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Database: UniProt
Entry: Q8SRL8_ENCCU
LinkDB: Q8SRL8_ENCCU
Original site: Q8SRL8_ENCCU 
ID   Q8SRL8_ENCCU            Unreviewed;       364 AA.
AC   Q8SRL8;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=NOP2-LIKE NUCLEOLAR PROTEIN {ECO:0000313|EMBL:CAD25564.1};
GN   OrderedLocusNames=ECU07_0320 {ECO:0000313|EMBL:CAD25564.1};
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD25564.1, ECO:0000313|Proteomes:UP000000819};
RN   [1] {ECO:0000313|EMBL:CAD25564.1, ECO:0000313|Proteomes:UP000000819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1 {ECO:0000313|EMBL:CAD25564.1,
RC   ECO:0000313|Proteomes:UP000000819};
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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; AL590447; CAD25564.1; -; Genomic_DNA.
DR   RefSeq; NP_585960.1; NM_001041582.1.
DR   AlphaFoldDB; Q8SRL8; -.
DR   STRING; 284813.Q8SRL8; -.
DR   GeneID; 859389; -.
DR   KEGG; ecu:ECU07_0320; -.
DR   VEuPathDB; MicrosporidiaDB:ECU07_0320; -.
DR   HOGENOM; CLU_005316_7_4_1; -.
DR   InParanoid; Q8SRL8; -.
DR   OMA; IRSKWHA; -.
DR   OrthoDB; 102852at2759; -.
DR   Proteomes; UP000000819; Chromosome VII.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:UniProt.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF4; 28S RRNA (CYTOSINE-C(5))-METHYLTRANSFERASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000819};
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          86..363
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        299
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         184..190
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         235
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   364 AA;  42142 MW;  4DC7705DE62D1582 CRC64;
     MNKKESSKLQ FDKRCIEMVR HVLEGRSTVK QEVYKMKDPK MYHKLVHMVV ENHDLLLDLI
     KRCKYMEDDR ELGVIRCFQI LDRRIRNTRM RRKFMKALGG RKLKLTKATV FVRINTLRGG
     TEEDIGFLDY EKSCVDGVYK ILDSKNIVFS EGYKNGKFVI QNISSCLPAH ILDPEEGSRV
     IDTCSAPGNK TSQLAMIMRN TGKIYAFERS KNRAETLRAQ LFKLGVSNTE VVEDDFMNAN
     PEDFEGIRYI LCDPSCSGSG MHLGYKMDKE RIEGLKSFQI EIVRHALRFR PEKLVYSVCS
     DHREEGEEVV EEILRSSEYE LENISMFWSS AHSSGFSFSQ DVVRCRRDES GAIGFFIALF
     VRKK
//
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