ID H3GDN6_PHYRM Unreviewed; 500 AA.
AC H3GDN6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra73687, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra73687}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra73687};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR EMBL; DS566001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3GDN6; -.
DR STRING; 164328.H3GDN6; -.
DR EnsemblProtists; Phyra73687; Phyra73687; Phyra73687.
DR VEuPathDB; FungiDB:PSURA_79272; -.
DR eggNOG; KOG1122; Eukaryota.
DR HOGENOM; CLU_005316_1_0_1; -.
DR InParanoid; H3GDN6; -.
DR OMA; YQGAMLY; -.
DR Proteomes; UP000005238; 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; IBA:GO_Central.
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; 2.
DR Pfam; PF01472; PUA; 1.
DR PRINTS; PR02008; RCMTFAMILY.
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:UP000005238};
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..487
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 416
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 366
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 500 AA; 54179 MW; BD84E157069817B1 CRC64;
MAPLEGSSAV PSATTLDAFS VTFPDQVEQE LGAAYGEPHW TNIKRALARP PAFTAVRVNT
LKLSRDEALQ ALQPHLNEFN AQLAALDASR QPIEAFAHAS LPDVLMIPSS PNGDTTVAFN
PELKSIVVDR LCGEAVLRGS DIFARGVMSA SSGINAEDPV NVFVDLDHNH TRGSDFASHN
GRKLLIARGV TKMARTEIFR AVRGLAVTQL VRVCPDAPPM NGVLRGQIYV QNLPCSVVAH
ALDPQEGDVI LDMCAAPGGK TSHVATLMRN KGTLVACDRS KRKALELRTL CDELQLECVV
PLKMDSTHAL LPKDQVDAGL AIAQSDRDFT SVAQVLARAK GNTPSQARLL QVEGFFPETF
DRILLDPPCS ALGLRPRLLH AGDTDNLAEY TNMQRNFLWV AAFLLKPGGT LVYSTCTINP
KENEQMVHHA LQNYPLKLVV QGEAHLGDRG LPGQGLNEHE ASLVQRFDPA NTELDTMGFF
CAKFIKTGPI RQEAKASPVL
//
