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Database: UniProt
Entry: W7AWR2_PLAVN
LinkDB: W7AWR2_PLAVN
Original site: W7AWR2_PLAVN 
ID   W7AWR2_PLAVN            Unreviewed;       469 AA.
AC   W7AWR2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=rRNA (Cytosine-C(5))-methyltransferase, putative {ECO:0000313|EMBL:CAD2112235.1};
GN   ORFNames=PVPCR_1305460 {ECO:0000313|EMBL:CAD2112235.1}, YYG_04928
GN   {ECO:0000313|EMBL:EUD69866.1};
OS   Plasmodium vinckei petteri.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=138298 {ECO:0000313|EMBL:EUD69866.1, ECO:0000313|Proteomes:UP000030659};
RN   [1] {ECO:0000313|EMBL:EUD69866.1, ECO:0000313|Proteomes:UP000030659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR {ECO:0000313|EMBL:EUD69866.1,
RC   ECO:0000313|Proteomes:UP000030659};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium vinckei petteri CR.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAD2112235.1, ECO:0000313|Proteomes:UP000515268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ramaprasad A.;
RL   Submitted (AUG-2020) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; LR865418; CAD2112235.1; -; Genomic_DNA.
DR   EMBL; KI965409; EUD69866.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7AWR2; -.
DR   EnsemblProtists; EUD69866; EUD69866; YYG_04928.
DR   VEuPathDB; PlasmoDB:PVPCR_1305460; -.
DR   eggNOG; KOG2360; Eukaryota.
DR   OrthoDB; 240101at2759; -.
DR   Proteomes; UP000030659; Unassembled WGS sequence.
DR   Proteomes; UP000515268; Chromosome PVPCR_13.
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; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 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};
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          99..469
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        404
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         221
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         261
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         309
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   469 AA;  54861 MW;  67CBD2F87DDEEA9F CRC64;
     MSFIYRKAAQ MLMKCSKGDG IKDVLFKKED QSIKKIYFIV HKSMEDLDIF NKIYNTHLSK
     ICKNKYLGIV LLCVLIHRKK IDGGGELKRE ILKKEKEIFK LYNNLKNNND VKINILTKYF
     IIYLNDNPNI VNEIKTLLPI ENDEDVENLY KICTSKVKNL IDSIYYKNNK IRILDKSSGL
     VVKSANIQKG MTIVDVCSSP GSKAILSLLN LENKGYLICI EKSKTRCYTL IREILKNDEY
     IGYYTNENMN ETDKINIDKK DLFINNENNI YYIKHKNNEL IIKIYNCDFL KLTHKDFQEI
     GDIDVVFVDP SCSSSGMPDF VHKENMRKVF LQTKQIENDK NKKNEEDEKY NSYNIYSDIS
     EERIPKVPNT LIDKIKNLSN FQKDILNHAL ITIKTAKTFI YSTCSFFEEE NEQVIKNVLE
     KNLEFSIENA GTDKFLFKNG KYAFSDKCVR TFPNRDNCRG IFICKMCRK
//
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