ID   Y1957_STAAC             Reviewed;         453 AA.
AC   Q5HEM5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Uncharacterized RNA methyltransferase SACOL1957;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=SACOL1957;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW38398.1; -; Genomic_DNA.
DR   RefSeq; WP_001147868.1; NC_002951.2.
DR   AlphaFoldDB; Q5HEM5; -.
DR   SMR; Q5HEM5; -.
DR   EnsemblBacteria; AAW38398; AAW38398; SACOL1957.
DR   KEGG; sac:SACOL1957; -.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   OMA; FYAGDMK; -.
DR   Proteomes; UP000000530; 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; 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; 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   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..453
FT                   /note="Uncharacterized RNA methyltransferase SACOL1957"
FT                   /id="PRO_0000162015"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         74
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         315
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         336
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         384
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   453 AA;  51682 MW;  6C2B04CE66888180 CRC64;
     MQAIAKNDIK TGTVVDLTHE GHGVVKIDRF PIFIPQALIN EQIEYKIIKV KKNFAIGKLL
     NINTRSENRV APPCIYYERC GGCQLQHLSY EAQLEMKKEQ VINLFQRKAH FDNSKINDTV
     GMTDPWRYRN KSQIPVGKNE QNEVIMGFYR QRSHDIIDME SCLIQDSQHQ EVMNEVKSIL
     KDLNVSIYQE QLKKGLMRHL VVRTGYHTDE MMIIFVTNGK KWPQKNAVVE KILDAFPNVT
     SIKQNINDSH SNVIMGRQSI TLYGKDTIID QLTDSTFKIS DQSFYQINSE QTEKLYNKAI
     EYAQLTGNEV VLDTYCGIGT IGLYMAPLAK HVYGVEVVPS AIEDAQQNAT INQCNNTTFV
     CGKAEEVILQ WKAQGIKPDV VMVDPPRKGC DETFIQTLLT LEPKRIVYIS CNPATQQRDA
     LLLAEKYQLE EVTPVDMFPQ TTHVETVALF NLK