FLPA_PYRAB
ID FLPA_PYRAB Reviewed; 227 AA.
AC Q9V2L5; G8ZFP1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=PYRAB00600;
GN ORFNames=PAB2306;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248283; CAB48983.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69432.1; -; Genomic_DNA.
DR PIR; H75191; H75191.
DR RefSeq; WP_010867184.1; NC_000868.1.
DR AlphaFoldDB; Q9V2L5; -.
DR SMR; Q9V2L5; -.
DR STRING; 272844.PAB2306; -.
DR EnsemblBacteria; CAB48983; CAB48983; PAB2306.
DR GeneID; 1494943; -.
DR KEGG; pab:PAB2306; -.
DR PATRIC; fig|272844.11.peg.67; -.
DR eggNOG; arCOG00078; Archaea.
DR HOGENOM; CLU_059055_2_0_2; -.
DR OMA; INMATHR; -.
DR OrthoDB; 58340at2157; -.
DR PhylomeDB; Q9V2L5; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; RNA-binding; rRNA processing; Transferase;
KW tRNA processing.
FT CHAIN 1..227
FT /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT /id="PRO_0000148543"
FT BINDING 86..87
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 227 AA; 25737 MW; 8442FB50E3241AA3 CRC64;
MVEVKKHKFP GVYIVIDDDG SEKIATKNLV PGQRVYGERV IKWEGEEYRI WNPHRSKLGA
AIMNGLKNFP IKPGKSVLYL GIASGTTASH VSDVIGWEGK IFGIEFSPRV LRELVPIVED
RKNIVPILGD ATKPEEYRAL VPKVDVIFED VAQPTQAKIL IDNAEVYLKK GGYGMIAVKS
RSIDVTKEPE QVFREVEKEL SEYFEVIERL NLEPYEKDHA LFVVRKT
