ID A0A2C9XT64_9ENTE Unreviewed; 456 AA.
AC A0A2C9XT64;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:OTP12604.1};
GN ORFNames=A5844_000837 {ECO:0000313|EMBL:OTP12604.1};
OS Enterococcus sp. 10A9_DIV0425.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1987383 {ECO:0000313|EMBL:OTP12604.1, ECO:0000313|Proteomes:UP000194933};
RN [1] {ECO:0000313|EMBL:OTP12604.1, ECO:0000313|Proteomes:UP000194933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10A9_DIV0425 {ECO:0000313|EMBL:OTP12604.1,
RC ECO:0000313|Proteomes:UP000194933};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 10A9_DIV0425.";
RL Submitted (MAY-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}.
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:OTP12604.1}.
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; NGMO01000001; OTP12604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9XT64; -.
DR STRING; 1987383.A5844_000837; -.
DR Proteomes; UP000194933; 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}; Reference proteome {ECO:0000313|Proteomes:UP000194933};
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 5..63
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 287
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 316
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 337
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 385
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 456 AA; 51858 MW; C531C05E289ED24B CRC64;
MKQQTVKKNE RYTVDIVDLS YEGLGVAKID GYPLFIENTL PGEQVEVLVV KAGTKFGYGK
VEKFLTTSPD RQDIESTVLL RTGIAPLAHL KYEQQLLFKQ KQVEQVLTKI AKMPDVPVLP
TIGMEDPVGY RNKAQIPVRR VDGELVTGFY KKNSHDLVEI TDFFIQDSKI DQAIIKVREI
LQRFQVRGYN EEKNEGQIRH IIVRRGHYSH EMMVVLVTRK EKFFKAKEIA EAIHEALPEV
VSVIQNINEE KTNVILGKQE KVLYGRSYIE DQLLGKTYRI SSKSFYQVNT AQTEVLYQKA
IDFAELKKDD VLIDAYSGIG TIGLSLADQV AKVYGMEMIP EAIEDAQFNA LTNKIENVHY
EVGKAETVMK KWQDKGVKPT VVMVDPPRKG LDASFIDSTI EMKPERIVYI SCNPATFARD
AKLFAEGGYR LQKVQPVDLF PQTHHIECVG LLTRNK
//
