ID A0A1H1GDE4_9BACI Unreviewed; 466 AA.
AC A0A1H1GDE4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SDR11119.1};
GN ORFNames=SAMN05216231_3652 {ECO:0000313|EMBL:SDR11119.1};
OS Virgibacillus salinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=553311 {ECO:0000313|EMBL:SDR11119.1, ECO:0000313|Proteomes:UP000199444};
RN [1] {ECO:0000313|EMBL:SDR11119.1, ECO:0000313|Proteomes:UP000199444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10449 {ECO:0000313|EMBL:SDR11119.1,
RC ECO:0000313|Proteomes:UP000199444};
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; FNKD01000005; SDR11119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1GDE4; -.
DR STRING; 553311.SAMN05216231_3652; -.
DR Proteomes; UP000199444; 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; 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:UP000199444};
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 7..65
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 413
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 288
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 317
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 338
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 386
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 466 AA; 52390 MW; ED68DFCCCC9A67D0 CRC64;
MAKHTAPVEK NETITLNFED LTHEGNGVGK INGYPLFVPQ ALPGEEGKVK VVKANKNFGF
GKLLELTKES PDRIEPVCHV HCNGCGLQHM SYSLQLEMKQ NQVKNAMKKI AHLEHVPVKS
IIGMDDPLHY RNKVQIPVGE KNGELITGFY QKRSHRIIEN TETCVTHNEV INGVVKSVRD
IANRLGIKAY NEQKHNGVLR HIMVRTGEET KDIMVVLVTR TDKLPHQDEL VKELTSEFPH
IKSVVHNVNH KRTNVIMGDK SKVIWGDEYI HDKIGEITFA ISAKSFYQVN PAQTRKLYDK
ALEYADIGTK DTVIDAYCGI GTISLFMAQK ARKVYGVEVV PEAISDAKKN AKLNGITNAE
FYVGEAEKVM PWWKMQGLNP DVIVVDPPRK GCDEELLKAM TEMQPKRIVY VSCNPSTLAR
DLRVLEDRGY ATQVVQPVDM FPQTGHVECC ALIERVKDYA VGSENL
//