ID   FLPA_PYRAE              Reviewed;         235 AA.
AC   Q8ZTI9;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=PAE3228;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64772.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZTI9; -.
DR   SMR; Q8ZTI9; -.
DR   STRING; 178306.PAE3228; -.
DR   EnsemblBacteria; AAL64772; AAL64772; PAE3228.
DR   KEGG; pai:PAE3228; -.
DR   PATRIC; fig|178306.9.peg.2431; -.
DR   eggNOG; arCOG00078; Archaea.
DR   HOGENOM; CLU_059055_2_0_2; -.
DR   InParanoid; Q8ZTI9; -.
DR   OMA; INMATHR; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
DR   GO; GO:1990259; F:histone-glutamine 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:1990258; P:histone glutamine methylation; IBA:GO_Central.
DR   GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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   PIRSF; PIRSF006540; Nop17p; 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..235
FT                   /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT                   /id="PRO_0000148544"
FT   BINDING         91..92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         110..111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         137..138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         157..160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
SQ   SEQUENCE   235 AA;  26503 MW;  9A8607C3552B497A CRC64;
     MSIEVVEVKP HERHYGVYVV KFEDGTERIA TKNLTPGRRV YGERLIKWGG DEYREWNPYR
     SKLAAAILNG LKLVPIKEGT HILYLGAASG TTPSHISDIV GENGLIYSVE FSPRVFREFM
     EKLVDQGRRN VVPILGDARF PYQYAHYVKG VDVVYIDVAQ PAQAKILADN ADYFLKPGGH
     VMLVIKAMSI DVTAPATETF KQEINTLKER GFDILETVHL EPYDTAHAMV IAKKR