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Database: UniProt
Entry: S4RW29_PETMA
LinkDB: S4RW29_PETMA
Original site: S4RW29_PETMA 
ID   S4RW29_PETMA            Unreviewed;       251 AA.
AC   S4RW29;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
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:ENSPMAP00000009419.1};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000009419.1, ECO:0000313|Proteomes:UP000245300};
RN   [1] {ECO:0000313|Ensembl:ENSPMAP00000009419.1}
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   AlphaFoldDB; S4RW29; -.
DR   STRING; 7757.ENSPMAP00000009419; -.
DR   Ensembl; ENSPMAT00000009459.1; ENSPMAP00000009419.1; ENSPMAG00000008534.1.
DR   GeneTree; ENSGT00950000183032; -.
DR   HOGENOM; CLU_055432_0_0_1; -.
DR   OMA; MAWHCSG; -.
DR   Proteomes; UP000245300; Unplaced.
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:UP000245300};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU003802};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU003802}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..251
FT                   /note="Protein-L-isoaspartate O-methyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004522806"
SQ   SEQUENCE   251 AA;  27056 MW;  6CB34DEADBFF8317 CRC64;
     MGRPVAQLAA LLFGSVLVAR FAAMAWRSSG SSNAELVGNL RKNGVIKSER VYQVMLATDR
     KHYAKRNPYV DTPQSIGYHA TVSAPHMHAF ALELLQDRLQ EGASALDVGS GSGYLTACLA
     RMIGPRGKVI GVDHIQELVS EAKVNVQRDD PSLITSGRIK LILGDGRLGY LEGAPYDAIH
     VGAAAAIVPH ALLDQLKPGG RLVLPVGAAG GDQMLEQHDK LEDGTIRSKP LMSVMYVPLT
     DRDKQWSRDE L
//
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