FLPA_METM7
ID FLPA_METM7 Reviewed; 232 AA.
AC A6VJQ1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=MmarC7_1619;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
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}.
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; CP000745; ABR66677.1; -; Genomic_DNA.
DR RefSeq; WP_012068137.1; NC_009637.1.
DR AlphaFoldDB; A6VJQ1; -.
DR SMR; A6VJQ1; -.
DR STRING; 426368.MmarC7_1619; -.
DR EnsemblBacteria; ABR66677; ABR66677; MmarC7_1619.
DR GeneID; 5327961; -.
DR KEGG; mmz:MmarC7_1619; -.
DR eggNOG; arCOG00078; Archaea.
DR HOGENOM; CLU_059055_2_0_2; -.
DR OMA; INMATHR; -.
DR OrthoDB; 58340at2157; -.
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; RNA-binding; rRNA processing; Transferase;
KW tRNA processing.
FT CHAIN 1..232
FT /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT /id="PRO_1000006940"
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"
SQ SEQUENCE 232 AA; 26333 MW; 3B3B9BE177982F74 CRC64;
MEKIKVKEIF NNVYSVDFGD GLKRIATKSL VPGKRVYGEK LVYSDSIEYR VWNPNKSKLG
AAIINGLKKM PIKKGTKVLY LGASAGTTPS HVADIAENSL VYALEFAPRI MREFIDSCNE
RKNLIPVLGD ANRPQDYSNI VEKVDVIFED VAQPNQAEIL VKNARWFLKE NGYAMISIKA
RSVDVTKNPR EIFAEQKKIL IEGGFEIVDE INIEPFEKDH MMMVGIWNET KY