ID   FLPA_META3              Reviewed;         231 AA.
AC   A6UV22;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Maeo_0761;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000743; ABR56344.1; -; Genomic_DNA.
DR   RefSeq; WP_011973476.1; NC_009635.1.
DR   AlphaFoldDB; A6UV22; -.
DR   SMR; A6UV22; -.
DR   STRING; 419665.Maeo_0761; -.
DR   EnsemblBacteria; ABR56344; ABR56344; Maeo_0761.
DR   GeneID; 5326418; -.
DR   KEGG; mae:Maeo_0761; -.
DR   eggNOG; arCOG00078; Archaea.
DR   HOGENOM; CLU_059055_2_0_2; -.
DR   OMA; INMATHR; -.
DR   OrthoDB; 58340at2157; -.
DR   Proteomes; UP000001106; 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   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..231
FT                   /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT                   /id="PRO_1000006937"
FT   BINDING         88..89
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         106..107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         131..132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         151..154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
SQ   SEQUENCE   231 AA;  26166 MW;  FF7F98B7A16E8D35 CRC64;
     MEKVKLKEIF NNIYELKSDD GLKRIATKSL VPSKRIYGEK LITGEDNLEY RIWNPNRSKL
     GAAIVNGLKT MPIKKGSKVL YLGVSAGTTP SHVADITENS PVYSVEFAPR IMREFLDVSK
     DRKNLIPILG DATNPVEYSN VVEEVDVIFE DVAQPKQAEI LVNNAKWFLK EGGYGMISIK
     ARSVDVLRNP KEIFEEQKQI LIEGGFEIVD EVNIEPFEKD HILFVGIWNK Q