ID C2KMF6_LEUMC Unreviewed; 498 AA.
AC C2KMF6;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:EEJ41576.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:EEJ41576.1};
GN Name=rumA {ECO:0000313|EMBL:EEJ41576.1};
GN ORFNames=HMPREF0555_1822 {ECO:0000313|EMBL:EEJ41576.1};
OS Leuconostoc mesenteroides subsp. cremoris ATCC 19254.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=586220 {ECO:0000313|EMBL:EEJ41576.1, ECO:0000313|Proteomes:UP000004283};
RN [1] {ECO:0000313|EMBL:EEJ41576.1, ECO:0000313|Proteomes:UP000004283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19254 {ECO:0000313|EMBL:EEJ41576.1,
RC ECO:0000313|Proteomes:UP000004283};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2009) 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:EEJ41576.1}.
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DR EMBL; ACKV01000120; EEJ41576.1; -; Genomic_DNA.
DR AlphaFoldDB; C2KMF6; -.
DR HOGENOM; CLU_014689_7_1_9; -.
DR Proteomes; UP000004283; 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; 2.40.50.1070; -; 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:SF45; -; 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 45..103
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 454
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 454
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 329
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 358
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 379
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 427
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 498 AA; 56074 MW; 375438DA31B5D7F1 CRC64;
MNMTEQNKRP YQKSRNNNGK KPYYGKNFDP RKSGAPRGIT SEGVNVRVGQ NFPITIKRLG
INGEGIGYFK RKIVFVPGAL PDEVAVVKVT EVEPKYIAAK VLKIREKSPD RVKLLDEFAD
SVGGFELEHM NYPAQLRFKK DVLVQSLEKF QPKGWSNYDI RDTIGMDHPY EYRNKAQFPV
RKIGDKLSVG MYKRGSHDLV DLPVVHTQTP DTMKVMRTVR ELLDKLSVSI YNEDKNRGTV
KTIVARVSQT TSEVQLTFIT NTDGFPGDTA LIEAINQALP EVTGIFQNYN PGRTSLVWGE
ETLKLWGKDY IEEKVLGKTF QLSPRAFMQL NHTQMSVVYN QALAALDLTH ADKLVDAYAG
VGTIGLSLAD KAGEVRGMEI IPEAVDDANQ NATLNHISNA HYEVGTAEKL FPKWQSEGWI
ADALVVDPPR TGLDTALRRE ILRTQPEKFV YISCNASTLA RDLVDLSKAY KVDYIQSIDM
FPQTARWEGV VKLTKRQK
//
