Y1838_STAAW
ID Y1838_STAAW Reviewed; 453 AA.
AC Q8NVT4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Uncharacterized RNA methyltransferase MW1838;
DE EC=2.1.1.-;
GN OrderedLocusNames=MW1838;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(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; BA000033; BAB95703.1; -; Genomic_DNA.
DR RefSeq; WP_001147864.1; NC_003923.1.
DR AlphaFoldDB; Q8NVT4; -.
DR SMR; Q8NVT4; -.
DR EnsemblBacteria; BAB95703; BAB95703; BAB95703.
DR KEGG; sam:MW1838; -.
DR HOGENOM; CLU_014689_7_0_9; -.
DR OMA; FYAGDMK; -.
DR Proteomes; UP000000418; 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 MW1838"
FT /id="PRO_0000162020"
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; 51706 MW; 6C2B04C8A68A4184 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 AIEDAQQNAT INQCNNTTFV
CGKAEEVILQ WKAQGIKPDV VMVDPPRKGC DETFIQTLLT LEPKRIVYIS CNPATQQRDA
LLLAEKYQLE EVTPVDMFPQ TTHVETVALF NLK