ID A0A1A3Q124_9MYCO Unreviewed; 401 AA.
AC A0A1A3Q124;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=23S rRNA methyltransferase {ECO:0000313|EMBL:OBK40128.1};
GN ORFNames=A5658_22820 {ECO:0000313|EMBL:OBK40128.1};
OS Mycobacterium sp. 1245111.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834073 {ECO:0000313|EMBL:OBK40128.1, ECO:0000313|Proteomes:UP000092232};
RN [1] {ECO:0000313|EMBL:OBK40128.1, ECO:0000313|Proteomes:UP000092232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1245111.1 {ECO:0000313|EMBL:OBK40128.1,
RC ECO:0000313|Proteomes:UP000092232};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
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:OBK40128.1}.
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DR EMBL; LZLV01000034; OBK40128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A3Q124; -.
DR STRING; 1834073.A5658_22820; -.
DR Proteomes; UP000092232; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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 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.
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 DOMAIN 1..63
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 359
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 332
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 401 AA; 42645 MW; EAE79C0A90730D28 CRC64;
MTAAPPPALG ELTLTVGPPA NGGSCVARHD GRVVFVRYAL PGEQVRVQVT ADRGSYWHAE
AIEVIEPSAD RTASLCPIAG VDGAGCCDLA FVDPAAARAL KAEVVSNQLA RLGNYQWRDP
DVQPLKPTGP TGWRTRIRLD VGADGRPGFH RYRSDELVTG LNCAQLPAGM TDGLADTAWP
SGAHLHVVVD DDGQRHVART VRHGRRNATE VVEGSHQGVH RAGRHSWQVP VTGFWQAHRD
AARTYSDLVS DWARPDPGMT AWDLYGGAGL FAAILADAVG ESGQVLSVDS ARAASRAARA
TLADLPQVRV VSDSVRRALT AQNGRADVAV LDPPRGGAGR DVIDLLAAAE VPRIVHIGCE
AASFARDIGL YQGHGYAVHK LSVFDSFPLT HHIECVALLA R
//