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Database: UniProt
Entry: A0A662XC77_9STRA
LinkDB: A0A662XC77_9STRA
Original site: A0A662XC77_9STRA 
ID   A0A662XC77_9STRA        Unreviewed;       533 AA.
AC   A0A662XC77;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=BBJ28_00018394 {ECO:0000313|EMBL:RLN74103.1};
OS   Nothophytophthora sp. Chile5.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Nothophytophthora.
OX   NCBI_TaxID=2483409 {ECO:0000313|EMBL:RLN74103.1, ECO:0000313|Proteomes:UP000274840};
RN   [1] {ECO:0000313|EMBL:RLN74103.1, ECO:0000313|Proteomes:UP000274840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chile5 {ECO:0000313|EMBL:RLN74103.1};
RA   Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA   Williams N.M., Mcdougal R.L.;
RT   "Genome sequencing of oomycete isolates from Chile give support for New
RT   Zealand origin for Phytophthora kernoviae and make available the first
RT   Nothophytophthora sp. genome.";
RL   Submitted (JUL-2018) 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:RLN74103.1}.
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DR   EMBL; MBAC02006450; RLN74103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A662XC77; -.
DR   Proteomes; UP000274840; 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; 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:UP000274840};
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          188..519
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        448
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         290..296
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         314
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         341
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         398
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   533 AA;  57912 MW;  D46D81B822ADF47B CRC64;
     MSCVTFQCGV LDERKVRSVP DSNVEHHVVH DPLAGAPFLI AMAPLEDAAI SLDAFAVSFP
     AEVEQELGAA YGEPHWTRIK RALATPPAFT AVRVNTLRLS RDDALLALQP HLEGFNARLA
     QLDAARTPIR AFAHAALPDV LMIPSAPPGN SIVRFDPKRK SVIVDRLCGE AVLRGSDVFA
     RGVMSASSGL NAEDEVNVFV DLDHAHTRGS DFSAHTGRKL LIARGVTKMA RTELFRAVRG
     LAITQLVRVC ADAPPMNGVL RGQVYVQNLP CSVVAHALDP QEGDVILDMC AAPGGKTSHV
     ATLMRNRGTL VACDRSKRKA LELRTLCEEL ELDCIVPLKM DSTHSVLPKD QVESAPSDCD
     FVSVAQVLAR ARERTPTQAR LLQVDGFFPE TFDRVLLDPP CSALGLRPRL LHAGDAANLA
     EYTNMQRNFL WAAAFLLKPG GTLVYSTCTI NPKENEQMVH HALQNYPLEL VSQGAAHLGD
     RGLSGQGLSE QEAALVQRFD PANAELDTMG FFCAKFVKTR SMRQEESVMP SSP
//
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