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Database: UniProt
Entry: F7V0X9_EEGSY
LinkDB: F7V0X9_EEGSY
Original site: F7V0X9_EEGSY 
ID   F7V0X9_EEGSY            Unreviewed;       767 AA.
AC   F7V0X9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase K/L {ECO:0000256|HAMAP-Rule:MF_01858};
DE   Includes:
DE     RecName: Full=23S rRNA m2G2445 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01858};
DE              EC=2.1.1.173 {ECO:0000256|HAMAP-Rule:MF_01858};
DE     AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmL {ECO:0000256|HAMAP-Rule:MF_01858};
DE   Includes:
DE     RecName: Full=23S rRNA m7G2069 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01858};
DE              EC=2.1.1.264 {ECO:0000256|HAMAP-Rule:MF_01858};
DE     AltName: Full=rRNA (guanine-N(7)-)-methyltransferase RlmK {ECO:0000256|HAMAP-Rule:MF_01858};
GN   Name=rlmL {ECO:0000256|HAMAP-Rule:MF_01858};
GN   OrderedLocusNames=EGYY_12590 {ECO:0000313|EMBL:BAK44422.1};
OS   Eggerthella sp. (strain YY7918).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Eggerthella.
OX   NCBI_TaxID=502558 {ECO:0000313|EMBL:BAK44422.1, ECO:0000313|Proteomes:UP000008929};
RN   [1] {ECO:0000313|EMBL:BAK44422.1, ECO:0000313|Proteomes:UP000008929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YY7918 {ECO:0000313|EMBL:BAK44422.1,
RC   ECO:0000313|Proteomes:UP000008929};
RX   PubMed=21914883;
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete Genomic Sequence of the Equol-Producing Bacterium Eggerthella sp.
RT   Strain YY7918, Isolated from Adult Human Intestine.";
RL   J. Bacteriol. 193:5570-5571(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YY7918 {ECO:0000313|Proteomes:UP000008929};
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete genome sequence of the equol-producing bacterium Eggerthella sp.
RT   strain YY7918 isolated from adult human intestine.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the guanine in position 2445
CC       (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01858}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2069) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(2069) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43772, Rhea:RHEA-COMP:10688, Rhea:RHEA-COMP:10689,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.264;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01858};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2445) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(2445) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42740, Rhea:RHEA-COMP:10215, Rhea:RHEA-COMP:10216,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.173;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01858};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01858}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmKL family.
CC       {ECO:0000256|HAMAP-Rule:MF_01858}.
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DR   EMBL; AP012211; BAK44422.1; -; Genomic_DNA.
DR   RefSeq; WP_013979672.1; NC_015738.1.
DR   AlphaFoldDB; F7V0X9; -.
DR   STRING; 502558.EGYY_12590; -.
DR   KEGG; eyy:EGYY_12590; -.
DR   eggNOG; COG0116; Bacteria.
DR   eggNOG; COG1092; Bacteria.
DR   HOGENOM; CLU_014042_2_0_11; -.
DR   OrthoDB; 9809404at2; -.
DR   Proteomes; UP000008929; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052915; F:23S rRNA (guanine(2445)-N(2))-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd11715; THUMP_AdoMetMT; 1.
DR   Gene3D; 3.30.2130.30; -; 1.
DR   Gene3D; 3.30.750.80; RNA methyltransferase domain (HRMD) like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 3.
DR   HAMAP; MF_01858; 23SrRNA_methyltr_KL; 1.
DR   InterPro; IPR017244; 23SrRNA_methyltr_KL.
DR   InterPro; IPR000241; RlmKL-like_Mtase.
DR   InterPro; IPR019614; SAM-dep_methyl-trfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR004114; THUMP_dom.
DR   PANTHER; PTHR47313; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE K/L; 1.
DR   PANTHER; PTHR47313:SF1; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE K_L; 1.
DR   Pfam; PF10672; Methyltrans_SAM; 1.
DR   Pfam; PF02926; THUMP; 1.
DR   Pfam; PF01170; UPF0020; 1.
DR   PIRSF; PIRSF037618; RNA_Mtase_bacteria_prd; 1.
DR   SMART; SM00981; THUMP; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   PROSITE; PS51165; THUMP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01858};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01858}; Reference proteome {ECO:0000313|Proteomes:UP000008929};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00529};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01858};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01858};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01858}.
FT   DOMAIN          47..158
FT                   /note="THUMP"
FT                   /evidence="ECO:0000259|PROSITE:PS51165"
SQ   SEQUENCE   767 AA;  83320 MW;  DA78EF37BA5A6E7B CRC64;
     MENKNLELFA SCLAGLEAPL AEELKRLGIK RVRPLGGGVA FYGDVRQALS ACLWSRLASR
     ILVVVGRVDA RDAQSLYQGV RALRWEDVIV AGASIALRAH GMNNELRNTK FTALKVKDAV
     CDQLLETRGV RPDVDTATPD ALIDVRVHEG KATVSLDLAG ESLYRRSYLS DDDTQDASLS
     CALAAGVLAL ADWRDRFAGG AALVDPACGD GMLVVEAASM ACDQAPGLVR DHWGFFGWAL
     SEPEVFNELI SEADERFERG LLRVVGEEAL EPAASTPPDI ARVRIAGAST SSPAIARARM
     HAKRAGLRQV VSVEQADAQS VGELVERVSS VAEQAAPDGT PRCVVACELP GAERMQSEAR
     AQAEAAAFIA AASSAPAASL FAVAGEKGIE ARFGVEPVVR TEIGRERLAT EVLVFDEAPR
     GTVTVVVPDS AGGAEHRVDV LESSSEQFAA RLRKVAKERR KWARREGVSC YRVYDADLPD
     YAVAIDVYPG AGEASGNLYL HIAEYAAPSS IDPGKAQRRY DDVLALAPVV LGVRPDHVFS
     KVRRRDKGGG QYREARRRSY VTQVQEDGYI FEVDLAGYLD TGLFLDHRLT RELVGAKAKG
     KRFLNLFAYT GTASVHAAGG GAQSTTTVDL SQTYLDWAAR NMAANGFAGD THTFERGDTM
     AWITEARRAG RRFDLVFVDP PTFSNSKAMG KRTWDVQRDH VELLIGVSRL LSEEGEVIFS
     CNLRTFKPDE EALAKYGVVL EDITAQTIPH DFERNPRIHK CYLARRS
//
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