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Database: UniProt
Entry: D7GVA9_9FIRM
LinkDB: D7GVA9_9FIRM
Original site: D7GVA9_9FIRM 
ID   D7GVA9_9FIRM            Unreviewed;       475 AA.
AC   D7GVA9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:CBL41751.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:CBL41751.1};
GN   ORFNames=CK3_21520 {ECO:0000313|EMBL:CBL41751.1};
OS   butyrate-producing bacterium SS3/4.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL41751.1, ECO:0000313|Proteomes:UP000008961};
RN   [1] {ECO:0000313|EMBL:CBL41751.1, ECO:0000313|Proteomes:UP000008961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41751.1,
RC   ECO:0000313|Proteomes:UP000008961};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SS3/4.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL41751.1, ECO:0000313|Proteomes:UP000008961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41751.1,
RC   ECO:0000313|Proteomes:UP000008961};
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; FP929062; CBL41751.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7GVA9; -.
DR   KEGG; bprs:CK3_21520; -.
DR   PATRIC; fig|245014.3.peg.691; -.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   BioCyc; BBAC245014:G1314-1858-MONOMER; -.
DR   Proteomes; UP000008961; Chromosome.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:GOC.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; 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:SF48; 23S RRNA (URACIL(747)-C(5))-METHYLTRANSFERASE RLMC; 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.
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        427
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        427
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         330
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         351
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         400
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   475 AA;  52959 MW;  F9F130DF0C8A9D5D CRC64;
     MEIKKNDKFT VTIEDMGEDG AGIGRVDGYI WFVKDALIGD TIEASAMKMK KNYGFARLVR
     VITPAKGRVE AKCPVARACG GCQLQELDYK EQLKFKEKKV YNHLKRIGGM ENLFLPEEAE
     QAEGVQDAVV MEPIIGMEDP WRYRNKAQYP IGRGKDGKPT AGFFAGRTHS LIPVPELDCL
     LGCLENKDYL AAVLKFMEDF GVEPYDEANH KGLVRHVLLR KGFASGEHMV CLVINGKKLP
     HEKEFIERLH ETGADSISLS FNMEKTNVIL GTEIKNLYGP GYITDKIGNI EYRISPLSFY
     QVNPVQTERL YGTALEFADL NGGETVWDLY CGIGTISSFL AQKAGKVCGV EIIPAAIEDA
     RENAKRNGLD NVEFFVGKAE EVLPEQYEKN HIKADVIVVD PPRKGCDELC LETIVKMAPE
     KVVYVSCDSS TLARDVKYFG ENGYAVKRVR TVDMFGMSGH VETVALLTKK CLHCN
//
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