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Database: UniProt
Entry: A0A1S2R1D5_9BACI
LinkDB: A0A1S2R1D5_9BACI
Original site: A0A1S2R1D5_9BACI 
ID   A0A1S2R1D5_9BACI        Unreviewed;       460 AA.
AC   A0A1S2R1D5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:OIK11637.1};
GN   ORFNames=BIV59_11400 {ECO:0000313|EMBL:OIK11637.1};
OS   Bacillus sp. MUM 13.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1678001 {ECO:0000313|EMBL:OIK11637.1, ECO:0000313|Proteomes:UP000180199};
RN   [1] {ECO:0000313|EMBL:OIK11637.1, ECO:0000313|Proteomes:UP000180199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUM 13 {ECO:0000313|EMBL:OIK11637.1,
RC   ECO:0000313|Proteomes:UP000180199};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Bacillus sp. MUM 13.";
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}.
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:OIK11637.1}.
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DR   EMBL; MLYQ01000038; OIK11637.1; -; Genomic_DNA.
DR   RefSeq; WP_071351605.1; NZ_MLYQ01000038.1.
DR   AlphaFoldDB; A0A1S2R1D5; -.
DR   Proteomes; UP000180199; 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:UP000180199};
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        416
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        416
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         291
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         320
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         341
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         389
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   460 AA;  51686 MW;  477E3C5840311393 CRC64;
     MKTEDNQLEV NQTFPLTIKR LGINGEGVGY FKRKVVFVPG ALPGEEIVAE AVKVQSKFSE
     AKIKTIRKPS PDRINPPCPV YEECGGCQLQ HMSYSRQLTE KRDIVIQSME RYGKVPLDSL
     NIKETIGMED PWFYRNKSQF QVGLKNGKVI AGLYGLNSHD LIDIPNCIVQ HPKSNKATRM
     IKKILTNLGI SIYNERKKKG AIRTIITRVG FETGEVQVVL VTNTEELPQK EKLIELIKSQ
     LPEVKSIIQN VNNKNTSLIF GDKTILLDGE QVITETLGDL SYELSARTFF QLNPIQTVKL
     YDEVKKAAAL TGTEKVVDAY CGVGTIGLWL AGDAKEVRGM DTIRESVEDA RQNAKRHKVN
     NVKYETGKAE NILPRWAKEG WKPDVLVADP PRSGLDDNLL QTILKVQPKK VIYVSCNPST
     LAKDLQILSK SYKVKYMQPV DMFPQTAHVE VVTELELNCN
//
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