ID D4S8G9_9FIRM Unreviewed; 465 AA.
AC D4S8G9;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:EFF65463.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:EFF65463.1};
GN Name=rumA {ECO:0000313|EMBL:EFF65463.1};
GN ORFNames=HMPREF7545_1834 {ECO:0000313|EMBL:EFF65463.1};
OS Selenomonas noxia ATCC 43541.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=585503 {ECO:0000313|EMBL:EFF65463.1, ECO:0000313|Proteomes:UP000003701};
RN [1] {ECO:0000313|EMBL:EFF65463.1, ECO:0000313|Proteomes:UP000003701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43541 {ECO:0000313|EMBL:EFF65463.1,
RC ECO:0000313|Proteomes:UP000003701};
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 (JAN-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:EFF65463.1}.
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DR EMBL; ACKT01000040; EFF65463.1; -; Genomic_DNA.
DR RefSeq; WP_006694204.1; NZ_GG749279.1.
DR AlphaFoldDB; D4S8G9; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_7_0_9; -.
DR InParanoid; D4S8G9; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000003701; 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};
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 14..72
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 420
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 420
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 295
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 345
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 393
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 465 AA; 52350 MW; BD242D1C778DA5E0 CRC64;
MKQKEKTKRT AMIPVRKGQI YNIPIDRLGT SGEGVGRYEN FTIFVPNALP GENVCIIIEE
VKKNYARGRV KEVLQASPKR IPPHCEIYAD CGGCQLQHLS YEAQLDAKRA QVAEALTHIG
KLSQIPVKET MRAEEPWNYR NKMQFPIGIN KGKILVGCFA QGSHNIIDTK NCHIQHTANN
DLANAMRDIV EHLHIPVYNE DTHKGVMRHI IGRVGRNNDL MAVIVTATKH LPRAKDVVRM
LRERLPNLVS IHQNIQTYHN NVIMGRDTQL LWGRPTIIDS LGRLNFHISP RSFFQVNTRQ
AERLYEQALA YADLHGTETV IDAYCGTGTI TLFLAQRARK VYGIEIVQPA ILDARKNARD
NHVKNAEFIV GDATAVMPAL YKQGIRPDVV VIDPPRAGCN ETVLCTFANM RPQRIIYVSC
NPATLARDLA ILKELGYITQ EVQPVDLFPQ TSHVENVALI TKKSI
//
