ID   FLPA_AERPE              Reviewed;         233 AA.
AC   Q9Y9U3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=APE_2196;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE.
RX   PubMed=22869109; DOI=10.1107/s1744309112026528;
RA   de Silva U., Zhou Z., Brown B.A. II;
RT   "Structure of Aeropyrum pernix fibrillarin in complex with natively bound
RT   S-adenosyl-L-methionine at 1.7 A resolution.";
RL   Acta Crystallogr. F 68:854-859(2012).
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}.
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; BA000002; BAA81207.1; -; Genomic_DNA.
DR   PIR; G72527; G72527.
DR   PDB; 4DF3; X-ray; 1.73 A; A/B=1-233.
DR   PDBsum; 4DF3; -.
DR   AlphaFoldDB; Q9Y9U3; -.
DR   SMR; Q9Y9U3; -.
DR   STRING; 272557.APE_2196; -.
DR   EnsemblBacteria; BAA81207; BAA81207; APE_2196.
DR   KEGG; ape:APE_2196; -.
DR   PATRIC; fig|272557.25.peg.1467; -.
DR   eggNOG; arCOG00078; Archaea.
DR   OMA; INMATHR; -.
DR   Proteomes; UP000002518; 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..233
FT                   /note="Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase"
FT                   /id="PRO_0000148528"
FT   BINDING         90..91
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:22869109"
FT   BINDING         109..110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:22869109"
FT   BINDING         134..135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:22869109"
FT   BINDING         154..157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:22869109"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          16..21
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          26..31
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   HELIX           61..67
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          80..84
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   HELIX           90..99
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   HELIX           112..121
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          128..133
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   HELIX           138..141
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   HELIX           160..171
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          172..183
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   HELIX           186..190
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   HELIX           195..206
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          210..216
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   TURN            218..220
FT                   /evidence="ECO:0007829|PDB:4DF3"
FT   STRAND          224..230
FT                   /evidence="ECO:0007829|PDB:4DF3"
SQ   SEQUENCE   233 AA;  26700 MW;  83B5DA5A48D1F372 CRC64;
     MVEVVSVREH DRWRGVYVVE LEDGSLRIAT KNLVPGQRVY GERIFRYNGE EYREWNAYRS
     KLAAALLKGL IELPVKEGDR ILYLGIASGT TASHMSDIIG PRGRIYGVEF APRVMRDLLT
     VVRDRRNIFP ILGDARFPEK YRHLVEGVDG LYADVAQPEQ AAIVVRNARF FLRDGGYMLM
     AIKARSIDVT TEPSEVYKRE IKTLMDGGLE IKDVVHLDPF DRDHAMIYAV MRR