ID   FLPA_HALWD              Reviewed;         215 AA.
AC   Q18H64;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=HQ_2567A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC       family. {ECO:0000255|HAMAP-Rule:MF_00351}.
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DR   EMBL; AM180088; CAJ52679.1; -; Genomic_DNA.
DR   RefSeq; WP_011571797.1; NC_008212.1.
DR   AlphaFoldDB; Q18H64; -.
DR   SMR; Q18H64; -.
DR   STRING; 362976.HQ_2567A; -.
DR   EnsemblBacteria; CAJ52679; CAJ52679; HQ_2567A.
DR   GeneID; 4193988; -.
DR   KEGG; hwa:HQ_2567A; -.
DR   eggNOG; arCOG00078; Archaea.
DR   HOGENOM; CLU_059055_2_0_2; -.
DR   OMA; INMATHR; -.
DR   Proteomes; UP000001975; 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   Gene3D; 3.40.50.150; -; 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   Pfam; PF01269; Fibrillarin; 1.
DR   PRINTS; PR00052; FIBRILLARIN.
DR   SMART; SM01206; Fibrillarin; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00566; FIBRILLARIN; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; RNA-binding; rRNA processing;
KW   Transferase; tRNA processing.
FT   CHAIN           1..215
FT                   /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT                   /id="PRO_0000389602"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         76..77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         92..93
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         117..118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         138..141
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
SQ   SEQUENCE   215 AA;  23900 MW;  41229F12A71589BE CRC64;
     MKASSSLPDG VQRRQFDNRS RLTTHGTTVY GEPRDTDGWR LWDAGRSKLG AMFKLDIETG
     LTGGESILYL GAASGTTVSH VADFAGPTYA IEFAPRPVRD LLEVATTRPN LIPLLCDARQ
     PETYAHVVET DIEYLIQDVA TRGQATVALR NRQFLAPDGK LILMIKARSE DVLSDPEDVF
     DTIISTLREG YIIQTRQRLD RFHDDHLAVV ATPNM