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Database: UniProt
Entry: C0W1I3_9ACTO
LinkDB: C0W1I3_9ACTO
Original site: C0W1I3_9ACTO 
ID   C0W1I3_9ACTO            Unreviewed;       396 AA.
AC   C0W1I3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Putative 23S rRNA (Uracil-5-)-methyltransferase RumB {ECO:0000313|EMBL:EEH63349.1};
GN   ORFNames=HMPREF0044_1273 {ECO:0000313|EMBL:EEH63349.1};
OS   Gleimia coleocanis DSM 15436.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Gleimia.
OX   NCBI_TaxID=525245 {ECO:0000313|EMBL:EEH63349.1, ECO:0000313|Proteomes:UP000010301};
RN   [1] {ECO:0000313|EMBL:EEH63349.1, ECO:0000313|Proteomes:UP000010301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15436 {ECO:0000313|EMBL:EEH63349.1,
RC   ECO:0000313|Proteomes:UP000010301};
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:EEH63349.1}.
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DR   EMBL; ACFG01000034; EEH63349.1; -; Genomic_DNA.
DR   RefSeq; WP_006546131.1; NZ_DS999540.1.
DR   AlphaFoldDB; C0W1I3; -.
DR   STRING; 525245.HMPREF0044_1273; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_0_0_11; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000010301; 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; 1.
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:UP000010301};
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        345
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        345
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         219
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         248
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         269
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   396 AA;  44019 MW;  512D705ACA446061 CRC64;
     MFNQVSESPQ LCSYYAAQQC LSCPQIEVPY EQQVAEKTAR VKSLLPMIAE DAWLPTQESA
     SVGFRNKAKM VVTGSAANAM LGILGSDYAG QDLTECPLYS QHMRDFLKTF QRWIRELGIS
     PYSVKERRGE LKYILVTESP DGQFLVRWVL RSHRWVSRLR NFVSVMQEEF PEIAVVSANI
     LAEHVALTEG PEEISLYGDY LPFQLGRVKL QLLPRSFFQT NTFIAHAMYQ QAQRWAIALK
     PDRAVDLFCG VGGFALFLAA TCRAVTGVEL SAPAIAAAKR GAVASGLENV DFYAADATSF
     SISEGGLQLT RRDMIVVNPP RRGIGVELAN WINESQARVI IYSSCNPVSL AKDMELLGSY
     KATRARVFDM FPGTDHAEVM VLLVKEPQGN AERKTV
//
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