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Database: UniProt
Entry: A0A2I3RLG8_PANTR
LinkDB: A0A2I3RLG8_PANTR
Original site: A0A2I3RLG8_PANTR 
ID   A0A2I3RLG8_PANTR        Unreviewed;       250 AA.
AC   A0A2I3RLG8; A0A2J8PS11;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|RuleBase:RU003802};
DE            EC=2.1.1.77 {ECO:0000256|RuleBase:RU003802};
GN   Name=PCMT1 {ECO:0000313|Ensembl:ENSPTRP00000065186.1,
GN   ECO:0000313|VGNC:VGNC:49015};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000065186.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000065186.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000065186.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00035815};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12706;
CC         Evidence={ECO:0000256|ARBA:ARBA00035815};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005369, ECO:0000256|RuleBase:RU003802}.
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DR   EMBL; AACZ04054481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I3RLG8; -.
DR   Ensembl; ENSPTRT00000082288.1; ENSPTRP00000065186.1; ENSPTRG00000018699.6.
DR   VGNC; VGNC:49015; PCMT1.
DR   GeneTree; ENSGT00950000183032; -.
DR   Proteomes; UP000002277; Chromosome 6.
DR   Bgee; ENSPTRG00000018699; Expressed in hindlimb stylopod muscle and 22 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR000682; PCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00080; pimt; 1.
DR   PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11579:SF7; PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O-METHYLTRANSFERASE; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01279; PCMT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|RuleBase:RU003802};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU003802};
KW   Transferase {ECO:0000256|RuleBase:RU003802}.
SQ   SEQUENCE   250 AA;  26375 MW;  4334E876DF652CE1 CRC64;
     MPGARSGGSG GDGSNSGSYS GDASGAVTVW EVVSLLGKLL GTVVALKVVL YLLRVCLAMA
     WKSGGASHSE LIHNLRSFQA TISAPHMHAY ALELLFDQLH EGAKALDVGS GSGILTACFA
     RMVGCTGKVI GIDHIKELVD DSINNVRKDD PTLLSSGRVQ LVVGDGRMGY AEEAPYDAIH
     VGAAAPVVPQ ALIDQLKPGG RLILPVGPAG GNQMLEQYDK LQDGSIKMKP LMGVIYVPLT
     DKEKQWSRWK
//
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