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Database: UniProt
Entry: D4LWF3_9FIRM
LinkDB: D4LWF3_9FIRM
Original site: D4LWF3_9FIRM 
ID   D4LWF3_9FIRM            Unreviewed;       455 AA.
AC   D4LWF3;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:CBL21956.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:CBL21956.1};
GN   ORFNames=CK5_03360 {ECO:0000313|EMBL:CBL21956.1};
OS   Blautia obeum A2-162.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=657314 {ECO:0000313|EMBL:CBL21956.1, ECO:0000313|Proteomes:UP000008955};
RN   [1] {ECO:0000313|EMBL:CBL21956.1, ECO:0000313|Proteomes:UP000008955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2-162 {ECO:0000313|EMBL:CBL21956.1,
RC   ECO:0000313|Proteomes:UP000008955};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Ruminococcus obeum A2-162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL21956.1, ECO:0000313|Proteomes:UP000008955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2-162 {ECO:0000313|EMBL:CBL21956.1,
RC   ECO:0000313|Proteomes:UP000008955};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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; FP929054; CBL21956.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4LWF3; -.
DR   KEGG; rob:CK5_03360; -.
DR   PATRIC; fig|657314.3.peg.1471; -.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   Proteomes; UP000008955; Chromosome.
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};
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          2..60
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        410
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         284
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         313
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         334
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         383
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   455 AA;  51483 MW;  CCF5E330CB6EBC92 CRC64;
     MEYRKNDIVT LEIVDCGTDG EGIGKADGFT VFVKDAVIGD TVTAKIMKAK KNYGYGRLME
     ILKPSPYRVE PICPSARQCG GCQLQAVSYE EQKAFKEKKL RGHLERIGGF KELPMEPLIG
     MDEPYHYRNK AQFPVGRNKE GRIVTGFYAG RTHAIIENRD CALGIPQNKE VLDRVIAHME
     KYNIAPYDEM TGKGLVRHIF VRYGFFTGEL MVCLIINGQD LPHQKELVEK LGEIPGMTSI
     SLNINKKRNN VILGDKVKTI WGKEYITDKI GDISYEISPL SFFQVNPHQT WKLYSKALEY
     ADLHGEETVW DLYCGIGTIS LFLAQKAKFV RGVEIVPAAI EDARRNAHLN EIDNVEFFVG
     KAEEVLPREY EKNGVYADVI VVDPPRKGCD EMLLKTILKM QPKRVVYVSC DSATLARDLR
     FLCDNGYELK KVCGVDQFPQ TVHVEVVCCL HRVNS
//
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