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Database: UniProt
Entry: A0A1B9XX56_9FLAO
LinkDB: A0A1B9XX56_9FLAO
Original site: A0A1B9XX56_9FLAO 
ID   A0A1B9XX56_9FLAO        Unreviewed;       483 AA.
AC   A0A1B9XX56;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:OCK42148.1};
GN   ORFNames=BA195_11005 {ECO:0000313|EMBL:OCK42148.1};
OS   Tenacibaculum soleae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=447689 {ECO:0000313|EMBL:OCK42148.1, ECO:0000313|Proteomes:UP000093186};
RN   [1] {ECO:0000313|EMBL:OCK42148.1, ECO:0000313|Proteomes:UP000093186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-KL19 {ECO:0000313|EMBL:OCK42148.1,
RC   ECO:0000313|Proteomes:UP000093186};
RA   Eisen J.A., Coil D.A., Lujan K.M.;
RT   "Draft Genome Sequence of Tenacibaculum soleae UCD-KL19.";
RL   Submitted (JUN-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:OCK42148.1}.
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DR   EMBL; MAKX01000024; OCK42148.1; -; Genomic_DNA.
DR   RefSeq; WP_068705519.1; NZ_MAKX01000024.1.
DR   AlphaFoldDB; A0A1B9XX56; -.
DR   STRING; 447689.BA195_11005; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000093186; 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:UP000093186};
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          9..71
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        441
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         310
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"
FT   BINDING         366
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         414
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   483 AA;  54732 MW;  184F91A565D1B51C CRC64;
     MPRRERNKFV KRNQVLELKI EDYAFGGKGI ARIHSEEGSF VVFVPNTLPG QLVKAQIKKS
     SKKYAEAKLM DVLQASDDEV TVPFQDIPGA PYIQLPIDLQ HQYKKESTLS LFKRIGKVAN
     IDDLFDEFIT SPNVFHYRNK MEYGFSAIGY DRVNKTDADF FTLGFKRRGV WWMGDNLNKD
     SGLFDAQVED NLKVIREYCE KTGLAPWHGP KKEGFFRYFV VRKSYKTNEL LFNLVTTSYD
     LPKFDMQAFA TLLKDIFGER LAGLLHTIND EVGDRTIATS GSIELIAGKD KIIEELLGLN
     FEISMKSFFQ TNPKSAEKLY TKVIDYALEN KEAIDNTVVM DLFCGTGTIG QILASRSQNA
     KIVGVDIVAS AIEDAKKNAK RNKIEGLEFY AADVGKFLNE HPQFQNKIRT IILDPARAGI
     APKTLKKIIN LNADRMVYVS CNPATQARDT EELINCGYQL KKISLVDQFP HTAHIETVVL
     FEK
//
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