ID A0A0A3Z9F1_9GAMM Unreviewed; 705 AA.
AC A0A0A3Z9F1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 ECO:0000313|EMBL:KGT94271.1};
GN ORFNames=NG99_10195 {ECO:0000313|EMBL:KGT94271.1};
OS Erwinia typographi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=371042 {ECO:0000313|EMBL:KGT94271.1, ECO:0000313|Proteomes:UP000030351};
RN [1] {ECO:0000313|EMBL:KGT94271.1, ECO:0000313|Proteomes:UP000030351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M043b {ECO:0000313|EMBL:KGT94271.1,
RC ECO:0000313|Proteomes:UP000030351};
RA Chan K.-G., Tan W.-S.;
RT "Genome sequence of Erwinia typographi M043b.";
RL Submitted (OCT-2014) 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}.
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:KGT94271.1}.
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DR EMBL; JRUQ01000029; KGT94271.1; -; Genomic_DNA.
DR RefSeq; WP_034891965.1; NZ_JRUQ01000029.1.
DR AlphaFoldDB; A0A0A3Z9F1; -.
DR STRING; 371042.NG99_10195; -.
DR eggNOG; COG0116; Bacteria.
DR eggNOG; COG1092; Bacteria.
DR OrthoDB; 9809404at2; -.
DR Proteomes; UP000030351; Unassembled WGS sequence.
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; 2.
DR HAMAP; MF_01858; 23SrRNA_methyltr_KL; 1.
DR InterPro; IPR017244; 23SrRNA_methyltr_KL.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
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; PS00092; N6_MTASE; 1.
DR PROSITE; PS51165; THUMP; 1.
DR PROSITE; PS01261; UPF0020; 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};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00529}; 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 43..154
FT /note="THUMP"
FT /evidence="ECO:0000259|PROSITE:PS51165"
SQ SEQUENCE 705 AA; 79014 MW; 4F596B7B7640FA2B CRC64;
MNSLFASTAR GLEELLKSEL EAMGAQACQV VQGGVHYQGD DRLMYQSLMW SRLASRILLP
LTECGVYSDL DLYLGVQAID WPAMFGSDKT FAVHFSGLNE VIRNSQYGAL KVKDAIVDSF
TRKNLPRPDV DREQPDIRVN VWLNKDTASI ALDLSGAGLH QRGYRQQTGL APLKENLAAA
IVLRSGWQAG TPLVDPLCGS GTLLIEAAMI ASDRAPGLHR QHWGFTGWAK FDEALWREAI
AEAQVRAKRG LQETTSRFYG YDIDSRVIEL ARANARRAGL AGVISFGVQD VLKLTNPLPE
GPTGTVLSNP PYGERLESEP ALIALHSQLG RLMKSHFGGW NLSLFSASPE LLSCLQLRAD
RQFKAKNGPL DCVQKNYQLA VNSAAGAGGQ IAEDYANRLR KNLKKLEKWA RQEGLECYRL
YDADLPDYNV AVDRYGDWIV VQEYAPPKTI EPAKARQRLF DVITATLSVL DLPSDKLVLK
TRERQKGKSQ YQKLGEKGDF FEVSEFNAKM WVNLTDYLDT GLFLDHRIAR KMLGQMSKGK
DFLNLFAYTG SASVHAGLGG ARSTTTVDMS RTYLEWAERN LRLNGLTGRQ HRLMQADCLS
WLRESNEQFD LIFIDPPTFS NSRRMEESFD VQRDHLLLMK DLKRLLRKGG TMMFSNNKRG
FKMDHEGLAG LNLAAQDITA KTQSQDFARN RQIHNCWLIT HAGKE
//
