ID   Y257_AQUAE              Reviewed;         425 AA.
AC   O66617;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Uncharacterized RNA methyltransferase aq_257;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=aq_257;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01024}.
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DR   EMBL; AE000657; AAC06582.1; -; Genomic_DNA.
DR   PIR; E70323; E70323.
DR   RefSeq; NP_213177.1; NC_000918.1.
DR   RefSeq; WP_010880115.1; NC_000918.1.
DR   AlphaFoldDB; O66617; -.
DR   SMR; O66617; -.
DR   STRING; 224324.aq_257; -.
DR   PRIDE; O66617; -.
DR   DNASU; 1192851; -.
DR   EnsemblBacteria; AAC06582; AAC06582; aq_257.
DR   KEGG; aae:aq_257; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_0; -.
DR   InParanoid; O66617; -.
DR   OMA; SIIHVMN; -.
DR   OrthoDB; 1421660at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..425
FT                   /note="Uncharacterized RNA methyltransferase aq_257"
FT                   /id="PRO_0000161945"
FT   DOMAIN          1..57
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        381
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         70
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         308
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         354
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   425 AA;  49137 MW;  1A84A8AF5402F633 CRC64;
     MKDKPLKLTV EKLVYGGYGF SRLNGKAVFV RFASPKELVE AKVVKEKKDY TEAVVTKVLI
     SSPARRKAPC PYYGECGGCQ IQHLNYEEQL RSKKDILLES LERIGKIKEV PYEGEIPSKK
     EFNYRVRVQF KIQENRVGFY RWDVKEVVDV EECLLAHERI NELIPHIREV LKVIKDLQEV
     HVNYSPTRDE ATLKFVTITH TDEKLLQNIL ENVLPEWVVG IGDYGKVGNS LVKRYKVGRE
     HIFMDVGKWQ YRVSNDSFFQ VNYTLWEDFL KEVLDFSESY KKGLDLHCGV GFFTIPLSEQ
     GNFIEGADAN PSAIKDAEYN AKINNRDNVI FEEATAFKHL KRRIGEVINL VVVDPPRSGL
     LREERDLLLK NKPDKIVYIS CNPTTFARDL KILTKGGYEL KRLKLIDNFP QTYHIESIAL
     LEVKD