ID A0A1R4G0W9_9ACTO Unreviewed; 472 AA.
AC A0A1R4G0W9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:SJM61771.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:SJM61771.1};
GN ORFNames=CZ771_12995 {ECO:0000313|EMBL:SJM61771.1};
OS Actinomycetales bacterium JB111.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales.
OX NCBI_TaxID=1434822 {ECO:0000313|EMBL:SJM61771.1, ECO:0000313|Proteomes:UP000196124};
RN [1] {ECO:0000313|EMBL:SJM61771.1, ECO:0000313|Proteomes:UP000196124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB111 {ECO:0000313|EMBL:SJM61771.1,
RC ECO:0000313|Proteomes:UP000196124};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUHX01000077; SJM61771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4G0W9; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000196124; 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 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; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 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; 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:UP000196124};
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 REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 429
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 277
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 354
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 402
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 472 AA; 48307 MW; C5D1FE21806E387C CRC64;
MPERTPGRGN RARRGRRPGP GGGSRRNRPA EMTPEPVDAP VTVGAPAHGG FTVARVGDVV
TFVRHAAPGE SVRLAVTAKR SKVWFADAVE VLDPSADRVP HVWPEAGPGG IGGAELGHLR
PAAQRDWKSD VLAESLRRIG GERIAADAEA AAGSLRVLPV GPGTEGGTRT RIDLTVTADG
RPGMHRYRSD VVLPVTALPL ADPRLPVEEI LALDSLRPGA RLRAVVGSGP SPDGVARLLV
DGRAVPGSPV TSGRVAERVE TMFGPLDHAL DDAGFWQVHT SAPAALVESV LALAAGIDPD
PAALAGEGGD PDRAGRVTAS LAGSAVVELY SGAGLLTKAI GEAVGQGGAV LSLEGDVDAV
RSAADAIDHA SVRTLAGAVT GRSVAALGEE DDWRPGGVVV LDPPRSGARD EVVSAVAALA
PRRIVHVACD PAALARDLAS AAEAGYVVER IVALDLFPHT HHLEVVAALV PA
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