ID A0A0W1RV09_9GAMM Unreviewed; 668 AA.
AC A0A0W1RV09;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE EC=2.1.1.77 {ECO:0000256|HAMAP-Rule:MF_00090};
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein L-isoaspartyl methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE AltName: Full=Protein-beta-aspartate methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE Short=PIMT {ECO:0000256|HAMAP-Rule:MF_00090};
GN Name=pcm {ECO:0000256|HAMAP-Rule:MF_00090};
GN ORFNames=AUR63_07480 {ECO:0000313|EMBL:KTG17492.1};
OS Guyparkeria sp. XI15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Thioalkalibacteraceae; Guyparkeria.
OX NCBI_TaxID=1766620 {ECO:0000313|EMBL:KTG17492.1, ECO:0000313|Proteomes:UP000053033};
RN [1] {ECO:0000313|Proteomes:UP000053033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XI15 {ECO:0000313|Proteomes:UP000053033};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloferax marisrubri sp. nov., isolated from the Discovery deep brine-
RT seawater interface in the Red Sea.";
RL Submitted (DEC-2015) 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. {ECO:0000256|HAMAP-
CC Rule:MF_00090}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00090};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369, ECO:0000256|HAMAP-Rule:MF_00090}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00090}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTG17492.1}.
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; LOPX01000003; KTG17492.1; -; Genomic_DNA.
DR RefSeq; WP_058574197.1; NZ_LOPX01000003.1.
DR AlphaFoldDB; A0A0W1RV09; -.
DR STRING; 1766620.AUR63_07480; -.
DR Proteomes; UP000053033; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd14728; Ere-like; 1.
DR Gene3D; 1.20.1440.30; Biosynthetic Protein domain; 1.
DR Gene3D; 3.40.1660.10; EreA-like (biosynthetic domain); 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00090; PIMT; 1.
DR InterPro; IPR007815; Emycin_Estase.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00080; pimt; 1.
DR PANTHER; PTHR31299; ESTERASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05850)-RELATED; 1.
DR PANTHER; PTHR31299:SF0; PRIBOSYLTRAN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05139; Erythro_esteras; 1.
DR Pfam; PF01135; PCMT; 1.
DR SUPFAM; SSF159501; EreA/ChaN-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090,
KW ECO:0000313|EMBL:KTG17492.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053033};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:KTG17492.1}.
SQ SEQUENCE 668 AA; 74259 MW; E449372320858511 CRC64;
MPDRDQASRR EAMVDYQVQA RGVRAPRVLD AMRRVPREMF VPVDMREFAY EDTALPIAAG
QTITQPAIVA MMVEALALEG GERVLDVGTG SGYAAAVLAC IAERVYSIER IGELADLAGQ
ALASGGFHNV EVRTGDGSLG WPEAAPFDAI MVAAGAPAVP EALKHQLAIG GRLVVPVGSE
DEVQELVRIT RVGENDFRTE DIADVRFVPL VGEAGWAEGR PRPRRGFGRR TVSEADQRLI
ERIATVSEPF DSVDDLPLDG LLERIGDARL VLIGEASHGT SEFYRARQRI TRALIEEKGF
DFVAIEGDWP DAARIDHYVR HAEYPPSEWT AFARFPTWMW RNEEVRGFVD WLRGHNAERA
AADRVAFHGL DLYSLYNSIA AVLEYLDEVD PEAAAVARER YSCLTPFEPD PATYARMALS
PGYAGCEAPV VEMLRDLQQR HRVYAEKDGD RFLDAVQNAR LVANAEEYYR SMFYGSRSSW
NLRDTHMFET LEALLGHHGE GSRGVIWAHN SHVGDARATD MSRRGEFNIG QLCRARFGEA
VYSIGFGTDT GTVAAASNWD EPMEVKNLRP ALPDSYERLC HETGRAGFLL PLNAATADPE
VRTGLSEQRL ERAVGVIYRP ETERVSHYFH AELPRQFDEY IWVDRSRAVT PLDSRALAGA
ADTYPFGL
//
