ID A0A182DXJ5_ONCOC Unreviewed; 323 AA.
AC A0A182DXJ5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|RuleBase:RU003802};
DE EC=2.1.1.77 {ECO:0000256|RuleBase:RU003802};
GN ORFNames=NOO_LOCUS374 {ECO:0000313|EMBL:VDK61995.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t00374-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t00374-RA}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t00374-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDK61995.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU003802};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369, ECO:0000256|RuleBase:RU003802}.
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; UYRW01000035; VDK61995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182DXJ5; -.
DR STRING; 42157.A0A182DXJ5; -.
DR WBParaSite; nOo.2.0.1.t00374-RA; nOo.2.0.1.t00374-RA; nOo.2.0.1.g00374.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; Unassembled WGS sequence.
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:SF0; 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:UP000271087};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU003802};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU003802}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..323
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033257002"
FT REGION 33..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 35658 MW; AD8413632BB42A11 CRC64;
MPSMCPQFCY LLLLITTNCM LLAVFASTVH CDSSKDKGYC SEEESTDREE SIKSISATNI
EQEGANLQHS EREEAIKSRK MKIFEGATRL LTRNIRNAMA WMSGADSNVD LVNNLQNNNL
FKDERVRDAM LEVDRGDFAP VTPYGDHPVS IGHGATISAP HMHASSLELL KDHLREGNRA
LDVGSGSGYL TACMAIMVGK TGKVVGIDHI QALVDDSRRN IRKHHEDLLT DRRIILMKGD
GRKGYEKEAP YNAIHVGAAA PEIPTELIEQ LAKGGRMLIP LGPEGGPQRF VQVDKDVDGN
VTQKSLMGVI YVPLTDEQHQ LHN
//
