ID   Y687_ALKHC              Reviewed;         458 AA.
AC   Q9KF10;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Uncharacterized RNA methyltransferase BH0687;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BH0687;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB04406.1; -; Genomic_DNA.
DR   PIR; G83735; G83735.
DR   RefSeq; WP_010896862.1; NC_002570.2.
DR   AlphaFoldDB; Q9KF10; -.
DR   SMR; Q9KF10; -.
DR   STRING; 272558.10173301; -.
DR   EnsemblBacteria; BAB04406; BAB04406; BAB04406.
DR   KEGG; bha:BH0687; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   OMA; FYAGDMK; -.
DR   OrthoDB; 1421660at2; -.
DR   Proteomes; UP000001258; 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:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
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; PF01938; TRAM; 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..458
FT                   /note="Uncharacterized RNA methyltransferase BH0687"
FT                   /id="PRO_0000161951"
FT   DOMAIN          5..65
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         78
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         387
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   458 AA;  51555 MW;  3D33A661E8891240 CRC64;
     MSKQQAPVNK NDVVEVTIED LTHDGAGVAK VDGYALFIPK ALPGERLKAK VVKVKKGYGF
     GRVLNMIEAS PDRVEAPCPV FNQCGGCQLQ HMSYDAQLRY KQKQVQDVLE RIGKITAVTV
     RPTIGMNEPW RYRNKAQVPV GEREGGLIAG FYQERSHRII DMDECMIQHE ENDKVIRQVK
     ELARELGIRG YDEEKHRGTL RHVVARYGKN TGEIMVVLIT RGEELPHKKT LIERIHKAIP
     HVKSIVQNVN PKRTNVIFGD KTKVLWGEEY IYDTIGDIKF AISARSFYQV NPEQTKVLYD
     QALEFANLTG SETVIDAYCG IGTISLFLAQ QAKHVYGVEI VPEAISDAKR NARLNGFANV
     QFAVGDAEKV MPWWYAQGVR ADVIVVDPPR KGCDEALLKT ILNMKPDRVV YVSCNPATLA
     RDLRVLEDGG YETKDVQPVD MFPWTTHIES VAVLELKN