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Database: UniProt
Entry: E4LB44_9FIRM
LinkDB: E4LB44_9FIRM
Original site: E4LB44_9FIRM 
ID   E4LB44_9FIRM            Unreviewed;       494 AA.
AC   E4LB44;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:EFR61098.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:EFR61098.1};
GN   Name=rumA {ECO:0000313|EMBL:EFR61098.1};
GN   ORFNames=HMPREF9199_0682 {ECO:0000313|EMBL:EFR61098.1};
OS   Veillonella sp. oral taxon 158 str. F0412.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=879309 {ECO:0000313|EMBL:EFR61098.1, ECO:0000313|Proteomes:UP000003565};
RN   [1] {ECO:0000313|EMBL:EFR61098.1, ECO:0000313|Proteomes:UP000003565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0412 {ECO:0000313|EMBL:EFR61098.1,
RC   ECO:0000313|Proteomes:UP000003565};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (NOV-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}.
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:EFR61098.1}.
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DR   EMBL; AENU01000003; EFR61098.1; -; Genomic_DNA.
DR   RefSeq; WP_009372064.1; NZ_AENU01000003.1.
DR   AlphaFoldDB; E4LB44; -.
DR   STRING; 879309.HMPREF9199_0682; -.
DR   eggNOG; COG2265; Bacteria.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000003565; 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: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; 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; 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          44..102
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        449
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         324
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         353
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         374
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         422
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   494 AA;  54513 MW;  786264407456AA0A CRC64;
     MNGTGRTSRK HKSKQQNRRG ARSNQGQITS GTVSKKQQAI LNAPVKVGDE VLVTIHGIGS
     SGEGVGRVDD FTVFVPFALP EETVKVAIDM VKKTYATGRL LEIVTMAPNR IDASCDLYGF
     CGGCQLQHIT YEGQLSLKTQ KVKDVIERIG HQNPDLVKPA LGPKEPWAYR NKMQMPVGGT
     KGDIQMGFYA MGSHDIVQGT NCPIQDEGNN IIAQACYQIA KEFDIEPYDE HTGNGILRHV
     IGRIGQSGWM IILVTATDHL PHQEKWVEKL TERIPQVETI VHNVNGKRTN VILGPKNNIL
     YGDGTITDHI KDLRFTLSPH SFFQVNPEQT TVLYDQALAY ADLKGDETVI DAYCGTGTIS
     LFLAHKAKHV IGIEIVEPAI INARENAKCN GYDNTEFIVA DAAVEMPKLY KAGVRADVIV
     FDPIRAGCKE EVLTSAAGME PKRIVYVSCN PATMARDIEI LTHYGYELKE VQPVDMFPMT
     AHVETVCLLS RKDK
//
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