginyl residues. It plays a role in the
CC       repair and/or degradation of damaged proteins. This enzyme does not act
CC       on D-aspartyl residues.
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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highest contents in seeds.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
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DR   EMBL; L07941; AAA34297.1; -; mRNA.
DR   PIR; T06519; T06519.
DR   AlphaFoldDB; Q43209; -.
DR   SMR; Q43209; -.
DR   STRING; 4565.Traes_2DL_F483F3232.1; -.
DR   PRIDE; Q43209; -.
DR   EnsemblPlants; TraesCAD_scaffold_104953_01G000200.1; TraesCAD_scaffold_104953_01G000200.1; TraesCAD_scaffold_104953_01G000200.
DR   EnsemblPlants; TraesCLE_scaffold_112874_01G000200.1; TraesCLE_scaffold_112874_01G000200.1; TraesCLE_scaffold_112874_01G000200.
DR   EnsemblPlants; TraesPAR_scaffold_119715_01G000200.1; TraesPAR_scaffold_119715_01G000200.1; TraesPAR_scaffold_119715_01G000200.
DR   EnsemblPlants; TraesROB_scaffold_050953_01G000500.1; TraesROB_scaffold_050953_01G000500.1; TraesROB_scaffold_050953_01G000500.
DR   EnsemblPlants; TraesWEE_scaffold_135832_01G000200.1; TraesWEE_scaffold_135832_01G000200.1; TraesWEE_scaffold_135832_01G000200.
DR   Gramene; TraesCAD_scaffold_104953_01G000200.1; TraesCAD_scaffold_104953_01G000200.1; TraesCAD_scaffold_104953_01G000200.
DR   Gramene; TraesCLE_scaffold_112874_01G000200.1; TraesCLE_scaffold_112874_01G000200.1; TraesCLE_scaffold_112874_01G000200.
DR   Gramene; TraesPAR_scaffold_119715_01G000200.1; TraesPAR_scaffold_119715_01G000200.1; TraesPAR_scaffold_119715_01G000200.
DR   Gramene; TraesROB_scaffold_050953_01G000500.1; TraesROB_scaffold_050953_01G000500.1; TraesROB_scaffold_050953_01G000500.
DR   Gramene; TraesWEE_scaffold_135832_01G000200.1; TraesWEE_scaffold_135832_01G000200.1; TraesWEE_scaffold_135832_01G000200.
DR   eggNOG; KOG1661; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q43209; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IBA:GO_Central.
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.
DR   PROSITE; PS01279; PCMT; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..230
FT                   /note="Protein-L-isoaspartate O-methyltransferase"
FT                   /id="PRO_0000111883"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000250"
FT   VARIANT         18
FT                   /note="E -> D"
FT   VARIANT         41
FT                   /note="A -> N"
FT   VARIANT         52
FT                   /note="T -> N"
FT   VARIANT         54
FT                   /note="S -> L"
FT   VARIANT         122
FT                   /note="V -> A"
FT   VARIANT         143
FT                   /note="S -> L"
FT   VARIANT         147
FT                   /note="S -> E"
FT   VARIANT         156
FT                   /note="A -> V"
FT   VARIANT         203
FT                   /note="A -> S"
FT   VARIANT         208
FT                   /note="S -> T"
FT   VARIANT         210
FT                   /note="R -> V"
FT   VARIANT         214
FT                   /note="S -> T"
SQ   SEQUENCE   230 AA;  24708 MW;  7B600453B4B56C35 CRC64;
     MAQFWAEGSL EKNNALVEYL KQYGVVRTDK VAEVMETIDR ALFVPEGFTP YTDSPMPIGY
     NATISAPHMH ATCLELLKDY LQPGMHALDV GSGSGYLTAC FAMMVGPEGR AVGIEHIPEL
     VVASTENVER SAAAALMKDG SLSFHVSDGR LGWPDAAPYD AIHVGAAAPE IPRPLLEQLK
     PGGRMVIPVG TYSQDLQVID KSADGSTSVR NDASVRYVPL TSRSAQLQDS