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Database: UniProt
Entry: Q0TXJ1_PHANO
LinkDB: Q0TXJ1_PHANO
Original site: Q0TXJ1_PHANO 
ID   Q0TXJ1_PHANO            Unreviewed;       222 AA.
AC   Q0TXJ1;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|RuleBase:RU003802};
DE            EC=2.1.1.77 {ECO:0000256|RuleBase:RU003802};
GN   ORFNames=SNOG_15751 {ECO:0000313|EMBL:EAT76846.1};
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT76846.1, ECO:0000313|Proteomes:UP000001055};
RN   [1] {ECO:0000313|Proteomes:UP000001055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC   {ECO:0000313|Proteomes:UP000001055};
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA   Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA   McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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}.
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DR   EMBL; CH445364; EAT76846.1; -; Genomic_DNA.
DR   RefSeq; XP_001805889.1; XM_001805837.1.
DR   AlphaFoldDB; Q0TXJ1; -.
DR   STRING; 321614.Q0TXJ1; -.
DR   EnsemblFungi; SNOT_15751; SNOT_15751; SNOG_15751.
DR   GeneID; 5982819; -.
DR   KEGG; pno:SNOG_15751; -.
DR   VEuPathDB; FungiDB:JI435_157510; -.
DR   eggNOG; KOG1661; Eukaryota.
DR   HOGENOM; CLU_055432_0_0_1; -.
DR   InParanoid; Q0TXJ1; -.
DR   OMA; TISAIHM; -.
DR   OrthoDB; 303909at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IBA:GO_Central.
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:UP000001055};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU003802};
KW   Transferase {ECO:0000256|RuleBase:RU003802}.
SQ   SEQUENCE   222 AA;  23866 MW;  6075E30F35560DA6 CRC64;
     MAWRSSGDTN EELIDNLKKN GLIETERVKE AMMKVDRAHF APSSPYRDYP QPIGHAATIS
     APHMHANACE SLLTHLPPGA KVLDIGSGSG YLTAVLANLV GPKGTVIGID HIQPLVDMSI
     ANLSKSEVGK KMLETGQVKF VLGDGRKGWK EGAPYDAIHV GAAAAEHHAE LTEQLKSPGR
     LFVPVADGGS QHIYIVDKKE DGSVEKKKLY GVQYVPLTDA PK
//
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