FLPA_ARCFU
ID FLPA_ARCFU Reviewed; 210 AA.
AC O28192;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=AF_2087;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH NOP5 AND
RP S-ADENOSYL-L-METHIONINE.
RX PubMed=12598892; DOI=10.1038/nsb905;
RA Aittaleb M., Rashid R., Chen Q., Palmer J.R., Daniels C.J., Li H.;
RT "Structure and function of archaeal box C/D sRNP core proteins.";
RL Nat. Struct. Biol. 10:256-263(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH NOP5 AND
RP S-ADENOSYL-L-METHIONINE, FUNCTION, AND MUTAGENESIS OF THR-70; GLU-88;
RP TYR-89 AND ASP-133.
RX PubMed=15286083; DOI=10.1074/jbc.m406209200;
RA Aittaleb M., Visone T., Fenley M.O., Li H.;
RT "Structural and thermodynamic evidence for a stabilizing role of Nop5p in
RT S-adenosyl-L-methionine binding to fibrillarin.";
RL J. Biol. Chem. 279:41822-41829(2004).
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:15286083}.
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 ECO:0000269|PubMed:12598892, ECO:0000269|PubMed:15286083}.
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; AE000782; AAB89169.1; -; Genomic_DNA.
DR PIR; F69510; F69510.
DR RefSeq; WP_010879579.1; NC_000917.1.
DR PDB; 1NT2; X-ray; 2.90 A; A=1-210.
DR PDBsum; 1NT2; -.
DR AlphaFoldDB; O28192; -.
DR SMR; O28192; -.
DR IntAct; O28192; 1.
DR STRING; 224325.AF_2087; -.
DR EnsemblBacteria; AAB89169; AAB89169; AF_2087.
DR GeneID; 1485314; -.
DR KEGG; afu:AF_2087; -.
DR eggNOG; arCOG00078; Archaea.
DR HOGENOM; CLU_059055_2_0_2; -.
DR OMA; LREWDPR; -.
DR OrthoDB; 58340at2157; -.
DR PhylomeDB; O28192; -.
DR EvolutionaryTrace; O28192; -.
DR Proteomes; UP000002199; 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..210
FT /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT /id="PRO_0000148529"
FT BINDING 70..71
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 88..89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 113..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 133..136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00351"
FT MUTAGEN 70
FT /note="T->A: Loss of RNA methyltransferase activity. No
FT effect on affinity for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:15286083"
FT MUTAGEN 88
FT /note="E->A: Loss of RNA methyltransferase activity. No
FT effect on affinity for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:15286083"
FT MUTAGEN 89
FT /note="Y->A: Strongly reduced RNA methyltransferase
FT activity. Reduced affinity for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:15286083"
FT MUTAGEN 133
FT /note="D->A: Loss of RNA methyltransferase activity.
FT Strongly decreased affinity for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:15286083"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1NT2"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1NT2"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:1NT2"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:1NT2"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1NT2"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1NT2"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1NT2"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1NT2"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 151..162
FT /evidence="ECO:0007829|PDB:1NT2"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:1NT2"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:1NT2"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1NT2"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:1NT2"
SQ SEQUENCE 210 AA; 24327 MW; 56946F477586EDA5 CRC64;
MKELMRNVYL LDDTLVTKSK YGSHYGEKVF DGYREWVPWR SKLAAMILKG HRLKLRGDER
VLYLGAASGT TVSHLADIVD EGIIYAVEYS AKPFEKLLEL VRERNNIIPL LFDASKPWKY
SGIVEKVDLI YQDIAQKNQI EILKANAEFF LKEKGEVVIM VKARSIDSTA EPEEVFKSVL
KEMEGDFKIV KHGSLMPYHR DHIFIHAYRF
