ID   PIMT2_METAC             Reviewed;         238 AA.
AC   Q8TT94;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase 2;
DE            EC=2.1.1.77;
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase 2;
DE   AltName: Full=Protein L-isoaspartyl methyltransferase 2;
DE   AltName: Full=Protein-beta-aspartate methyltransferase 2;
DE            Short=PIMT 2;
GN   Name=pcm2; Synonyms=pcm-2; OrderedLocusNames=MA_0543;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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 (By similarity).
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
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DR   EMBL; AE010299; AAM03987.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TT94; -.
DR   SMR; Q8TT94; -.
DR   STRING; 188937.MA_0543; -.
DR   EnsemblBacteria; AAM03987; AAM03987; MA_0543.
DR   KEGG; mac:MA_0543; -.
DR   HOGENOM; CLU_055432_2_0_2; -.
DR   InParanoid; Q8TT94; -.
DR   OMA; MVDTQVR; -.
DR   PhylomeDB; Q8TT94; -.
DR   Proteomes; UP000002487; Chromosome.
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   GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00090; PIMT; 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   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..238
FT                   /note="Protein-L-isoaspartate O-methyltransferase 2"
FT                   /id="PRO_0000111915"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   238 AA;  26970 MW;  9B7EF47C884E035F CRC64;
     MVLVNAISEK DYIKDSRRRK KEEKEFEKLR KLLVEGLEDI VRDKKVLKAM FRVPRHRFVP
     EYEQRAAYTD RPLEIGHGQT ISTPHTVALM CEILELSEGH KVLEIGTGSG YNAAVMAELV
     GKTGHIYSVE RIEPLVNFAR KNLEQMGYDN VTVLLENGSM GYPRYAPYDR IAVTCAAPTI
     PKALLEQLKP GGIMVIPVGD YSQELIRVKK DSNGNIYKKR KGEVIFVPML GRHGFPRS