ID   PIMT_AERPE              Reviewed;         260 AA.
AC   Q9YDA1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase;
DE            EC=2.1.1.77;
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
DE   AltName: Full=Protein L-isoaspartyl methyltransferase;
DE   AltName: Full=Protein-beta-aspartate methyltransferase;
DE            Short=PIMT;
GN   Name=pcm; OrderedLocusNames=APE_1011.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA79996.2; -; Genomic_DNA.
DR   PIR; D72699; D72699.
DR   AlphaFoldDB; Q9YDA1; -.
DR   SMR; Q9YDA1; -.
DR   STRING; 272557.APE_1011.1; -.
DR   EnsemblBacteria; BAA79996; BAA79996; APE_1011.1.
DR   KEGG; ape:APE_1011.1; -.
DR   PATRIC; fig|272557.25.peg.728; -.
DR   eggNOG; arCOG00976; Archaea.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-UniRule.
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..260
FT                   /note="Protein-L-isoaspartate O-methyltransferase"
FT                   /id="PRO_0000111911"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   260 AA;  28978 MW;  68330AD0A58DE77B CRC64;
     MKSPVAGAVL DPSTPPPTTG TSWRWPGLRD ADPYREARLR MVEQLRRSGL VTSRRVLEAM
     ARVPRHLFVP PEYRGMAYED RPLPIGHGQT ISAPGVVGRM LQLLDPQPGE KVLDVGAGSG
     YQSALLAELV TPGGRVYAVE RIPELAEYAR ENLEKTGYRG VVEVVVGDGS KGLPQHAPYH
     RIKVAAAAPK PPKPLVEQLA PGGRMVIPIG TPDLQILTII EKTPDGRVRE RRDIEVLFVP
     LIGEHGYRED WRKQYWQWWR