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Database: UniProt
Entry: F2SIJ0_TRIRC
LinkDB: F2SIJ0_TRIRC
Original site: F2SIJ0_TRIRC 
ID   F2SIJ0_TRIRC            Unreviewed;       235 AA.
AC   F2SIJ0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|RuleBase:RU003802};
DE            EC=2.1.1.77 {ECO:0000256|RuleBase:RU003802};
GN   ORFNames=TERG_02678 {ECO:0000313|EMBL:EGD86421.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD86421.1, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; GG700649; EGD86421.1; -; Genomic_DNA.
DR   RefSeq; XP_003237970.1; XM_003237922.1.
DR   AlphaFoldDB; F2SIJ0; -.
DR   STRING; 559305.F2SIJ0; -.
DR   GeneID; 10376925; -.
DR   VEuPathDB; FungiDB:TERG_02678; -.
DR   eggNOG; KOG1661; Eukaryota.
DR   HOGENOM; CLU_055432_0_0_1; -.
DR   InParanoid; F2SIJ0; -.
DR   OMA; TISAIHM; -.
DR   OrthoDB; 303909at2759; -.
DR   Proteomes; UP000008864; 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   ECO:0000313|EMBL:EGD86421.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU003802};
KW   Transferase {ECO:0000256|RuleBase:RU003802, ECO:0000313|EMBL:EGD86421.1}.
SQ   SEQUENCE   235 AA;  25264 MW;  BDCAAEC066A93D1C CRC64;
     MAWQCTGRSN FQLIENLFTA DLIKSQRVKN AMLKVDRGHY SPSNPYNDSP QSIGFAATIS
     APHMHAHACE YLLPFLHPGA RVLDIGCGSG YLSHVFAELI TDAPASDGCV VGIDHIQGLV
     DLSLKNLAKS EEGRKLLDSG KIKIVKGDGR KGWAEGGPYD AIHVGAAAAT MHSELIDQLR
     APGRMFIPVD AESTTSVLGS QGQHVWIVDK AEDGSVNKKK VFGVSYVPLT DAPEE
//
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