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Database: UniProt
Entry: A0A257L479_9BACT
LinkDB: A0A257L479_9BACT
Original site: A0A257L479_9BACT 
ID   A0A257L479_9BACT        Unreviewed;       470 AA.
AC   A0A257L479;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=23S rRNA (Uracil(1939)-C(5))-methyltransferase RlmD {ECO:0000313|EMBL:OYU94447.1};
GN   ORFNames=CFE21_15680 {ECO:0000313|EMBL:OYU94447.1};
OS   Bacteroidetes bacterium B1(2017).
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=2015582 {ECO:0000313|EMBL:OYU94447.1, ECO:0000313|Proteomes:UP000216329};
RN   [1] {ECO:0000313|EMBL:OYU94447.1, ECO:0000313|Proteomes:UP000216329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|EMBL:OYU94447.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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:OYU94447.1}.
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DR   EMBL; NKJG01000007; OYU94447.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257L479; -.
DR   Proteomes; UP000216329; 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; 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:UP000216329};
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          1..64
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        428
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         302
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         331
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         352
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         401
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   470 AA;  53774 MW;  2EC924576E36FFF4 CRC64;
     MGKKKSKEPK FYENLHIVAA GSEGKSIARP EGMVVMLDYA VPGDIVNARV IQSKRRFEIA
     TITEVVTPSE DRVPTFCEHF GTCGGCKWQQ MSYESQLRYK QQQVLDSFER IGKFPFPPME
     PILGSAQTTH YRNKVEFSFT DRKWLTHATD IGTLSKAENA GLGYHIPGRF DKVFDMFTCH
     LMAPLNDAIR NSVRDFCLEH DYDFFNLYGQ TGFMRNMTLR NNMRGEWMLI VSFGHEDKEK
     REALLAHLHK NFPEIKALLY VINEKRNDTI FDLDIQVFAG DDFLIEELED LKFKIGPKSF
     FQTNAYQTIE LYKKAREFAA LTGEELVYDL YTGVGTIALF VSKMAKKVVG IEYVEQAIED
     AKKNAALNNI THTDFFAGDM KDLLTAEFMD LHGRPDVVIT DPPRAGMHED VIAQLLQVRP
     KRIVYVSCNP ATQARDIALL TDVYEVKKVQ PVDMFPHTHH VENIALLELK
//
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