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Database: UniProt
Entry: A0A1I6C110_9BACI
LinkDB: A0A1I6C110_9BACI
Original site: A0A1I6C110_9BACI 
ID   A0A1I6C110_9BACI        Unreviewed;       459 AA.
AC   A0A1I6C110;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SFQ86861.1};
GN   ORFNames=SAMN04488577_2900 {ECO:0000313|EMBL:SFQ86861.1};
OS   Bacillus sp. cl95.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ86861.1, ECO:0000313|Proteomes:UP000199578};
RN   [1] {ECO:0000313|EMBL:SFQ86861.1, ECO:0000313|Proteomes:UP000199578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL95 {ECO:0000313|EMBL:SFQ86861.1,
RC   ECO:0000313|Proteomes:UP000199578};
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; FOYF01000004; SFQ86861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6C110; -.
DR   STRING; 1761761.SAMN04488577_2900; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000199578; 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:SF45; -; 1.
DR   PANTHER; PTHR11061; RNA M5U 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:UP000199578};
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          8..66
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        417
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         292
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         321
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         342
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         390
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   459 AA;  51401 MW;  05F63C489F8377A8 CRC64;
     MNNQQTVKIQ PKQTFPLTIK RLGINGEGVG YFKRQVVFVP GALPGEEVVV EVTNVNPRFA
     EAKIKKIRIA SKERVQPPCP VYDQCGGCQL QHLSYAGQLR EKRDIVIQSL ERHTKLNLFA
     MDIRPTIGME DPWGYRNKSS FQVRQKAGKV LAGLYGLNSH QLINIEHCAV QHSQTNEATL
     AVRSILEELK IPIYNEKMQK GLVRTIVARV GVQTNELQVV LITTQKEIPN RDLLIEKIQS
     KLPNLKSIVQ NINGEKTSLI FGDETEVMAG EEFIQETLGD LQFELSARTF FQLNPTQTVN
     LYNEVKKAAA LTGVEKVVDA YCGVGTIGLW LADKAAEVRG MDIIPESIDD AKKNAKRHGF
     THTKYVPGKA EEVLPKWVKK GWKPDVIVVD PPRTGLDAQL LQTILNVKPQ KVVYVSCNPS
     TLAKDIQTLS KSYNVDYIQP VDMFPQTSHV ECVAKLIIK
//
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