ID A0A2D1SXL1_9BACL Unreviewed; 458 AA.
AC A0A2D1SXL1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=23S rRNA (Uracil(1939)-C(5))-methyltransferase RlmD {ECO:0000313|EMBL:ATP41861.1};
GN ORFNames=CSE16_18550 {ECO:0000313|EMBL:ATP41861.1};
OS Solibacillus sp. R5-41.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX NCBI_TaxID=2048654 {ECO:0000313|EMBL:ATP41861.1, ECO:0000313|Proteomes:UP000222866};
RN [1] {ECO:0000313|EMBL:ATP41861.1, ECO:0000313|Proteomes:UP000222866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R5-41 {ECO:0000313|EMBL:ATP41861.1,
RC ECO:0000313|Proteomes:UP000222866};
RA Guo Y., Chen Z., Wang H.;
RT "Complete genome sequence of Solibacillus sp. R5-41.";
RL Submitted (OCT-2017) 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; CP024123; ATP41861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D1SXL1; -.
DR KEGG; sob:CSE16_18550; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000222866; Chromosome.
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; IPR002792; TRAM_dom.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR NCBIfam; TIGR00479; rumA; 1.
DR PANTHER; PTHR11061:SF45; -; 1.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS50926; TRAM; 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:UP000222866};
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 DOMAIN 5..63
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
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 289
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"
FT BINDING 339
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 458 AA; 51745 MW; 942DF58F66093A42 CRC64;
MSEVKMEVGQ KFPLTIKKLG INGEGVGFYK RNVVFVKNAI PGEEVTVKLT KLQKNFSEAE
ILTIRKESEF RQEAPCPVYT ECGGCQLQHM TYDTQLLHKR DLVVQALEKY AKDVAAKTEI
RPTIGMENPW NYRNKSQFQV RKEGKRVYAG LFAENTNELL NINDCLVQHP MTSKITVGVR
KVLQKLNITI YDGKSLNGLV RTIVVRTGVK SGETQVCLVT TRNELPHKAE LIERIKKIDP
SIVSITQNVN RDKSSLIFGE ETLVLDGEMA IREKLGEFAF DLSTRAFFQL NPEQTVHLYN
EIKKAAALTG KENVVDAYCG VGTIGMWLAD GAREVRGMDN VDEAIADAKY NARSNANLQH
VRFFPGSADK WLFRWSKEGY RPDVISVDPP RTGLEPGFIK TVLNIKPKTF VYTSCNPSTL
ARDLQELSKI YDVEYIQPID MFPQTAQVEA VCRLVLRK
//