ID A0A1G7T5G8_9ACTN Unreviewed; 423 AA.
AC A0A1G7T5G8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family {ECO:0000313|EMBL:SDG30546.1};
GN ORFNames=SAMN05660324_2317 {ECO:0000313|EMBL:SDG30546.1};
OS Klenkia brasiliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Klenkia.
OX NCBI_TaxID=333142 {ECO:0000313|EMBL:SDG30546.1, ECO:0000313|Proteomes:UP000198863};
RN [1] {ECO:0000313|EMBL:SDG30546.1, ECO:0000313|Proteomes:UP000198863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44526 {ECO:0000313|EMBL:SDG30546.1,
RC ECO:0000313|Proteomes:UP000198863};
RA de Groot N.N.;
RL Submitted (OCT-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; FNCF01000003; SDG30546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7T5G8; -.
DR Proteomes; UP000198863; 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 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; 2.
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 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};
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..65
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 370
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 271
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 295
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 343
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 423 AA; 44044 MW; 327D4D914107BE53 CRC64;
MSTDRDSWVG QRFEVTVGPV AHGGHCVARH EGRVVFVRHA LPGERVVVAV TEDRHPGYCR
ADAVEVLDAS PDRVERPCKA SGPGRCGGCD WQHVDPAAQR RLKADVVTEQ FGRLAGMDVA
LDVEELPGGP LRWRSRARFA VDRAGRPGLR PHRSRDVVVL EDCPITVEPA VAAVLGRRWD
GAGAVDVAVD SVGGVTTTVL DRRGHARSTK VARPTGAEVT GARAERRAWH RDWQVEGTGF
WQVHPAAADA LVGAVAGFVG VRPGERVLDL YAGAGLFGGS LAAGVGAGGQ VVCVESDAGA
CAAAADNLAD LPQAEVWQGD VDAEGLAGLL AELDGPPDVV VLDPPRSGAG REVSEVLAGS
GARAVAYVAC DPASLARDVA VFAGAGWRLA GLRAFDAFPM TAHVECVALL LPGAQPVASA
ERS
//