ID A0A1G5S6L9_9FIRM Unreviewed; 460 AA.
AC A0A1G5S6L9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:SCZ81209.1};
GN ORFNames=SAMN03080599_02660 {ECO:0000313|EMBL:SCZ81209.1};
OS Acidaminobacter hydrogenoformans DSM 2784.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XII. Incertae Sedis; Acidaminobacter.
OX NCBI_TaxID=1120920 {ECO:0000313|EMBL:SCZ81209.1, ECO:0000313|Proteomes:UP000199208};
RN [1] {ECO:0000313|EMBL:SCZ81209.1, ECO:0000313|Proteomes:UP000199208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2784 {ECO:0000313|EMBL:SCZ81209.1,
RC ECO:0000313|Proteomes:UP000199208};
RA de Groot N.N.;
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; FMWL01000017; SCZ81209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5S6L9; -.
DR STRING; 1120920.SAMN03080599_02660; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000199208; 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; IPR002792; TRAM_dom.
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; 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:UP000199208};
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 1..58
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 412
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 385
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 460 AA; 50879 MW; EE41B853BF5E646A CRC64;
MKKNQIVNLT IEEMENLQEG IGYIDQKPVY VKGALKGQKV EVRISRNRKL HAEGKLLSVL
EKSEVEKASF CSHYGECGGC SLQTLPYDTQ VEMKKDWIGG LLEASLSPEV FESIDFTGVL
PSPKRLAYRN KMEFTFGNAV KGGETNLGLH KKGQFGSVIT TNQCQICDSD FTDILEAALN
LFKRLGVDHY SKFSHEGVLR HLVVRKGEKT GEILVALSAV GARPEDLKVF VDVLLGLELQ
DEIVGILYVE NPGKADAVNG EPVVLFGRDH YFDEILGLKF RVSLYSFFQT NTLGAERLYQ
TAFDGLEDIQ GKYVFDLFSG TGTIAQLLAQ RAERVVGVEI VADAVEAAIA NAAENQLSRC
EFRVGDVLEI LDHYEGHKPD VIVVDPPRMG IAPKALEKII AFGAPEILYI SCNPKTLVEN
LSVMSQSGYQ PVKVTGVDMF PHTGHCETIC WLKRRGGNME
//