ID C7NRM8_HALUD Unreviewed; 256 AA.
AC C7NRM8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000256|HAMAP-Rule:MF_01547};
DE EC=2.1.1.166 {ECO:0000256|HAMAP-Rule:MF_01547};
DE AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547};
DE AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547};
GN Name=rlmE {ECO:0000256|HAMAP-Rule:MF_01547};
GN OrderedLocusNames=Huta_1792 {ECO:0000313|EMBL:ACV11964.1};
OS Halorhabdus utahensis (strain DSM 12940 / JCM 11049 / AX-2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=519442 {ECO:0000313|EMBL:ACV11964.1, ECO:0000313|Proteomes:UP000002071};
RN [1] {ECO:0000313|EMBL:ACV11964.1, ECO:0000313|Proteomes:UP000002071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12940 / JCM 11049 / AX-2
RC {ECO:0000313|Proteomes:UP000002071};
RX PubMed=21304660; DOI=10.4056/sigs.31864;
RA Anderson I., Tindall B.J., Pomrenke H., Goker M., Lapidus A., Nolan M.,
RA Copeland A., Glavina Del Rio T., Chen F., Tice H., Cheng J.F., Lucas S.,
RA Chertkov O., Bruce D., Brettin T., Detter J.C., Han C., Goodwin L.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Pitluck S., Pati A.,
RA Mavromatis K., Ivanova N., Ovchinnikova G., Chen A., Palaniappan K.,
RA Chain P., Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Halorhabdus utahensis type strain (AX-2).";
RL Stand. Genomic Sci. 1:218-225(2009).
CC -!- FUNCTION: Specifically methylates the uridine in position 2552 of 23S
CC rRNA at the 2'-O position of the ribose in the fully assembled 50S
CC ribosomal subunit. {ECO:0000256|HAMAP-Rule:MF_01547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-
CC methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42720, Rhea:RHEA-COMP:10202, Rhea:RHEA-COMP:10203,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.166;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01547};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01547}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. {ECO:0000256|HAMAP-
CC Rule:MF_01547}.
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; CP001687; ACV11964.1; -; Genomic_DNA.
DR RefSeq; WP_015789536.1; NC_013158.1.
DR AlphaFoldDB; C7NRM8; -.
DR STRING; 519442.Huta_1792; -.
DR GeneID; 8384079; -.
DR KEGG; hut:Huta_1792; -.
DR eggNOG; arCOG00079; Archaea.
DR eggNOG; arCOG01641; Archaea.
DR HOGENOM; CLU_009422_4_4_2; -.
DR OrthoDB; 26307at2157; -.
DR Proteomes; UP000002071; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002792; TRAM_dom.
DR PANTHER; PTHR10920:SF13; PRE-RRNA 2'-O-RIBOSE RNA METHYLTRANSFERASE FTSJ3; 1.
DR PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF01938; TRAM; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01547};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01547}; Reference proteome {ECO:0000313|Proteomes:UP000002071};
KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_01547};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01547};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01547}.
FT DOMAIN 198..256
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 48
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 68
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
SQ SEQUENCE 256 AA; 27941 MW; 41B3F4214E2DFC85 CRC64;
MSGKDKYYNR AKQQGYRARS AFKLRQLDET ADLLGAERTV VDLGAAPGGW LQVAAERLGD
GGRVVGVDRQ RIDDLEEPDV PVETIRGDIT DESTVEAITD AVGEANLVLS DMAPNVTGEY
DLDHARSVHL ARQAFEVSLD VLGAGGDLVV KVFDGRDLDD LKTDIEEEFE YVREVRPDAS
RDSSSELYLV AKHRLTAPVR EGDTVEVEIV DTGEEGDGIA KVEGFTLFVA GVEEGETVTV
RVDDLKPQYG FAQPVE
//
