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Database: UniProt
Entry: M5GDJ8_DACPD
LinkDB: M5GDJ8_DACPD
Original site: M5GDJ8_DACPD 
ID   M5GDJ8_DACPD            Unreviewed;       228 AA.
AC   M5GDJ8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=DACRYDRAFT_22103 {ECO:0000313|EMBL:EJU02468.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU02468.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJU02468.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU02468.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; JH795862; EJU02468.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5GDJ8; -.
DR   STRING; 1858805.M5GDJ8; -.
DR   HOGENOM; CLU_055432_0_0_1; -.
DR   OMA; TISAIHM; -.
DR   OrthoDB; 303909at2759; -.
DR   Proteomes; UP000030653; Unassembled WGS sequence.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:InterPro.
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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:EJU02468.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW   Transferase {ECO:0000313|EMBL:EJU02468.1}.
SQ   SEQUENCE   228 AA;  24823 MW;  05E8C97AB1B91947 CRC64;
     MAWMCSGRTN KELVQRMIDS KLIKSERVAA AMKATDRASY VRYKEDAYVD SPQSIGYAAT
     ISAPHMHAHA AENLLPLLFP GAKVLDVGSG SGYTAAIFHR LVSSEGKKGL VVGVEHISEL
     TDWSVENLKR DGLAKAVEDG EIVMFAGDGR KGDPERGPFN AIHVGAASPE LPQVLVDQLA
     KPGRMFIPVG TNEQAIIQVD KDEQGAVTMK ELFGVMYVPL TDKTKQWR
//
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