ID A0A0G1XKK7_9BACT Unreviewed; 353 AA.
AC A0A0G1XKK7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase {ECO:0000313|EMBL:KKW31415.1};
GN ORFNames=UY76_C0058G0008 {ECO:0000313|EMBL:KKW31415.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWA2_52_8d.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618979 {ECO:0000313|EMBL:KKW31415.1, ECO:0000313|Proteomes:UP000034054};
RN [1] {ECO:0000313|EMBL:KKW31415.1, ECO:0000313|Proteomes:UP000034054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKW31415.1}.
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DR EMBL; LCRH01000058; KKW31415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1XKK7; -.
DR PATRIC; fig|1618979.3.peg.737; -.
DR Proteomes; UP000034054; 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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
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.
DR PROSITE; PS01231; TRMA_2; 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 ACT_SITE 311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 311
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 284
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 353 AA; 40048 MW; 6BE5E134B7630A68 CRC64;
MSTPCPHEDV CGSCSWAHIP YEKQLKQKFS DINGSFRLKE LPPWCKTILP SPVTEHYRNR
MDFVIDFEGR VGMREKGKWW RVVDGNTCFL ADEQIDTLFV QVRDWVKQSG LSYYDRKTSE
RVPPISTEPG EVISDKIVST PFHPTTFIWS QNSTITDVSF GDKLETISGP GYIEEEILGS
RYRISPNAFF QTNPHGAALL LQTVEGFCGD LSGRTLLDLY CGSGFFSVAL ANRATRTIGV
EMVQEAIDDA RVNAQLNNVN IEFHDAKTEK FDWTQFGADV VILDPPRSGM HDKALADILK
NPPEEIVYVS CNFKNFAREM VQLQNIYRVD GMRAIDLFPH TPHVELVTKL SRI
//
