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Database: UniProt
Entry: A0A183IYC2_9BILA
LinkDB: A0A183IYC2_9BILA
Original site: A0A183IYC2_9BILA 
ID   A0A183IYC2_9BILA        Unreviewed;       135 AA.
AC   A0A183IYC2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SBAD_LOCUS8620 {ECO:0000313|EMBL:VDP18245.1};
OS   Soboliphyme baturini.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX   NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0000893101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SBAD_0000893101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP18245.1, ECO:0000313|Proteomes:UP000270296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UZAM01011796; VDP18245.1; -; Genomic_DNA.
DR   WBParaSite; SBAD_0000893101-mRNA-1; SBAD_0000893101-mRNA-1; SBAD_0000893101.
DR   Proteomes; UP000050793; Unplaced.
DR   Proteomes; UP000270296; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:InterPro.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000270296};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   135 AA;  14905 MW;  988099E114A2968F CRC64;
     MIDVLILRIP SFVLLLMLVI QKVVCLLAFR AVCSMAWISH GVNNTDMVQA LKRNGIITSD
     RVENAMLAVD RGNYSLRNPY YDSPQGIGYG ATISAPHMVI VFATLHYTPP GSVGNVLTVE
     LKNDCTHKME PFAHC
//
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