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Database: UniProt
Entry: C3MMU5_SULIL
LinkDB: C3MMU5_SULIL
Original site: C3MMU5_SULIL 
ID   C3MMU5_SULIL            Unreviewed;       220 AA.
AC   C3MMU5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=protein-L-isoaspartate(D-aspartate) O-methyltransferase {ECO:0000256|ARBA:ARBA00011890};
DE            EC=2.1.1.77 {ECO:0000256|ARBA:ARBA00011890};
GN   OrderedLocusNames=LS215_2879 {ECO:0000313|EMBL:ACP36812.1};
OS   Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=429572 {ECO:0000313|EMBL:ACP36812.1, ECO:0000313|Proteomes:UP000001747};
RN   [1] {ECO:0000313|EMBL:ACP36812.1, ECO:0000313|Proteomes:UP000001747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1 {ECO:0000313|Proteomes:UP000001747};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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.
CC       {ECO:0000256|ARBA:ARBA00025330}.
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:ARBA00029295};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005369}.
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DR   EMBL; CP001399; ACP36812.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3MMU5; -.
DR   KEGG; sis:LS215_2879; -.
DR   HOGENOM; CLU_055432_2_0_2; -.
DR   OMA; TISAIHM; -.
DR   OrthoDB; 33618at2157; -.
DR   Proteomes; UP000001747; Chromosome.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11579:SF0; PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O-METHYLTRANSFERASE; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:ACP36812.1};
KW   Transferase {ECO:0000313|EMBL:ACP36812.1}.
SQ   SEQUENCE   220 AA;  25030 MW;  A6335C9A9FA61EF4 CRC64;
     MGAKEDLLRS IKNSKLANAF IKVNREDFLP QLLKKYAYDP NYIDKPFYVT PNITTTALSL
     GIYILDILNL EENQKVLEIG TGIGYYTALI AEVVGENNIV SIEIDDTMFE YAKNVLLIRY
     PLIKLLKTDG SLGYEKEAPY DRIVVWAAAP TIPCKLYDQL KENGIMVVPI GGEKAQGLYR
     ITKTGYEPKI ERIGDVIFMK MRGLFGFYDN DDPNERRIKN
//
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