ID   FLPA_METMZ              Reviewed;         193 AA.
AC   P0CW08; O53133;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 27.
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};
DE   Flags: Fragment;
GN   Name=flpA {ECO:0000255|HAMAP-Rule:MF_00351}; Synonyms=fibM;
OS   Methanosarcina mazei (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S-6;
RX   PubMed=10925204; DOI=10.1016/s0378-1119(00)00235-3;
RA   Hickey A.J., Macario A.J.L., Conway de Macario E.;
RT   "Identification of genes in the genome of the archaeon Methanosarcina
RT   mazeii that code for homologs of nuclear eukaryotic molecules involved in
RT   RNA processing.";
RL   Gene 253:77-85(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   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC       family. {ECO:0000255|HAMAP-Rule:MF_00351}.
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DR   EMBL; Y16231; CAA76128.1; -; Genomic_DNA.
DR   PIR; T47220; T47220.
DR   AlphaFoldDB; P0CW08; -.
DR   SMR; P0CW08; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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; RNA-binding; rRNA processing; Transferase;
KW   tRNA processing.
FT   CHAIN           1..>193
FT                   /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT                   /id="PRO_0000148535"
FT   BINDING         82..83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         100..101
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         125..126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   BINDING         145..148
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT   NON_TER         193
SQ   SEQUENCE   193 AA;  21483 MW;  CD07699509553551 CRC64;
     MPEIRQLSEG IFEVTKDKKQ LSTLNLDPGK VVYGEKLISV EGDEYRTWDP RRSKLGAMVL
     KKFDIPLKRN SKVLYLGAAS GTTVSHVSDI VSEGAVYSVE FAPRSMRDFI GLASRRKNIF
     PILADAGKPD SYAHIVEPVD VIFQDVAQPN QAEIAARNAV RFLKKDGYLL LSIKARSIDT
     AASPKEIFKE EVK