ID FLPA_PYRFU Reviewed; 227 AA. AC Q8U4M2; DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00351}; DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00351}; GN Name=flpA {ECO:0000255|HAMAP-Rule:MF_00351}; OrderedLocusNames=PF0059; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. RT horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS), AND SUBUNIT. RX PubMed=14975761; DOI=10.1016/j.bbrc.2004.01.114; RA Deng L., Starostina N.G., Liu Z.J., Rose J.P., Terns R.M., Terns M.P., RA Wang B.C.; RT "Structure determination of fibrillarin from the hyperthermophilic archaeon RT Pyrococcus furiosus."; RL Biochem. Biophys. Res. Commun. 315:726-732(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH NOP5, AND SUBUNIT. RX PubMed=17617422; DOI=10.1016/j.jmb.2007.06.029; RA Oruganti S., Zhang Y., Li H., Robinson H., Terns M.P., Terns R.M., Yang W., RA Li H.; RT "Alternative conformations of the archaeal Nop56/58-fibrillarin complex RT imply flexibility in box C/D RNPs."; RL J. Mol. Biol. 371:1141-1150(2007). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE; RPL7AE; NOP5 AND RNA SUBSTRATE, SUBUNIT, AND RP FUNCTION. RX PubMed=20864039; DOI=10.1016/j.molcel.2010.08.022; RA Xue S., Wang R., Yang F., Terns R.M., Terns M.P., Zhang X., Maxwell E.S., RA Li H.; RT "Structural basis for substrate placement by an archaeal box C/D RT ribonucleoprotein particle."; RL Mol. Cell 39:939-949(2010). RN [5] RP STRUCTURE BY NMR IN COMPLEX WITH RPL7AE; NOP5 AND RNA SUBSTRATE, FUNCTION, RP AND SUBUNIT. RX PubMed=24121435; DOI=10.1038/nature12581; RA Lapinaite A., Simon B., Skjaerven L., Rakwalska-Bange M., Gabel F., RA Carlomagno T.; RT "The structure of the box C/D enzyme reveals regulation of RNA RT methylation."; RL Nature 502:519-523(2013). CC -!- FUNCTION: Involved in pre-rRNA and tRNA processing. Utilizes the methyl CC donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl CC methylation of ribose moieties in rRNA and tRNA. Site specificity is CC provided by a guide RNA that base pairs with the substrate. Methylation CC occurs at a characteristic distance from the sequence involved in base CC pairing with the guide RNA. {ECO:0000255|HAMAP-Rule:MF_00351, CC ECO:0000269|PubMed:20864039, ECO:0000269|PubMed:24121435}. CC -!- SUBUNIT: Interacts with nop5. Component of box C/D small CC ribonucleoprotein (sRNP) particles that contain rpl7ae, FlpA and nop5, CC plus a guide RNA. These sRNP particles form homodimers, giving rise to CC an asymmetric holoenzyme. {ECO:0000255|HAMAP-Rule:MF_00351, CC ECO:0000269|PubMed:14975761, ECO:0000269|PubMed:17617422, CC ECO:0000269|PubMed:20864039, ECO:0000269|PubMed:24121435}. CC -!- INTERACTION: CC Q8U4M2; Q8U4M1: PF0060; NbExp=7; IntAct=EBI-16078587, EBI-16078570; CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin CC family. {ECO:0000255|HAMAP-Rule:MF_00351}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE009950; AAL80183.1; -; Genomic_DNA. DR RefSeq; WP_011011171.1; NZ_CP023154.1. DR PDB; 1PRY; X-ray; 1.97 A; A=1-227. DR PDB; 2NNW; X-ray; 2.70 A; B/D=1-227. DR PDB; 3NMU; X-ray; 2.73 A; F/J=1-227. DR PDB; 3NVK; X-ray; 3.21 A; I/J=1-227. DR PDB; 3NVM; X-ray; 3.41 A; B=1-227. DR PDB; 4BY9; NMR; -; E/H/K/N=1-227. DR PDBsum; 1PRY; -. DR PDBsum; 2NNW; -. DR PDBsum; 3NMU; -. DR PDBsum; 3NVK; -. DR PDBsum; 3NVM; -. DR PDBsum; 4BY9; -. DR AlphaFoldDB; Q8U4M2; -. DR BMRB; Q8U4M2; -. DR SASBDB; Q8U4M2; -. DR SMR; Q8U4M2; -. DR DIP; DIP-60606N; -. DR IntAct; Q8U4M2; 2. DR STRING; 186497.PF0059; -. DR PaxDb; 186497-PF0059; -. DR GeneID; 41711846; -. DR KEGG; pfu:PF0059; -. DR PATRIC; fig|186497.12.peg.63; -. DR eggNOG; arCOG00078; Archaea. DR HOGENOM; CLU_059055_2_0_2; -. DR OrthoDB; 6244at2157; -. DR PhylomeDB; Q8U4M2; -. DR EvolutionaryTrace; Q8U4M2; -. DR Proteomes; UP000001013; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_00351; RNA_methyltransf_FlpA; 1. DR InterPro; IPR000692; Fibrillarin. DR InterPro; IPR020813; Fibrillarin_CS. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR10335:SF17; FIBRILLARIN; 1. DR PANTHER; PTHR10335; RRNA 2-O-METHYLTRANSFERASE FIBRILLARIN; 1. DR Pfam; PF01269; Fibrillarin; 1. DR PIRSF; PIRSF006540; Nop17p; 1. DR PRINTS; PR00052; FIBRILLARIN. DR SMART; SM01206; Fibrillarin; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS00566; FIBRILLARIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Methyltransferase; Reference proteome; RNA-binding; KW rRNA processing; Transferase; tRNA processing. FT CHAIN 1..227 FT /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase" FT /id="PRO_0000148545" FT BINDING 86..87 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00351" FT BINDING 105..106 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 130..131 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 150..153 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 12..16 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:3NVK" FT STRAND 22..27 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:3NMU" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:2NNW" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 46..50 FT /evidence="ECO:0007829|PDB:1PRY" FT TURN 53..55 FT /evidence="ECO:0007829|PDB:1PRY" FT HELIX 57..63 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 76..81 FT /evidence="ECO:0007829|PDB:1PRY" FT HELIX 87..95 FT /evidence="ECO:0007829|PDB:1PRY" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:2NNW" FT STRAND 99..106 FT /evidence="ECO:0007829|PDB:1PRY" FT HELIX 108..118 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 124..128 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:3NVM" FT HELIX 134..140 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 144..149 FT /evidence="ECO:0007829|PDB:1PRY" FT HELIX 156..167 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 168..179 FT /evidence="ECO:0007829|PDB:1PRY" FT HELIX 180..183 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:1PRY" FT HELIX 189..201 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 204..211 FT /evidence="ECO:0007829|PDB:1PRY" FT TURN 213..215 FT /evidence="ECO:0007829|PDB:1PRY" FT STRAND 216..225 FT /evidence="ECO:0007829|PDB:1PRY" SQ SEQUENCE 227 AA; 25762 MW; A2190B2983FD6EF3 CRC64; MVEVKKHKFP GVYVVIDDDG SEKIATKNLV PGQRVYGERV IKWEGEEYRI WNPHRSKLGA AIVNGLKNFP IKPGKSVLYL GIASGTTASH VSDIVGWEGK IYGIEFSPRV LRELVPIVEE RRNIIPILGD ATKPEEYRAL VTKVDVIFED VAQPTQAKIL IDNAKAYLKR GGYGMIAVKS RSIDVTKEPE QVFKEVEREL SEYFEVIERL NLEPYEKDHA LFVVRKP //