ID   PIMT_SODGM              Reviewed;         208 AA.
AC   Q2NVM1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase;
DE            EC=2.1.1.77;
DE   AltName: Full=Protein-beta-aspartate methyltransferase;
DE            Short=PIMT;
DE   AltName: Full=Protein L-isoaspartyl methyltransferase;
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
GN   Name=pcm; OrderedLocusNames=SG0529;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K.,
RA   Hattori M., Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights
RT   into the symbiotic lifestyle of Sodalis glossinidius in the tsetse
RT   host.";
RL   Genome Res. 16:149-156(2006).
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       (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-
CC       isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate
CC       alpha-methyl ester.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the L-isoaspartyl/D-aspartyl protein
CC       methyltransferase family.
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DR   EMBL; AP008232; BAE73804.1; -; Genomic_DNA.
DR   RefSeq; YP_454209.1; -.
DR   GeneID; 3868230; -.
DR   GenomeReviews; AP008232_GR; SG0529.
DR   KEGG; sgl:SG0529; -.
DR   NMPDR; fig|343509.6.peg.1189; -.
DR   HOGENOM; Q2NVM1; -.
DR   OMA; Q2NVM1; YMVARMS.
DR   BioCyc; SGLO343509:SG0529-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-meth...; IEA:HAMAP.
DR   GO; GO:0006464; P:protein modification process; IEA:HAMAP.
DR   GO; GO:0030091; P:protein repair; IEA:HAMAP.
DR   HAMAP; MF_00090; -; 1.
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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    208       Protein-L-isoaspartate O-
FT                                methyltransferase.
FT                                /FTId=PRO_1000004829.
FT   ACT_SITE     59     59       By similarity.
SQ   SEQUENCE   208 AA;  23338 MW;  49639535825F18CD CRC64;
     MVDVRTQTLL AQLRQQGIRD ERLLQAMEAV PREHFIDEAF EHKAYDNTAL PIGLGQTISQ
     PYIVARMTEL LALWPESRVL EIGTGSGYQT AILAHLVKHV CSVERIKKLQ WQAKRRLKLL
     DLHNISTRHG DGWQGWLSRG PFDAIIVTAA PPEIPQALMA QLDEGGVMVL PVGDEQQHLT
     RVRRKGGEFV VDTVEAVRFV PLVKGELA
//