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Database: UniProt
Entry: L0K4H6_9EURY
LinkDB: L0K4H6_9EURY
Original site: L0K4H6_9EURY 
ID   L0K4H6_9EURY            Unreviewed;       302 AA.
AC   L0K4H6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=NOL1/NOP2/sun family putative RNA methylase {ECO:0000313|EMBL:AGB39450.1};
GN   ORFNames=Natoc_3735 {ECO:0000313|EMBL:AGB39450.1};
OS   Natronococcus occultus SP4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB39450.1, ECO:0000313|Proteomes:UP000010878};
RN   [1] {ECO:0000313|EMBL:AGB39450.1, ECO:0000313|Proteomes:UP000010878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP4 {ECO:0000313|EMBL:AGB39450.1,
RC   ECO:0000313|Proteomes:UP000010878};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA   Klenk H.-P.;
RT   "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL   Submitted (NOV-2012) 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}.
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DR   EMBL; CP003929; AGB39450.1; -; Genomic_DNA.
DR   RefSeq; WP_015322884.1; NC_019974.1.
DR   AlphaFoldDB; L0K4H6; -.
DR   STRING; 694430.Natoc_3735; -.
DR   GeneID; 14402583; -.
DR   KEGG; nou:Natoc_3735; -.
DR   eggNOG; arCOG00973; Archaea.
DR   HOGENOM; CLU_005316_7_0_2; -.
DR   OrthoDB; 14725at2157; -.
DR   Proteomes; UP000010878; Chromosome.
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   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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000010878};
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   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;  33338 MW;  2E402F4562F2C1FB CRC64;
     MEPLERYRPI VDDFEAFLAA CERPLGNAVR VNTIKATVDR ARAVLEAEDV GYEGADWNPR
     VLRLETDSPG STWASFHGYT HGQEEVSAVP ATVLDPEPGE RVWDCCAAPG GKATQLAALM
     DDRGTVVAND SNLGRISALR FNAERLGATS LAVTNDDARN YSLERFDFEE FDRSLVDAPC
     SCEGTIRKNP DALDGWSEGY LDEVSGIQKG ILRRAVQATR EDGTVVYSTC TFAPEENEAV
     IQHVLEEEDC RVVDFDLGLE HSPGLTEWDG EEYDERLEKA ARIYPHQNDT GGFFVAKLEV
     TA
//
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