ID A0A1H0E5X6_9BACI Unreviewed; 460 AA.
AC A0A1H0E5X6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=23S rRNA (Uracil1939-C5)-methyltransferase {ECO:0000313|EMBL:SDN77718.1};
GN ORFNames=SAMN04488053_103215 {ECO:0000313|EMBL:SDN77718.1};
OS Alkalicoccus daliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX NCBI_TaxID=745820 {ECO:0000313|EMBL:SDN77718.1, ECO:0000313|Proteomes:UP000198778};
RN [1] {ECO:0000313|Proteomes:UP000198778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10369 {ECO:0000313|Proteomes:UP000198778};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNIL01000003; SDN77718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0E5X6; -.
DR STRING; 745820.SAMN04488053_103215; -.
DR Proteomes; UP000198778; 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:0034470; P:ncRNA processing; IEA:UniProt.
DR GO; GO:0009451; P:RNA modification; IEA:UniProt.
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; 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 NCBIfam; TIGR00479; rumA; 1.
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.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000198778};
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 415
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 415
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 290
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 319
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 340
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 388
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 460 AA; 52126 MW; FB3A463DC9B2C601 CRC64;
MSAEFKAKIH SLDDKGSGRA EVWRENEKGN LKKLKLTLPQ TLRGEEVRVT VEERAKKRWR
TLPDEIINEH KERVTPPCPH FVKCGGCVWQ HWQYSGQLAE KTAHVKHAIE EQGFDPALVT
DTIGMEDPWH YRNKMEFTFS PEGALGLMEQ GNFRSVISLE TCLIAGKEMV EAAMEVADWN
TAHQLKGYDK DEHVGLLRHL MVRQSFATGE MMLGIFATES PDGPLTEPVN DLIKRIEEKF
PQVKSLLWLE NRDWADRAQS ENTHLLSGRD FIHDEMAGYK FRLWFDTFFQ TNPVQAQKLV
DIALDMAEPK ETEKMMDLFC GVGTFSLPFA NRVGKLAGIE LVESSIASAK RNAEDNGIHN
TTFLAENART GIDKMLESFG RPELLLLDPP RSGAGGKVMR RIGRAQPERI VYVSCNPDTL
ATDMKELADF GYELKALQPV DLFPQTVHVE CVARLEKAEK
//
