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Database: UniProt
Entry: A0A1H1GH33_9BACI
LinkDB: A0A1H1GH33_9BACI
Original site: A0A1H1GH33_9BACI 
ID   A0A1H1GH33_9BACI        Unreviewed;       500 AA.
AC   A0A1H1GH33;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=23S rRNA (Uracil1939-C5)-methyltransferase {ECO:0000313|EMBL:SDR12373.1};
GN   ORFNames=SAMN05216231_3713 {ECO:0000313|EMBL:SDR12373.1};
OS   Virgibacillus salinus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=553311 {ECO:0000313|EMBL:SDR12373.1, ECO:0000313|Proteomes:UP000199444};
RN   [1] {ECO:0000313|EMBL:SDR12373.1, ECO:0000313|Proteomes:UP000199444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10449 {ECO:0000313|EMBL:SDR12373.1,
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; SDR12373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1GH33; -.
DR   STRING; 553311.SAMN05216231_3713; -.
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; 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; 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; 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   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        451
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        451
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         326
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         355
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         376
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         424
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   500 AA;  55877 MW;  00EC2FCF473E49E3 CRC64;
     MPMTKKKNSE SRKKGKKHNK SEKQYVARGS RTEGGKSKGK HTANNARQRS QKNATAEVTC
     SGLTNDGKGI VQWKGKQLEV AHLMPGETAE VNISKKGRFF DTELKRVIKP SEDRANLSRS
     SYYEGVGCHI QHMNEHAQKR FKQKIIDELM KPFGKPEPII TMELPFYYRN KNVMTFGLNK
     KRQIICGLYA ENTHQIIPME RSIIHDQKAD EIIQTIKGMM KSFKMQPYNE DTGQGFLRHV
     LVRVGKKSGE IMVVLVAASP MFKGSNNFVK ALRKEHPEIT TILLNVNNRD TSMVLGKQEK
     VLFGKGTITD TLCGLKFDIS AKSFYQINPV QTEKLYAKAI DMAELTGKET VVDAYCGIGT
     IGLIASKKAG KVIGVELNND AVRDAIHNSK RNGVKNARFY QGDAGEFMVK MAARGEKADV
     VIMDPPRSGS DEAFLSSMVK LQPKRVVYVS CNPVTQARDL KYLEKNGYAV EGIQPVDMFP
     QTAHVEAVAK LVLKEEAGNR
//
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