ID B6GBJ0_9ACTN Unreviewed; 437 AA.
AC B6GBJ0;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:EEA90343.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:EEA90343.1};
GN Name=rumA {ECO:0000313|EMBL:EEA90343.1};
GN ORFNames=COLSTE_01449 {ECO:0000313|EMBL:EEA90343.1};
OS Collinsella stercoris DSM 13279.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=445975 {ECO:0000313|EMBL:EEA90343.1, ECO:0000313|Proteomes:UP000003560};
RN [1] {ECO:0000313|EMBL:EEA90343.1, ECO:0000313|Proteomes:UP000003560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90343.1,
RC ECO:0000313|Proteomes:UP000003560};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Collinsella stercoris (DSM 13279).";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEA90343.1, ECO:0000313|Proteomes:UP000003560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90343.1,
RC ECO:0000313|Proteomes:UP000003560};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) 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:EEA90343.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABXJ01000077; EEA90343.1; -; Genomic_DNA.
DR AlphaFoldDB; B6GBJ0; -.
DR STRING; 445975.COLSTE_01449; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_8_1_11; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000003560; 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; 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; 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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000003560};
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..53
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 437 AA; 47527 MW; 886E7DAF2EA3CE5E CRC64;
MRLTIETMTY GPDGLARTPE GKAVFVAGGL IGDTVEARIC EDGPSFSRAV VEEVLEPSPD
HVQPPCPFIG ICGGCPWGGL SHEAQLQAKE ENLRSALARI GKFSPKEVDD LMRPIRHAKD
AWGYRNKIEL APVHENGKFR LGMHGRDASQ IIKVDACPLF EKKHAKAVKA VAGALGFLGN
SRDLQLERVA IRSSRRTGAL EVALWTPTGA FPRAQVSRVL GDAVRATSVV RVMSKGEKRA
RRVSGVEALA GEGSWTEKIG DETMRLSAPS FFQVNTRAAE ILIDLVMEAL DPQPHELGID
LYCGAGTFTL PLARRCEFVS AVESYGPAVR DLRRNLDIAN ITNVDVIGGD AVREFPDEDA
DVLVVDPPRA GLAPEAIDLI ASTSARDVAY VSCDPATLAR DLRRFVEEGT FRPVWATPVD
LFPQTFHCET VVRLTRA
//
