ID E0PEJ8_STREI Unreviewed; 456 AA.
AC E0PEJ8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:EFM27175.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:EFM27175.1};
GN Name=rumA {ECO:0000313|EMBL:EFM27175.1};
GN ORFNames=HMPREF9319_1310 {ECO:0000313|EMBL:EFM27175.1};
OS Streptococcus equinus ATCC 700338.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=864569 {ECO:0000313|EMBL:EFM27175.1, ECO:0000313|Proteomes:UP000004290};
RN [1] {ECO:0000313|EMBL:EFM27175.1, ECO:0000313|Proteomes:UP000004290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700338 {ECO:0000313|EMBL:EFM27175.1,
RC ECO:0000313|Proteomes:UP000004290};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-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:EFM27175.1}.
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DR EMBL; AEEL01000016; EFM27175.1; -; Genomic_DNA.
DR RefSeq; WP_003065521.1; NZ_GL397128.1.
DR AlphaFoldDB; E0PEJ8; -.
DR GeneID; 64019153; -.
DR HOGENOM; CLU_014689_7_0_9; -.
DR Proteomes; UP000004290; 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; 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 1..59
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 408
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 408
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 312
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 333
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 381
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 456 AA; 51469 MW; 5A524888E1B205DD CRC64;
MLSKNAIVDA EITDLSHEGA GVAKVDGFVF FVENALPGEK IKMRVLKVKK NIGFGKVEEY
VTISEHRNQD LNVDYLRTGI ADFGHLAYAE QLKFKRKQVM DNLYKTAGIS DVEVSETLGM
AHPYAYRNKA QVPVRRVNGQ LETGFFRKHS HDLMPISDYY IQNKEIDRLI NFTRDLLRRF
DLKPYDEKEQ TGLIRNLVVR RGHYSGEMML VFVTTRPKIF RIEQIIEKIV AEFPAVKSIV
QNINDKNTNA IFGKEFKTLY GKDTIVDSML GNQYEISARS FYQVNTEMAE KLYQTAIDFS
DLTPKDIVID AYSGIGTIGL SFAKNVKAVY GVEVIEEAVE DAKRNAALNS ITNAHYIADP
AEHAMATWSK DGIKPSVILV DPPRKGLTEN FIKASVAMQP EKITYISCNP ATMARDIKLY
QELGYKLIKV QPVDLFPNTH HVEAVSLLVR VGGTAK
//
