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Database: UniProt
Entry: M0C4T5_9EURY
LinkDB: M0C4T5_9EURY
Original site: M0C4T5_9EURY 
ID   M0C4T5_9EURY            Unreviewed;       302 AA.
AC   M0C4T5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=RNA methylase {ECO:0000313|EMBL:ELZ17332.1};
GN   ORFNames=C477_13915 {ECO:0000313|EMBL:ELZ17332.1};
OS   Haloterrigena salina JCM 13891.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=1227488 {ECO:0000313|EMBL:ELZ17332.1, ECO:0000313|Proteomes:UP000011657};
RN   [1] {ECO:0000313|EMBL:ELZ17332.1, ECO:0000313|Proteomes:UP000011657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13891 {ECO:0000313|EMBL:ELZ17332.1,
RC   ECO:0000313|Proteomes:UP000011657};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ17332.1}.
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DR   EMBL; AOIS01000045; ELZ17332.1; -; Genomic_DNA.
DR   RefSeq; WP_008895067.1; NZ_AOIS01000045.1.
DR   AlphaFoldDB; M0C4T5; -.
DR   STRING; 1227488.C477_13915; -.
DR   PATRIC; fig|1227488.3.peg.2775; -.
DR   eggNOG; arCOG00973; Archaea.
DR   OrthoDB; 14725at2157; -.
DR   Proteomes; UP000011657; 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 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; IPR011023; Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00446; nop2p; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF76; TRNA_RRNA CYTOSINE-C5-METHYLASE, NOL1_NOP2_SUN FAMILY; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000011657};
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          17..301
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   COILED          28..55
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        230
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         106..112
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         177
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   302 AA;  33124 MW;  D275CDCFB7BE7B48 CRC64;
     MEPLERYRPI VDDFDAFLEA CERPLGNAAR VNTIKASVER TLEALEEEGL AYEQADWNPR
     VLDLETGSPG STWTSFHGFT HGQEEVSAVP PVVLDPQPGE RVWDSCAAPG GKATQLAALM
     DDEGTVVAND NNLGRISALR FNAERLGATS LAVTNADARN YSLNRFDFDE FDRALVDAPC
     TCEGTIRKNP DALDNWSEGA IASVAGVQKG ILRRAIQATR EGGTVVYSTC TFAPEENEAV
     VQHALEEEDC RVVDFDLDLE YSPGLTEWDG EEFDSSLERT ARIYPHQNDT GGFFVTKLEV
     TA
//
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