ID A0A0M8TQU0_9ACTN Unreviewed; 446 AA.
AC A0A0M8TQU0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KOU62364.1};
GN ORFNames=ADK57_24740 {ECO:0000313|EMBL:KOU62364.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU62364.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KOU62364.1}.
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DR EMBL; LGDG01000221; KOU62364.1; -; Genomic_DNA.
DR RefSeq; WP_053751743.1; NZ_LGDG01000221.1.
DR AlphaFoldDB; A0A0M8TQU0; -.
DR STRING; 1415546.ADK57_24740; -.
DR PATRIC; fig|1415546.3.peg.5362; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000037741; 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; 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 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; 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:UP000037741};
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 11..72
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 399
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 275
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 304
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 328
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 372
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 446 AA; 48339 MW; 0FCD75FCE1953BCD CRC64;
MQAEPKKTQA ASLVGEEYEV EVGPVAHGGH CIARTDEGQV LFVRHTLPGE RVVARVTDGE
EGARFLRADA VSVLSASKDR IEAPCPYAGP GRCGGCDWQH AKPGAQRRLK GEVVAEQLQR
LAGLTPEEAG WDGTVLPAEG DKLPAGQVPQ WRTRVQYAVT PDGQAGLRRH RSHEVEPIDH
CMIAAESVSE LGIEKRDWTG MESVEAIGAT GSQDRQVILT PRPGARLPLV ELDKPVSVMR
VEEKDGGVHR VHGRPFVRER ADGRTHRVGS GGFWQVHPKA ADTLVTAVMQ GLLPRKGEMA
LDLYCGVGLF AGALADRLGD QGAVLGIESG KRAVEDARHN LADFDRVRIE QGKVESVLPR
TGITEVDLIV LDPPRAGAGR KTVEHIASLD ARRIAYVACD PAALARDLGY FRDGGYRVRT
LRVFDLFPMT HHMECVAILE PANKAA
//
