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   16-JUN-2009, entry version 52.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase;
DE            Short=PIMT;
DE            EC=2.1.1.77;
DE   AltName: Full=Protein-beta-aspartate methyltransferase;
DE   AltName: Full=Protein L-isoaspartyl methyltransferase;
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
GN   Name=PCM;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RC   STRAIN=cv. Augusta;
RX   MEDLINE=94032221; PubMed=8198620; DOI=10.1021/bi00092a020;
RA   Mudgett M.B., Clarke S.;
RT   "Characterization of plant L-isoaspartyl methyltransferases that may
RT   be involved in seed survival: purification, cloning, and sequence
RT   analysis of the wheat germ enzyme.";
RL   Biochemistry 32:11100-11111(1993).
CC   -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl
CC       residues in peptides and proteins that result from spontaneous
CC       decomposition of normal L-aspartyl and L-asparaginyl residues. It
CC       plays a role in the repair and/or degradation of damaged proteins.
CC       This enzyme does not act on D-aspartyl residues.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-
CC       isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate
CC       alpha-methyl ester.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highest contents in seeds.
CC   -!- SIMILARITY: Belongs to the L-isoaspartyl/D-aspartyl protein
CC       methyltransferase family.
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DR   EMBL; L07941; AAA34297.1; -; mRNA.
DR   PIR; T06519; T06519.
DR   UniGene; Ta.162; -.
DR   HSSP; P22061; 1I1N.
DR   Gramene; Q43209; -.
DR   BRENDA; 2.1.1.77; 253.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-meth...; IEA:EC.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR000682; PCMT.
DR   PANTHER; PTHR11579; PCMT; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   TIGRFAMs; TIGR00080; pimt; 1.
DR   PROSITE; PS01279; PCMT; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    230       Protein-L-isoaspartate O-
FT                                methyltransferase.
FT                                /FTId=PRO_0000111883.
FT   ACT_SITE     65     65       By similarity.
FT   VARIANT      18     18       E -> D.
FT   VARIANT      41     41       A -> N.
FT   VARIANT      52     52       T -> N.
FT   VARIANT      54     54       S -> L.
FT   VARIANT     122    122       V -> A.
FT   VARIANT     143    143       S -> L.
FT   VARIANT     147    147       S -> E.
FT   VARIANT     156    156       A -> V.
FT   VARIANT     203    203       A -> S.
FT   VARIANT     208    208       S -> T.
FT   VARIANT     210    210       R -> V.
FT   VARIANT     214    214       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
//