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Database: UniProt
Entry: U2V9M1_9ACTN
LinkDB: U2V9M1_9ACTN
Original site: U2V9M1_9ACTN 
ID   U2V9M1_9ACTN            Unreviewed;       438 AA.
AC   U2V9M1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:ERL12027.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:ERL12027.1};
GN   Name=rumA_2 {ECO:0000313|EMBL:ERL12027.1};
GN   ORFNames=HMPREF1248_0733 {ECO:0000313|EMBL:ERL12027.1};
OS   Coriobacteriaceae bacterium BV3Ac1.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae.
OX   NCBI_TaxID=1111135 {ECO:0000313|EMBL:ERL12027.1, ECO:0000313|Proteomes:UP000016652};
RN   [1] {ECO:0000313|EMBL:ERL12027.1, ECO:0000313|Proteomes:UP000016652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BV3AC1 {ECO:0000313|Proteomes:UP000016652};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (SEP-2013) 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:ERL12027.1}.
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DR   EMBL; AWUP01000011; ERL12027.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2V9M1; -.
DR   PATRIC; fig|1111135.3.peg.978; -.
DR   eggNOG; COG2265; Bacteria.
DR   Proteomes; UP000016652; 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:UP000016652};
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..54
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        393
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        393
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         273
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
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         323
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"
SQ   SEQUENCE   438 AA;  47235 MW;  98310345A4BD0353 CRC64;
     MLTLQIERMA YGADAIAHTP EGKTIFVSGA VPGDTAEVEV IQDGSNFSKG RVTHIVESSK
     KRVAPPCPYA TICGGCPWGV LSKEAQLEAK RSSVVDALVR IGHFETAKAE SLVADCERPS
     ADWGYRNKVE LAVSWQKGRL VVGMHAKDGS VIKVDSCPLL QDKHAKLVKA VSGALGYLGG
     TNELGLERVG IRVALHTKDI EIALWGKPGA FPRAQAAKVL GDATHANSMV RILTKGLKKA
     RRITGVEVLS GKGYWTERIA GQRMALSAPS FFQVNTLGAE RLIELVLAGL DPQPDEEAMD
     LYCGAGTFTL PLAKRCEFVS AVEASGPAVR DLRRNLDNAQ LQNVDVIGGD AGREFPDSDA
     NLIVVDPPRA GLAENVVTQL SEQRVRRIAY VSCDPATLAR DLARFCAIGN YRPLRITPVD
     LFPQTYHVEC VVLMSRAD
//
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