FLPA_SACS2
ID FLPA_SACS2 Reviewed; 232 AA.
AC P58032;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00351};
DE Short=FIB;
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00351};
GN Name=flpA {ECO:0000255|HAMAP-Rule:MF_00351}; OrderedLocusNames=SSO0940;
GN ORFNames=C33_014;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, MUTAGENESIS OF ALA-85 AND PRO-129, AND SUBUNIT.
RX PubMed=11959980; DOI=10.1073/pnas.082101999;
RA Omer A.D., Ziesche S., Ebhardt H., Dennis P.P.;
RT "In vitro reconstitution and activity of a C/D box methylation guide
RT ribonucleoprotein complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5289-5294(2002).
RN [3]
RP FUNCTION.
RX PubMed=15522081; DOI=10.1111/j.1365-2958.2004.04319.x;
RA Ziesche S.M., Omer A.D., Dennis P.P.;
RT "RNA-guided nucleotide modification of ribosomal and non-ribosomal RNAs in
RT Archaea.";
RL Mol. Microbiol. 54:980-993(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEXES WITH RNA;
RP S-ADENOSYL-L-METHIONINE; NOP5 AND RPL7AE, AND SUBUNIT.
RX PubMed=19666563; DOI=10.1073/pnas.0905128106;
RA Ye K., Jia R., Lin J., Ju M., Peng J., Xu A., Zhang L.;
RT "Structural organization of box C/D RNA-guided RNA methyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13808-13813(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH GUIDE RNA; SUBSTRATE
RP RNA AND RPL7AE, SUBUNIT, AND FUNCTION.
RX PubMed=21270896; DOI=10.1038/nature09688;
RA Lin J., Lai S., Jia R., Xu A., Zhang L., Lu J., Ye K.;
RT "Structural basis for site-specific ribose methylation by box C/D RNA
RT protein complexes.";
RL Nature 469:559-563(2011).
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:11959980, ECO:0000269|PubMed:15522081,
CC ECO:0000269|PubMed:21270896}.
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:11959980, ECO:0000269|PubMed:19666563,
CC ECO:0000269|PubMed:21270896}.
CC -!- INTERACTION:
CC P58032; Q97ZH3: SSO0939; NbExp=5; IntAct=EBI-2944159, EBI-2944135;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000255|HAMAP-Rule:MF_00351}.
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DR EMBL; AE006641; AAK41216.1; -; Genomic_DNA.
DR PIR; A99245; A99245.
DR RefSeq; WP_009992372.1; NC_002754.1.
DR PDB; 3ID5; X-ray; 4.01 A; B/F=1-232.
DR PDB; 3ID6; X-ray; 2.60 A; C=1-232.
DR PDB; 3PLA; X-ray; 3.15 A; E/F/M=1-232.
DR PDB; 5JPQ; EM; 7.30 A; W/X=1-232.
DR PDBsum; 3ID5; -.
DR PDBsum; 3ID6; -.
DR PDBsum; 3PLA; -.
DR PDBsum; 5JPQ; -.
DR AlphaFoldDB; P58032; -.
DR SMR; P58032; -.
DR DIP; DIP-48939N; -.
DR IntAct; P58032; 2.
DR STRING; 273057.SSO0940; -.
DR EnsemblBacteria; AAK41216; AAK41216; SSO0940.
DR GeneID; 44129869; -.
DR KEGG; sso:SSO0940; -.
DR PATRIC; fig|273057.12.peg.936; -.
DR eggNOG; arCOG00078; Archaea.
DR HOGENOM; CLU_059055_2_0_2; -.
DR InParanoid; P58032; -.
DR OMA; INMATHR; -.
DR PhylomeDB; P58032; -.
DR EvolutionaryTrace; P58032; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
DR GO; GO:1990259; F:histone-glutamine methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1990258; P:histone glutamine methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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..232
FT /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT /id="PRO_0000148549"
FT BINDING 89..90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 108..109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 133..134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 153..156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT MUTAGEN 85
FT /note="A->V: Loss of methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11959980"
FT MUTAGEN 129
FT /note="P->A: Decreased methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11959980"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3PLA"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3ID6"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3ID6"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:3ID6"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:3ID6"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:3ID6"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3ID6"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3ID6"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:3ID6"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:3ID6"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:3PLA"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3PLA"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:3ID6"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3ID6"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3ID6"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:3ID6"
SQ SEQUENCE 232 AA; 26422 MW; CFFB34D2D4FA9CF2 CRC64;
MSEVITVKQT NMENIYECEF NDGSFRLCTR NLVPNFNVYG ERLIKYEGVE YREWNAFRSK
LAGAILKGLK TNPIRKGTKV LYLGAASGTT ISHVSDIIEL NGKAYGVEFS PRVVRELLLV
AQRRPNIFPL LADARFPQSY KSVVENVDVL YVDIAQPDQT DIAIYNAKFF LKVNGDMLLV
IKARSIDVTK DPKEIYKTEV EKLENSNFET IQIINLDPYD KDHAIVLSKY KG
