ID   PIMT1_METAC             Reviewed;         251 AA.
AC   Q8TT93;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase 1;
DE            EC=2.1.1.77;
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase 1;
DE   AltName: Full=Protein L-isoaspartyl methyltransferase 1;
DE   AltName: Full=Protein-beta-aspartate methyltransferase 1;
DE            Short=PIMT 1;
GN   Name=pcm1; Synonyms=pcm-1; OrderedLocusNames=MA_0544;
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; AAM03988.1; -; Genomic_DNA.
DR   RefSeq; WP_011020593.1; NC_003552.1.
DR   AlphaFoldDB; Q8TT93; -.
DR   SMR; Q8TT93; -.
DR   STRING; 188937.MA_0544; -.
DR   EnsemblBacteria; AAM03988; AAM03988; MA_0544.
DR   GeneID; 1472436; -.
DR   KEGG; mac:MA_0544; -.
DR   HOGENOM; CLU_055432_2_0_2; -.
DR   InParanoid; Q8TT93; -.
DR   OMA; TISAIHM; -.
DR   OrthoDB; 88476at2157; -.
DR   PhylomeDB; Q8TT93; -.
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..251
FT                   /note="Protein-L-isoaspartate O-methyltransferase 1"
FT                   /id="PRO_0000111914"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        98
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   251 AA;  27873 MW;  7B3481CCB7A995E3 CRC64;
     MPERKEKGQV SVGAAEDRGK KGHSEKKDKR KQEENQEELH QLEEMRERLI RRIGIHGADE
     KVLKAMLRVP RHLFVPEYAK KGAYIDTPLE IGFGQTISAP HMVAIMCDLL ELSEGLKVLE
     IGAGSGYNAA VMGELVGKSG HVYTVERIEP LVDFARENLK KAGYENVTVL LDDGSMGYSK
     CAPYDRIVVT CAAPDIPEPL LEQLKPGGIM IIPVGDYIQE LVRIKKDPEG KIHEEKRGGV
     VFVPLIGKYG F