FLPA_PYRHO
ID FLPA_PYRHO Reviewed; 227 AA.
AC O57811;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, 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 EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00351};
GN Name=flpA {ECO:0000255|HAMAP-Rule:MF_00351}; OrderedLocusNames=PH0052;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RG Berkeley structural genomics center (BSGC);
RT "A structural approach to gene function and structure quality for
RT Pyrococcus horikoshii fibrillarin.";
RL Submitted (JAN-2005) to the PDB data bank.
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; BA000001; BAA29120.1; -; Genomic_DNA.
DR PIR; A71224; A71224.
DR RefSeq; WP_010884167.1; NC_000961.1.
DR PDB; 1G8A; X-ray; 1.40 A; A=1-227.
DR PDBsum; 1G8A; -.
DR AlphaFoldDB; O57811; -.
DR SMR; O57811; -.
DR STRING; 70601.3256437; -.
DR EnsemblBacteria; BAA29120; BAA29120; BAA29120.
DR GeneID; 1443949; -.
DR KEGG; pho:PH0052; -.
DR eggNOG; arCOG00078; Archaea.
DR OMA; INMATHR; -.
DR OrthoDB; 58340at2157; -.
DR EvolutionaryTrace; O57811; -.
DR Proteomes; UP000000752; 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; RNA-binding; rRNA processing; Transferase;
KW tRNA processing.
FT CHAIN 1..227
FT /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT /id="PRO_0000148546"
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"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1G8A"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1G8A"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1G8A"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1G8A"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1G8A"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1G8A"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1G8A"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1G8A"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 168..179
FT /evidence="ECO:0007829|PDB:1G8A"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1G8A"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:1G8A"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1G8A"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:1G8A"
SQ SEQUENCE 227 AA; 25828 MW; 1B634D4DC15103E8 CRC64;
MVEVKKHKFP GVYTVIDDDG SERIATKNLV PGQRVYGERV IKWEGEEYRI WNPNRSKLGA
AIMNGLKNFP IKPGKSVLYL GIASGTTASH VSDIVGWEGK IFGIEFSPRV LRELVPIVEE
RRNIVPILGD ATKPEEYRAL VPKVDVIFED VAQPTQAKIL IDNAEVYLKR GGYGMIAVKS
RSIDVTKEPE QVFREVEREL SEYFEVIERL NLEPYEKDHA LFVVRKT
