ID   Y1582_STAES             Reviewed;         456 AA.
AC   Q8CRU6;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Uncharacterized RNA methyltransferase SE_1582;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=SE_1582;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO05181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE015929; AAO05181.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_765137.1; NC_004461.1.
DR   RefSeq; WP_002485149.1; NC_004461.1.
DR   AlphaFoldDB; Q8CRU6; -.
DR   SMR; Q8CRU6; -.
DR   STRING; 176280.SE_1582; -.
DR   EnsemblBacteria; AAO05181; AAO05181; SE_1582.
DR   KEGG; sep:SE_1582; -.
DR   PATRIC; fig|176280.10.peg.1546; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   Proteomes; UP000001411; 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; 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   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..456
FT                   /note="Uncharacterized RNA methyltransferase SE_1582"
FT                   /id="PRO_0000162021"
FT   DOMAIN          3..61
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
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   456 AA;  52395 MW;  A554040E1C99AFB5 CRC64;
     METIKKNEVK TGKVIDLTHE GHGVVKVDRY PIFIPNALID EEIKFKLIKV KKNFAIGKLI
     EVISESDDRV TPPCIYYAKC GGCQLQHMTY RAQLDMKREQ VVNLFHRKGP FENTVIKETI
     GMVNPWRYRN KSQIPVGQSN SNQVIMGFYR QRSHDIIDMD SCLIQDRQHQ EVMNRVKYWL
     NELNISIYNE KTKTGLIRHL VVRTGYHTDE MMVIFVTNGA TFKQSELLVN KLKKEFPNIT
     SIKQNINNSH SNVIMGRQSM TLYGKDKIED QLSEVTYHIS DLSFYQINSS QTEKLYQQAL
     NYAQLTGKEI VLDTYCGIGT IGLYMAPLAK HVYGVEVVPQ AIKDAEDNAT KNQLKNTTFE
     CGKAEDVILT WKSQGIKPDV VMVDPPRKGC DETFLTTLLK LNPKRIVYIS CNPSTQQRDA
     QILAEQYELV EITPVDMFPQ TTHIETVALF VRKEEE