ID L8DIU7_9NOCA Unreviewed; 392 AA.
AC L8DIU7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=23S rRNA methyltransferase/RumA {ECO:0000313|EMBL:CCQ16679.1};
GN ORFNames=RHODMAR_3299 {ECO:0000313|EMBL:CCQ16679.1};
OS Rhodococcus sp. AW25M09.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ16679.1, ECO:0000313|Proteomes:UP000011207};
RN [1] {ECO:0000313|EMBL:CCQ16679.1, ECO:0000313|Proteomes:UP000011207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ16679.1,
RC ECO:0000313|Proteomes:UP000011207};
RA Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA Smalaas A.O., Altermark B.;
RT "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL Submitted (DEC-2012) 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:CCQ16679.1}.
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DR EMBL; CAPS01000084; CCQ16679.1; -; Genomic_DNA.
DR AlphaFoldDB; L8DIU7; -.
DR STRING; 1268303.RHODMAR_3299; -.
DR eggNOG; COG2265; Bacteria.
DR Proteomes; UP000011207; 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; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR012340; NA-bd_OB-fold.
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};
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 REGION 176..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 349
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 322
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 392 AA; 41691 MW; 1A63D1695358AB1A CRC64;
MFVRHGLPGE RVLAKVTEDR GGSFCRADAV EILVPSVDRV DAVCPISGPG GSGCCDYSHA
SLEAGRTMKA SVVAEQLRRV AGIEREVLVE ELPGTGDGRG WRTRVRLAVD AGGQPGFHRY
RSSSILTELR CPQMDSVAYE GLSNRQWRPG SELQVVVDGS GERHVVEIAP AQVSRTGRRA
PGRRGAAARR AASSRARPEK AVIGSGRVTE FVSDRAWTLD ATGFWQAHRG AAQTYTDVVT
EWADASPGDG AWDLYGGVGV FAAALAPGVG STGHVSSVEF SRRAAEDGRS ALADLAQVSF
VPGRVERSMD ALTQPVSVAV LDPPRAGAGR DVIDALAARR PRSVVHVGCD PASFARDVSL
YRAAGYELTD VRAFDAFPLT SHVECIGRFV RG
//