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Database: UniProt
Entry: A0A328SEH3_9EURY
LinkDB: A0A328SEH3_9EURY
Original site: A0A328SEH3_9EURY 
ID   A0A328SEH3_9EURY        Unreviewed;       209 AA.
AC   A0A328SEH3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   ORFNames=BZ136_02875 {ECO:0000313|EMBL:RAP49758.1};
OS   Methanosphaera sp. rholeuAM74.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=1945579 {ECO:0000313|EMBL:RAP49758.1, ECO:0000313|Proteomes:UP000248971};
RN   [1] {ECO:0000313|EMBL:RAP49758.1, ECO:0000313|Proteomes:UP000248971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RholeuAM74 {ECO:0000313|EMBL:RAP49758.1};
RA   Hoedt E.C., Parks D.H., Rosewarne C.P., Denman S.E., Mcsweeney C.S.,
RA   O Cuiv P., Hugenholtz P., Tyson G.W., Morrison M.;
RT   "Culture- and metagenomics-based expansion of the genus Methanosphaera
RT   reveals their evolutionary depth and metabolic versatility.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:RAP49758.1}.
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DR   EMBL; MUZZ01000076; RAP49758.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328SEH3; -.
DR   Proteomes; UP000248971; Unassembled WGS sequence.
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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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   PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:UP000248971};
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          22..201
FT                   /note="Ribosomal RNA methyltransferase FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01547,
FT                   ECO:0000256|PIRSR:PIRSR005461-1"
FT   BINDING         54
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT   BINDING         56
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT   BINDING         94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT   BINDING         118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
SQ   SEQUENCE   209 AA;  23687 MW;  FF1390BEB106ACC2 CRC64;
     MSRWKAKHDK EHYYKLAKKE NYRSRASFKL KQLNKKYKII KPDHKVVDLG AAPGGWSQVV
     TEIIGEEGCG QVVSVDLEYI KPIDHEAFLA IKGDFTTQEV QNTIVEAIDG RADVVLSDAS
     PKLCGIKDID NFRTYDLASS VLDITDNILK NDGDLIMKAF QGEAYQKLIS DLKKKFRNVK
     TTKPNSSRKR SSEMYIIARG FKAKKIKNS
//
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