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Database: UniProt
Entry: O28240_ARCFU
LinkDB: O28240_ARCFU
Original site: O28240_ARCFU 
ID   O28240_ARCFU            Unreviewed;       324 AA.
AC   O28240;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=Proliferating-cell nucleolar antigen P120, putative {ECO:0000313|EMBL:AAB89215.1};
GN   OrderedLocusNames=AF_2039 {ECO:0000313|EMBL:AAB89215.1};
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325 {ECO:0000313|EMBL:AAB89215.1, ECO:0000313|Proteomes:UP000002199};
RN   [1] {ECO:0000313|EMBL:AAB89215.1, ECO:0000313|Proteomes:UP000002199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16
RC   {ECO:0000313|Proteomes:UP000002199};
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.P., Clayton R.A., Tomb J., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B., Peterson S.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L., Utterback T., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB89215.1; -; Genomic_DNA.
DR   PIR; F69504; F69504.
DR   RefSeq; WP_010879531.1; NC_000917.1.
DR   AlphaFoldDB; O28240; -.
DR   STRING; 224325.AF_2039; -.
DR   PaxDb; 224325-AF_2039; -.
DR   DNASU; 1485265; -.
DR   EnsemblBacteria; AAB89215; AAB89215; AF_2039.
DR   GeneID; 24795787; -.
DR   KEGG; afu:AF_2039; -.
DR   eggNOG; arCOG00973; Archaea.
DR   HOGENOM; CLU_005316_7_0_2; -.
DR   OrthoDB; 14725at2157; -.
DR   PhylomeDB; O28240; -.
DR   Proteomes; UP000002199; 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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
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: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   Pfam; PF17125; Methyltr_RsmF_N; 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:UP000002199};
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          40..316
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        251
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   324 AA;  36548 MW;  D7C2EE6B49973B4F CRC64;
     MKVLDFPSSK KAKELAVKYG YDEFIVRRWL HFFGDETEDI IRAFEEGIPK YIRINTLKID
     EKGLLERLES RGFKLKKTEV PYCFEVVEEP YSIGATPEYL MGYYYVMDKS SCIPPLALEP
     KPGEVVVDLA ASPGGKTTFL SMLMENKGAV IAVEPQKERL QPLIDNINRM GAMNVAVINV
     DGRRVPAMGI KADRVLLDAP CTGEGIIHKD PSRKTDRGKE DILFCSSLQR ELVLAAFDCL
     KEGGVMVYST CSLTPEENEF VVDFLLERRK GVVEEIEWGD EALALPGVKN EVSKARRFYP
     HRHQCSGFFV ARIRKVGDSK AKPE
//
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