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Database: UniProt
Entry: A0A0W8D698_PHYNI
LinkDB: A0A0W8D698_PHYNI
Original site: A0A0W8D698_PHYNI 
ID   A0A0W8D698_PHYNI        Unreviewed;       495 AA.
AC   A0A0W8D698;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Aldo/keto reductase family {ECO:0000313|EMBL:KUF91908.1};
GN   ORFNames=AM587_10013696 {ECO:0000313|EMBL:KUF73680.1}, AM588_10006131
GN   {ECO:0000313|EMBL:KUF91908.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF91908.1, ECO:0000313|Proteomes:UP000054636};
RN   [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, Race 0
RC   {ECO:0000313|EMBL:KUF73680.1}, Race 1 {ECO:0000313|EMBL:KUF91908.1},
RC   and race 1 {ECO:0000313|Proteomes:UP000054636};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUF91908.1}.
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DR   EMBL; LNFO01006026; KUF73680.1; -; Genomic_DNA.
DR   EMBL; LNFP01000523; KUF91908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8D698; -.
DR   STRING; 4790.A0A0W8D698; -.
DR   EnsemblProtists; KUF73680; KUF73680; AM587_10013696.
DR   EnsemblProtists; KUF91908; KUF91908; AM588_10006131.
DR   OMA; GYTEEWL; -.
DR   OrthoDB; 1077100at2759; -.
DR   Proteomes; UP000052943; Unassembled WGS sequence.
DR   Proteomes; UP000054636; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd21150; PUA_NSun6-like; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF34; TRNA (CYTOSINE(72)-C(5))-METHYLTRANSFERASE NSUN6; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01472; PUA; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50890; PUA; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          154..483
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         254..260
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         278
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         305
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         362
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   495 AA;  53838 MW;  E66B805F92701FF1 CRC64;
     MAPLEDTSGV VGATTLDAFS VSFPDQVEQE LGDAYGEPHW TNIKRALARP PAFTAVRVNT
     LKLSLEEALQ ALKPHLDGFN TQLAALDASR QPIEAFAHAS LPDVLMIPSS PSGQTIVEYN
     PELKSIVVDR LCGEAVLRGS DIFARGVMSA SAGINAEDEV NVFVDLDHNH TRGSDFATHN
     GRKLLIARGV TKMARTEIFR AVRGLAVTQL VRVCPDAPPM NGVMRGQIYV QNLPCSVVAH
     VLDPQEGDVI LDMCAAPGGK TSHVATLMRN KGILVACDRS KRKALELRTL CEDLHLDCVE
     PLKMDSTHAL LPKDKVDTAP QSGDYTSVAQ VLARAKQITP SQARLLQVEG FYPETFDRIL
     LDPPCSALGL RPRLLHAGDA DNLAEYTNMQ RNFLWVAAFL LKPGGTLVYS TCTINPKENE
     QMVHHALQNY PLKLVSQGEA HLGDRGLPGQ GLTDEEASLV QRFDPANTDL DTMGFFCAKF
     IKTGPIRQDQ TPATP
//
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