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Database: UniProt
Entry: W6LG04_9TRYP
LinkDB: W6LG04_9TRYP
Original site: W6LG04_9TRYP 
ID   W6LG04_9TRYP            Unreviewed;       865 AA.
AC   W6LG04;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=GSHART1_T00006909001 {ECO:0000313|EMBL:CCW69611.1};
OS   Phytomonas sp. Hart1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW69611.1, ECO:0000313|Proteomes:UP000053358};
RN   [1] {ECO:0000313|EMBL:CCW69611.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW69611.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW69611.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW69611.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
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; HF955204; CCW69611.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6LG04; -.
DR   EnsemblProtists; CCW69611; CCW69611; GSHART1_T00006909001.
DR   OrthoDB; 126975at2759; -.
DR   Proteomes; UP000053358; 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   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; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22808:SF10; PUTATIVE-RELATED; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:UP000053358};
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          208..552
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        465
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         313..319
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         345
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         373
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         412
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   865 AA;  97027 MW;  87154099098BB65A CRC64;
     MKRREVRRKR ERENLSPALH ALIDLVPCNT DPRKYLTQHF CASCDPNGAI VEDGTTFLEG
     DGLGRLLLAL KEGCPRGVRD LLHLTRRVPH SRSTIDKVSV AELCFVLSHA SRPLTIRERR
     CGAGGEADSW NDDTPLLQYF KGKRFDAIIR GGNASMPLIR ENFTPVVIQD IEPEPSFTID
     RSSVGFPLNR TVEDSKAFLN PTLEWEKYLA SIRISLPMSL RVHQSERVLR WIALNFLMHS
     DSEVKSIVSL TKVLPESTAM FSSSNHDYHT HPHTEYVCRT LHAAGAVSFQ EVVSAIPVLV
     LGLQPHHSVL ELCAAPGSKT LQMLDETLKR GWTVDIEKSV VIANEKDRVK ATQILPARLK
     RYHAPNVLCT RCDATQWPKL YYYETNSSET KLGGNSKAPF LFEKQFDRII CDVPCSGDGT
     LRKERSVAAT WSLDYIQTLV PTQKALLRRG LDLLKTNGVL VYSTCSINPM EDEEVVCSAL
     DLFRDTVELL DVNVILQKQG VQLRSQGGLH SVDLESLIES QVPSSYNGAK VLRVLPHRDD
     TGGFFVAAFR KVRQQDQTEI KIAPQKLNQW TRGKLWAPIS KNDPVWGNIA EFYSFDRDFF
     RYYNNDNSDN NSMITTTTDG TTVESATERK GRLVPVYHLN PHGMQSRRIV FITPALANIV
     FNTKPFKGPG VELVSVGARG FEAYDNNFLP KAECRWRAVV ESASYLAPLF SSRKLLFTVG
     THHGLLEALF RNGFVYLRDY WWTLLGDESV NASNISKGRL FPFVKAGPLE ELLGIAKSCP
     TDELDSISCR IRDMLGTEVR VGGVLLGIYY SQEPLQEPWF LSATLSGSKL ELAVDTSLRG
     FGLMAFLNKF DSLDSHKDIG RVSDG
//
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