ID   R9AIU6_WALI9            Unreviewed;       974 AA.
AC   R9AIU6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Protein-L-isoaspartate(D-aspartate) O-methyltransferase {ECO:0000313|EMBL:EOR02035.1};
GN   ORFNames=J056_003711 {ECO:0000313|EMBL:EOR02035.1};
OS   Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR02035.1, ECO:0000313|Proteomes:UP000014064};
RN   [1] {ECO:0000313|Proteomes:UP000014064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX   PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA   Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT   "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT   ichthyophaga: haloadaptations present and absent.";
RL   BMC Genomics 14:617-617(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; KE007228; EOR02035.1; -; Genomic_DNA.
DR   RefSeq; XP_009267202.1; XM_009268927.1.
DR   AlphaFoldDB; R9AIU6; -.
DR   STRING; 1299270.R9AIU6; -.
DR   GeneID; 20376663; -.
DR   KEGG; wic:J056_003711; -.
DR   eggNOG; KOG1661; Eukaryota.
DR   HOGENOM; CLU_304868_0_0_1; -.
DR   OMA; RIWWYLV; -.
DR   OrthoDB; 303909at2759; -.
DR   Proteomes; UP000014064; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR   InterPro; IPR000682; PCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   NCBIfam; TIGR00080; pimt; 1.
DR   PANTHER; PTHR31001:SF88; MISCELLANEOUS ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR   PANTHER; PTHR31001; UNCHARACTERIZED TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR   PROSITE; PS01279; PCMT; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:EOR02035.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW   Transferase {ECO:0000313|EMBL:EOR02035.1}.
FT   DOMAIN          30..61
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50048"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   974 AA;  108965 MW;  470BE0984FBB8279 CRC64;
     MSSAIFQTAD AATGTSEIKP KKTRNRQALS CTECKRRKIK CDREHPCGAC KKRGEQYKCI
     WEEKPASKPG KSSAASSDDV SCLREQLSDT QACLHALANF LRFSGIPIPQ NIFDSIGVTT
     SPSSTGILAD MDFENEETAA AFTLEGIAMG RKPDESFNDE AALLRRKRTD SIGSVGRRTV
     QDTPIPSNSS TSVPVYCDPP SITTSLDHTS TPLATFPFTP KPEQITMTKD ILQYLPNKHK
     ADILVSFYIQ HLEWFHKPLH VPTFLSDYAH YWQEMSVGFA YDNIDSKWMA LYASVLCVAT
     HFGGEYYYTG GFAFSNPDVE TRNEKEADTY YQISRSALSQ SDFLINHSIE AIQTIIILGL
     YLHNKNQTET HLILMSTAIK MAQLMGLSRI PDEIPGGEAE GDVLEREMGR RLWHSLVFQD
     SFNASASSYS YAIHVDQMTT SVPANADDEG LVRQKEINCQ PDSVWTDMSY FRSKLQFANI
     TRKIVDTLNR DSKGSYAFVI EMDAEYRAAL DRIPTFLRLD LAEYDAAVLS MKPCRAWERL
     MMSFTIHNRL MRLHRGYMTE GYTNREYAYS TQACVASAKT LLELMKEGQK YNWPASRWWV
     VLIQCWTASV VILIDLFHTV DTIEADEKSK EVGETLMIFR DIQHTSTVAK KAVLTLDRLL
     QEDKQRRGDG VPAKKRRISV EGFTPVGLAP NFPGLHGDTA TPRQPQNMLD SVFTSPVDGG
     RTVWENMFMK ELDFLNDSNV DVNWKFDEAW LCSAKTNVEL IKNLRSSNLI HSDIVANAMK
     KVDRAHYVRI KAAAYEDSPQ SIGHSATISA PHMHAHATEN LLSLLQPGYK VLDVGSGSGY
     SCAVFHQLIG NNGTVVGIDH IEQLVENSVD NLKRDGLEDA INSGAIKMIA GDGRQGVAEH
     GPYNAIHVGA AAPRMPDVLI DQLATPGRMF VPVEKTGGYG QSIWQVDKDE NGIVHKEELF
     PVMYVPLTER ELQR
//