ID A0A1M6G9N9_9FIRM Unreviewed; 456 AA.
AC A0A1M6G9N9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=23S rRNA (Uracil1939-C5)-methyltransferase {ECO:0000313|EMBL:SHJ06690.1};
GN ORFNames=SAMN02745751_01663 {ECO:0000313|EMBL:SHJ06690.1};
OS Dethiosulfatibacter aminovorans DSM 17477.
OC Bacteria; Bacillota; Tissierellia; Dethiosulfatibacter.
OX NCBI_TaxID=1121476 {ECO:0000313|EMBL:SHJ06690.1, ECO:0000313|Proteomes:UP000184052};
RN [1] {ECO:0000313|EMBL:SHJ06690.1, ECO:0000313|Proteomes:UP000184052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17477 {ECO:0000313|EMBL:SHJ06690.1,
RC ECO:0000313|Proteomes:UP000184052};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQZL01000010; SHJ06690.1; -; Genomic_DNA.
DR RefSeq; WP_073049121.1; NZ_FQZL01000010.1.
DR AlphaFoldDB; A0A1M6G9N9; -.
DR STRING; 1121476.SAMN02745751_01663; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000184052; 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:UP000184052};
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 6..64
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 287
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 316
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 337
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 456 AA; 51989 MW; ECDD8546EC05E72E CRC64;
MQENVEFKVN DIMEVEIVDI NHRGQGVARI DGFVVFVDDL IMGDEARIRI IEKKKNYGVG
KLVELTKKSE YRTEPQCKYF WECGGCQTMH IVYDKQLEYK KNRVESEIRK AIGENDIKIN
ETLGMENPYR YRNKGSFPVA RHRGNVAIGA YKLGTHDIVD LDKCIIQHEA ADRIVNTFRT
LMEVLKLEPY DEIAHKGLVK HLMIRSNRKN EIMLIIVTSK NKLPNKSEII GKLLEEIPEI
KSIVLNVNER QTNVILGNKN KVIYGKPVLK DWIYDLEFSI SPHSFFQVNP FQTEVLYSKA
LEYAELDEDK VVYDIYCGIG TISLAAARKS KHVYGIEIVQ AAIDDAKKNA VKNTIENADF
YCGKAEDVFP KLHSQGIDAD IVIVDPPRKG CEKSVLETII TMKPEKVVYV SCNPSTLARD
LKILGDGGYE ILEVQPVDMF PHGTHVECVV KLECRH
//
