FLPA_PYRFU
ID FLPA_PYRFU Reviewed; 227 AA.
AC Q8U4M2;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, 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=PF0059;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS), AND SUBUNIT.
RX PubMed=14975761; DOI=10.1016/j.bbrc.2004.01.114;
RA Deng L., Starostina N.G., Liu Z.J., Rose J.P., Terns R.M., Terns M.P.,
RA Wang B.C.;
RT "Structure determination of fibrillarin from the hyperthermophilic archaeon
RT Pyrococcus furiosus.";
RL Biochem. Biophys. Res. Commun. 315:726-732(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH NOP5, AND SUBUNIT.
RX PubMed=17617422; DOI=10.1016/j.jmb.2007.06.029;
RA Oruganti S., Zhang Y., Li H., Robinson H., Terns M.P., Terns R.M., Yang W.,
RA Li H.;
RT "Alternative conformations of the archaeal Nop56/58-fibrillarin complex
RT imply flexibility in box C/D RNPs.";
RL J. Mol. Biol. 371:1141-1150(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE; RPL7AE; NOP5 AND RNA SUBSTRATE, SUBUNIT, AND
RP FUNCTION.
RX PubMed=20864039; DOI=10.1016/j.molcel.2010.08.022;
RA Xue S., Wang R., Yang F., Terns R.M., Terns M.P., Zhang X., Maxwell E.S.,
RA Li H.;
RT "Structural basis for substrate placement by an archaeal box C/D
RT ribonucleoprotein particle.";
RL Mol. Cell 39:939-949(2010).
RN [5]
RP STRUCTURE BY NMR IN COMPLEX WITH RPL7AE; NOP5 AND RNA SUBSTRATE, FUNCTION,
RP AND SUBUNIT.
RX PubMed=24121435; DOI=10.1038/nature12581;
RA Lapinaite A., Simon B., Skjaerven L., Rakwalska-Bange M., Gabel F.,
RA Carlomagno T.;
RT "The structure of the box C/D enzyme reveals regulation of RNA
RT methylation.";
RL Nature 502:519-523(2013).
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 ECO:0000269|PubMed:20864039, ECO:0000269|PubMed:24121435}.
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. These sRNP particles form homodimers, giving rise to
CC an asymmetric holoenzyme. {ECO:0000255|HAMAP-Rule:MF_00351,
CC ECO:0000269|PubMed:14975761, ECO:0000269|PubMed:17617422,
CC ECO:0000269|PubMed:20864039, ECO:0000269|PubMed:24121435}.
CC -!- INTERACTION:
CC Q8U4M2; Q8U4M1: PF0060; NbExp=7; IntAct=EBI-16078587, EBI-16078570;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000255|HAMAP-Rule:MF_00351}.
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DR EMBL; AE009950; AAL80183.1; -; Genomic_DNA.
DR RefSeq; WP_011011171.1; NZ_CP023154.1.
DR PDB; 1PRY; X-ray; 1.97 A; A=1-227.
DR PDB; 2NNW; X-ray; 2.70 A; B/D=1-227.
DR PDB; 3NMU; X-ray; 2.73 A; F/J=1-227.
DR PDB; 3NVK; X-ray; 3.21 A; I/J=1-227.
DR PDB; 3NVM; X-ray; 3.41 A; B=1-227.
DR PDB; 4BY9; NMR; -; E/H/K/N=1-227.
DR PDBsum; 1PRY; -.
DR PDBsum; 2NNW; -.
DR PDBsum; 3NMU; -.
DR PDBsum; 3NVK; -.
DR PDBsum; 3NVM; -.
DR PDBsum; 4BY9; -.
DR AlphaFoldDB; Q8U4M2; -.
DR BMRB; Q8U4M2; -.
DR SASBDB; Q8U4M2; -.
DR SMR; Q8U4M2; -.
DR DIP; DIP-60606N; -.
DR IntAct; Q8U4M2; 2.
DR STRING; 186497.PF0059; -.
DR EnsemblBacteria; AAL80183; AAL80183; PF0059.
DR GeneID; 41711846; -.
DR KEGG; pfu:PF0059; -.
DR PATRIC; fig|186497.12.peg.63; -.
DR eggNOG; arCOG00078; Archaea.
DR HOGENOM; CLU_059055_2_0_2; -.
DR OMA; INMATHR; -.
DR OrthoDB; 58340at2157; -.
DR PhylomeDB; Q8U4M2; -.
DR EvolutionaryTrace; Q8U4M2; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome; RNA-binding;
KW rRNA processing; Transferase; tRNA processing.
FT CHAIN 1..227
FT /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT /id="PRO_0000148545"
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 BINDING 130..131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 150..153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3NVK"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3NMU"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2NNW"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1PRY"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1PRY"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1PRY"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1PRY"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:2NNW"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1PRY"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3NVM"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1PRY"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 168..179
FT /evidence="ECO:0007829|PDB:1PRY"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1PRY"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:1PRY"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1PRY"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:1PRY"
SQ SEQUENCE 227 AA; 25762 MW; A2190B2983FD6EF3 CRC64;
MVEVKKHKFP GVYVVIDDDG SEKIATKNLV PGQRVYGERV IKWEGEEYRI WNPHRSKLGA
AIVNGLKNFP IKPGKSVLYL GIASGTTASH VSDIVGWEGK IYGIEFSPRV LRELVPIVEE
RRNIIPILGD ATKPEEYRAL VTKVDVIFED VAQPTQAKIL IDNAKAYLKR GGYGMIAVKS
RSIDVTKEPE QVFKEVEREL SEYFEVIERL NLEPYEKDHA LFVVRKP
