ID   Y2648_BRADU             Reviewed;         415 AA.
AC   Q89RW4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Uncharacterized RNA methyltransferase bll2648;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=bll2648;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC47913.1; -; Genomic_DNA.
DR   RefSeq; NP_769288.1; NC_004463.1.
DR   RefSeq; WP_011085434.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89RW4; -.
DR   SMR; Q89RW4; -.
DR   STRING; 224911.27350904; -.
DR   PRIDE; Q89RW4; -.
DR   EnsemblBacteria; BAC47913; BAC47913; BAC47913.
DR   GeneID; 64022403; -.
DR   KEGG; bja:bll2648; -.
DR   PATRIC; fig|224911.44.peg.2248; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_8_0_5; -.
DR   InParanoid; Q89RW4; -.
DR   OMA; SIIHVMN; -.
DR   PhylomeDB; Q89RW4; -.
DR   Proteomes; UP000002526; 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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05175; MTS; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 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..415
FT                   /note="Uncharacterized RNA methyltransferase bll2648"
FT                   /id="PRO_0000161959"
FT   ACT_SITE        373
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         66
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         300
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         347
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   415 AA;  44446 MW;  C5CA86C3D21D2F3D CRC64;
     MVERLRIDHV GHRGDGVALG AGEAIYVPYA LGGETVEVDH VAGNHPDRRK LLAVDVASPE
     RVAPFCPHFG ICGGCAIQHW AAEPYHAWKR SIVVETLAQA GIDCEVAPLV DAHGVGRRRV
     TLHGRFGTHD ILKVGFSAAS SHDVIPIHRC PILDPALDGA LDAAWALAEP LTSKMPVTKP
     LDIQVTATTN GLDVDVRGSG PLPTPLVTAL SRVAEQHRLA RLTRHGELVL QRLPPTVKMG
     RTEVTLPPGS FLQATVAGEE TLASLVAERV GKAKEVLDLF CGVGPFALRL AEKARVTAYD
     SDAGAVAALA KAARTPGLKP IRCEPRDLFR RPLVPQELRD FDAVVFDPPR QGAQAQALKL
     AASTVPVIVA VSCNVATFAR DARLLIDGGY RIDGVVPVDQ FRHTPHVELV ARFAR