FLPA_METJA
ID FLPA_METJA Reviewed; 230 AA.
AC Q58108;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=MJ0697;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MASS SPECTROMETRY.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=10089444; DOI=10.1107/s0907444998007513;
RA Wang H., Yokota H., Kim R., Kim S.-H.;
RT "Expression, purification and preliminary X-ray analysis of a fibrillarin
RT homolog from Methanococcus jannaschii, a hyperthermophile.";
RL Acta Crystallogr. D 55:338-340(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=10654930; DOI=10.1093/emboj/19.3.317;
RA Wang H., Boisvert D., Kim K.K., Kim R., Kim S.-H.;
RT "Crystal structure of a fibrillarin homologue from Methanococcus
RT jannaschii, a hyperthermophile, at 1.6-A resolution.";
RL EMBO J. 19:317-323(2000).
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 -!- MASS SPECTROMETRY: Mass=25971; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10089444};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin
CC family. {ECO:0000255|HAMAP-Rule:MF_00351}.
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DR EMBL; L77117; AAB98690.1; -; Genomic_DNA.
DR PIR; A64387; A64387.
DR RefSeq; WP_010870202.1; NC_000909.1.
DR PDB; 1FBN; X-ray; 1.60 A; A=1-230.
DR PDB; 1G8S; X-ray; 1.60 A; A=1-230.
DR PDBsum; 1FBN; -.
DR PDBsum; 1G8S; -.
DR AlphaFoldDB; Q58108; -.
DR SMR; Q58108; -.
DR IntAct; Q58108; 2.
DR STRING; 243232.MJ_0697; -.
DR EnsemblBacteria; AAB98690; AAB98690; MJ_0697.
DR GeneID; 1451564; -.
DR KEGG; mja:MJ_0697; -.
DR eggNOG; arCOG00078; Archaea.
DR HOGENOM; CLU_059055_2_0_2; -.
DR InParanoid; Q58108; -.
DR OMA; INMATHR; -.
DR OrthoDB; 58340at2157; -.
DR PhylomeDB; Q58108; -.
DR EvolutionaryTrace; Q58108; -.
DR Proteomes; UP000000805; 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..230
FT /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT /id="PRO_0000148533"
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"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1FBN"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1FBN"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1FBN"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1FBN"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1FBN"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1FBN"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:1FBN"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1FBN"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1FBN"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1FBN"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 168..179
FT /evidence="ECO:0007829|PDB:1FBN"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1FBN"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:1FBN"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1FBN"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:1FBN"
SQ SEQUENCE 230 AA; 25966 MW; 9ECAAD7C4C606756 CRC64;
MEDIKIKEIF ENIYEVDLGD GLKRIATKSI VKGKKVYDEK IIKIGDEEYR IWNPNKSKLA
AAIIKGLKVM PIKRDSKILY LGASAGTTPS HVADIADKGI VYAIEYAPRI MRELLDACAE
RENIIPILGD ANKPQEYANI VEKVDVIYED VAQPNQAEIL IKNAKWFLKK GGYGMIAIKA
RSIDVTKDPK EIFKEQKEIL EAGGFKIVDE VDIEPFEKDH VMFVGIWEGK
