ID   Y1897_STAAM             Reviewed;         453 AA.
AC   Q99SY9;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Uncharacterized RNA methyltransferase SAV1897;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=SAV1897;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB58059.1; -; Genomic_DNA.
DR   RefSeq; WP_001147865.1; NC_002758.2.
DR   AlphaFoldDB; Q99SY9; -.
DR   SMR; Q99SY9; -.
DR   World-2DPAGE; 0002:Q99SY9; -.
DR   PaxDb; Q99SY9; -.
DR   EnsemblBacteria; BAB58059; BAB58059; SAV1897.
DR   KEGG; sav:SAV1897; -.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   OMA; FYAGDMK; -.
DR   PhylomeDB; Q99SY9; -.
DR   BioCyc; SAUR158878:SAV_RS10390-MON; -.
DR   Proteomes; UP000002481; 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 SAV1897"
FT                   /id="PRO_0000162016"
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;  51722 MW;  F1D4E4C8A68A5E7B 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 IGLYMAPHAK HVYGVEVVPS SIEDAQQNAT INQCNNTTFV
     CGKAEEVILQ WKAQGIKPDV VMVDPPRKGC DETFIQTLLT LEPKRIVYIS CNPATQQRDA
     LLLAEKYQLE EVTPVDMFPQ TTHVETVALF NLK