ID   PIMT_METMA              Reviewed;         243 AA.
AC   Q8PW90;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 49.
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=MM_1706;
OS   Methanosarcina mazei (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
RX   MEDLINE=22120827; PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM31402.1; -; Genomic_DNA.
DR   RefSeq; NP_633730.1; -.
DR   HSSP; Q8TZR3; 1JG1.
DR   GeneID; 1480048; -.
DR   GenomeReviews; AE008384_GR; MM_1706.
DR   KEGG; mma:MM_1706; -.
DR   NMPDR; fig|192952.1.peg.1706; -.
DR   HOGENOM; Q8PW90; -.
DR   OMA; Q8PW90; RERFAPP.
DR   BioCyc; MMAZ192952:MM1706-MON; -.
DR   BRENDA; 2.1.1.77; 261165.
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    243       Protein-L-isoaspartate O-
FT                                methyltransferase.
FT                                /FTId=PRO_0000111918.
FT   ACT_SITE     87     87       By similarity.
SQ   SEQUENCE   243 AA;  27120 MW;  DF83E0D0591A1B1C CRC64;
     MPERRGIVLV NAVSEKDLGE DKRKREKEKE CEKLRKLLVE GLEGFVIDEK VLQAMLRVPR
     HRFVPEYEQR AAYVDMPLEI GHGQTISAPH MVAMMCEILE LAEGHKVLEI GAGSGYNAAV
     MSELVGKTGH IYTVERVEPL ANFAKKNLKE AGYKNVTVLL ENGSMGYPGY APYDRIAVTC
     AAPNIPETLL EQLKPGGIMV IPVGSYSQEL IRVKKDSTGK IYRKKKGDVI FVPMIGKHGF
     RRI
//