ID FLPA_METJA Reviewed; 230 AA. AC Q58108; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 135. 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=MJ0697; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM OS 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MASS SPECTROMETRY. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10089444; DOI=10.1107/s0907444998007513; RA Wang H., Yokota H., Kim R., Kim S.-H.; RT "Expression, purification and preliminary X-ray analysis of a fibrillarin RT homolog from Methanococcus jannaschii, a hyperthermophile."; RL Acta Crystallogr. D 55:338-340(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10654930; DOI=10.1093/emboj/19.3.317; RA Wang H., Boisvert D., Kim K.K., Kim R., Kim S.-H.; RT "Crystal structure of a fibrillarin homologue from Methanococcus RT jannaschii, a hyperthermophile, at 1.6-A resolution."; RL EMBO J. 19:317-323(2000). 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 -!- 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. {ECO:0000255|HAMAP-Rule:MF_00351}. CC -!- MASS SPECTROMETRY: Mass=25971; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:10089444}; 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; L77117; AAB98690.1; -; Genomic_DNA. DR PIR; A64387; A64387. DR RefSeq; WP_010870202.1; NC_000909.1. DR PDB; 1FBN; X-ray; 1.60 A; A=1-230. DR PDB; 1G8S; X-ray; 1.60 A; A=1-230. DR PDBsum; 1FBN; -. DR PDBsum; 1G8S; -. DR AlphaFoldDB; Q58108; -. DR SMR; Q58108; -. DR IntAct; Q58108; 2. DR STRING; 243232.MJ_0697; -. DR PaxDb; 243232-MJ_0697; -. DR EnsemblBacteria; AAB98690; AAB98690; MJ_0697. DR GeneID; 1451564; -. DR KEGG; mja:MJ_0697; -. DR eggNOG; arCOG00078; Archaea. DR HOGENOM; CLU_059055_2_0_2; -. DR InParanoid; Q58108; -. DR OrthoDB; 6244at2157; -. DR PhylomeDB; Q58108; -. DR EvolutionaryTrace; Q58108; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central. DR GO; GO:1990259; F:histone H2AQ104 methyltransferase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central. DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IBA:GO_Central. DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central. 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..230 FT /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase" FT /id="PRO_0000148533" FT BINDING 87..88 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 /evidence="ECO:0000255|HAMAP-Rule:MF_00351" FT BINDING 130..131 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00351" FT BINDING 150..153 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00351" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:1FBN" FT TURN 10..12 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 13..17 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 25..28 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 41..44 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 47..51 FT /evidence="ECO:0007829|PDB:1FBN" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:1FBN" FT HELIX 58..64 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:1FBN" FT HELIX 87..95 FT /evidence="ECO:0007829|PDB:1FBN" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 99..106 FT /evidence="ECO:0007829|PDB:1FBN" FT HELIX 108..117 FT /evidence="ECO:0007829|PDB:1FBN" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 124..128 FT /evidence="ECO:0007829|PDB:1FBN" FT HELIX 134..137 FT /evidence="ECO:0007829|PDB:1FBN" FT TURN 138..140 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 144..149 FT /evidence="ECO:0007829|PDB:1FBN" FT HELIX 156..167 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 168..179 FT /evidence="ECO:0007829|PDB:1FBN" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:1FBN" FT HELIX 189..203 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 205..212 FT /evidence="ECO:0007829|PDB:1FBN" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:1FBN" FT STRAND 220..227 FT /evidence="ECO:0007829|PDB:1FBN" SQ SEQUENCE 230 AA; 25966 MW; 9ECAAD7C4C606756 CRC64; MEDIKIKEIF ENIYEVDLGD GLKRIATKSI VKGKKVYDEK IIKIGDEEYR IWNPNKSKLA AAIIKGLKVM PIKRDSKILY LGASAGTTPS HVADIADKGI VYAIEYAPRI MRELLDACAE RENIIPILGD ANKPQEYANI VEKVDVIYED VAQPNQAEIL IKNAKWFLKK GGYGMIAIKA RSIDVTKDPK EIFKEQKEIL EAGGFKIVDE VDIEPFEKDH VMFVGIWEGK //