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
//