ID A0A0J5S525_9PAST Unreviewed; 393 AA.
AC A0A0J5S525;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=23S rRNA methyltransferase {ECO:0000313|EMBL:KMK51917.1};
GN ORFNames=RO21_03765 {ECO:0000313|EMBL:KMK51917.1};
OS Muribacter muris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Muribacter.
OX NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK51917.1, ECO:0000313|Proteomes:UP000036270};
RN [1] {ECO:0000313|EMBL:KMK51917.1, ECO:0000313|Proteomes:UP000036270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK51917.1,
RC ECO:0000313|Proteomes:UP000036270};
RA Christensen H., Nicklas W., Bisgaard M.;
RT "Reclassification of Actinobacillus muris as Muribacter muris.";
RL Submitted (DEC-2014) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-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:KMK51917.1}.
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DR EMBL; JWIZ01000021; KMK51917.1; -; Genomic_DNA.
DR RefSeq; WP_047976460.1; NZ_JWIZ01000021.1.
DR AlphaFoldDB; A0A0J5S525; -.
DR STRING; 67855.RO21_03765; -.
DR PATRIC; fig|67855.3.peg.609; -.
DR Proteomes; UP000036270; Unassembled WGS sequence.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR GO; GO:0001510; P:RNA methylation; IEA:GOC.
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; 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.
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:UP000036270};
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 10..71
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 276
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 393 AA; 44745 MW; DE6AE9F27E8AF6BC CRC64;
MALFYSDKRA KKVAQPTALQ RFAVQALDYQ GLGVAKLNGK TWFIENALPD EVVDADILEE
KRQYGRAQAV RFIQKSAKRQ DPHCAVYHQC GGCQMRHIPI ELQRDTKQST LFRRLQTLQA
EPIVCEPMLA GNAARYRRRA KFSVMWEKGQ LVIGFRQANS HAIIPLQDCD VLEPALAALL
PPLQRLFAAW QQKKAVGHIE LVRADNGVAM LLRHIGELKE ADRTHLLAFA EHYHLMLFVM
TDKDQLEQWY GEPPFYTING LKLGFSIRDF IQINADLNEK MVAQARENAQ RNGISNAAFY
QTDLDQSFID QPWAAQPFNK VLLDPARQGA YFALAHLCRL APERIVYVSC NPATLVRDAE
KLIQDGYRLA KCAMIDMFPH TAHLESISLF VKK
//