GenomeNet

Database: UniProt
Entry: A0A2Z2HS08_9EURY
LinkDB: A0A2Z2HS08_9EURY
Original site: A0A2Z2HS08_9EURY 
ID   A0A2Z2HS08_9EURY        Unreviewed;       256 AA.
AC   A0A2Z2HS08;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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   ORFNames=B1756_07400 {ECO:0000313|EMBL:ARS89583.1};
OS   Natrarchaeobaculum aegyptiacum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrarchaeobaculum.
OX   NCBI_TaxID=745377 {ECO:0000313|EMBL:ARS89583.1, ECO:0000313|Proteomes:UP000250088};
RN   [1] {ECO:0000313|Proteomes:UP000250088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JW/NM-HA 15 {ECO:0000313|Proteomes:UP000250088};
RA   Zhao B.;
RT   "Natronthermophilus aegyptiacus gen. nov.,sp. nov., an aerobic, extremely
RT   halophilic alkalithermophilic archaeon isolated from the athalassohaline
RT   Wadi An Natrun, Egypt.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP019893; ARS89583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z2HS08; -.
DR   KEGG; naj:B1756_07400; -.
DR   OrthoDB; 194891at2157; -.
DR   Proteomes; UP000250088; Chromosome.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
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:ARS89583.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000250088};
KW   Transferase {ECO:0000313|EMBL:ARS89583.1}.
SQ   SEQUENCE   256 AA;  28251 MW;  D7E4286993A90B68 CRC64;
     MDPAVLRDDM VDGLESPPRE VIESEAVAEA MRAVPRRLFL PDDRNAYADS DHEVRGSRIL
     APSTVARLLE ALALEPDDDV LVVGVGVGYT AAVCAEIVGE TNAHAVDIAR PLVFDARENL
     ERAGYGGVLV DCRDGANGLP EYAPFDRILL EAAVAESPRA LREQLSPSGR LVYPRLRDAR
     GQRLEVQTAA GERSPRGIVE FDPLLVAGEQ TGAVERNRTA REDREFAARR AESRRGWEQE
     WIEWDAGSRR SNWPSR
//
DBGET integrated database retrieval system