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Database: UniProt
Entry: C0W460_9ACTO
LinkDB: C0W460_9ACTO
Original site: C0W460_9ACTO 
ID   C0W460_9ACTO            Unreviewed;       410 AA.
AC   C0W460;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Putative 23S rRNA (Uracil-5-)-methyltransferase RumB {ECO:0000313|EMBL:EEH66482.1};
GN   ORFNames=HMPREF0058_0654 {ECO:0000313|EMBL:EEH66482.1};
OS   Actinomyces urogenitalis DSM 15434.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=525246 {ECO:0000313|EMBL:EEH66482.1, ECO:0000313|Proteomes:UP000004778};
RN   [1] {ECO:0000313|EMBL:EEH66482.1, ECO:0000313|Proteomes:UP000004778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15434 {ECO:0000313|EMBL:EEH66482.1,
RC   ECO:0000313|Proteomes:UP000004778};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEH66482.1}.
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DR   EMBL; ACFH01000044; EEH66482.1; -; Genomic_DNA.
DR   RefSeq; WP_006547621.1; NZ_DS999574.1.
DR   AlphaFoldDB; C0W460; -.
DR   STRING; 103621.GCA_001067145_01514; -.
DR   GeneID; 81708784; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_0_0_11; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000004778; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000004778};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}.
FT   ACT_SITE        366
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        366
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         238
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         271
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         292
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   410 AA;  43951 MW;  C1DC1D99DB3EBAD5 CRC64;
     MTATGPSAAF CQRHRAGTCH SCPHQDLPLA EQLALKQARV AALLADGAAA LSPQVWQEPV
     ASAASRFRNK AKMVVSGTVQ APVLGILGPQ GRGIDLRACP LHVEAIEEAL PVLARTVTRL
     GLVPYDVSAR RGELKHLLVT ASPDGDLMVR WVLRSRRHLE VLRDELPRLR EELETLAVMS
     VNLQPVHQAI IEGEEEIVLT TEPGGDRLLM RLELPEQAGP SADHRDLPLL LPTQSFFQTN
     TAVAEQLYAT AARWAGDLDT GSRPAQVWDL FCGVGGFALA LAGPGRQVLG VEVSAPAIDG
     ARQAARLMGL DAQAARFEAG DARVLDPGAG AVPDLLVLNP PRRGIGQDLA ARIESAGVER
     VLYSSCNPAS LARDLEAMSS YTAVRAQLFD MFPHTDHAEV LIELRRSPSA
//
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