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Database: UniProt
Entry: A0A0J8VKD0_9ENTR
LinkDB: A0A0J8VKD0_9ENTR
Original site: A0A0J8VKD0_9ENTR 
ID   A0A0J8VKD0_9ENTR        Unreviewed;       705 AA.
AC   A0A0J8VKD0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
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:KMV33606.1};
GN   ORFNames=ACH50_16785 {ECO:0000313|EMBL:KMV33606.1};
OS   Franconibacter pulveris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Franconibacter.
OX   NCBI_TaxID=435910 {ECO:0000313|EMBL:KMV33606.1, ECO:0000313|Proteomes:UP000037315};
RN   [1] {ECO:0000313|EMBL:KMV33606.1, ECO:0000313|Proteomes:UP000037315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ34 {ECO:0000313|EMBL:KMV33606.1,
RC   ECO:0000313|Proteomes:UP000037315};
RA   Pal S., Banerjee T.D., Roy A., Sar P., Kazy S.K.;
RT   "Genome sequencing of Cronobacter sp. strain DJ34 isolated from petroleum
RT   contaminated sludge of Duliajan Oil Fields, Assam, India.";
RL   Submitted (JUN-2015) 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:KMV33606.1}.
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DR   EMBL; LFEJ01000022; KMV33606.1; -; Genomic_DNA.
DR   RefSeq; WP_024560855.1; NZ_LFEJ01000022.1.
DR   AlphaFoldDB; A0A0J8VKD0; -.
DR   STRING; 1121863.GCA_000621185_00177; -.
DR   PATRIC; fig|1656095.3.peg.3141; -.
DR   OrthoDB; 9809404at2; -.
DR   Proteomes; UP000037315; 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; 2.
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;  79333 MW;  A824D99C5D4AAFB6 CRC64;
     MNSLFASTAR GLEELLKTEL ESLGAERCQV VQGGVHFEGD TTLLYQSLMW SRLASRILLP
     LGECKVYSDL DLYLGVQAID WTSLLAPDAT FAVHFSGLND TIRNSQYGAM KVKDAIVDAF
     TRKNLPRPTV DREAPDLRIN VWLNKETASI AIDLSGEGLH QRGYRDRTGQ APIKENLAAA
     IVMRSGWQPG TPLLDPMCGS GTLLIEAAMI ATDRAPGLHR TRWGFTGWSQ HDENTWKAVK
     TEAQVRARRG LSEYASRFYG SDNDPRVIER ARTNARRAGL ADLIAFSVQD VAQLKNPQPE
     GPHGAVISNP PYGERLESEP ALIALHSLLG RTMKSQFGGW KLSLFSASPE LLSCLQLRAD
     RQFKAKNGPL DCVQKNYQLA ETAAGAEPAQ LAEDYANRLR KNLKKLDKWA KQEGIECYRI
     YDADLPDYNV AVDRYADWVV IQEYAPPKTI DPAKARQRLF DVIAATISVL GLAPNKLVLK
     TRERQKGKNQ YQKMAEKGEF MEVREYNARL WVNLTDYLDT GLFLDHRIAR RMLGEMSKGK
     DFLNLFSYTG SASVHAGLGG ARSTTTVDMS RTYLEWAERN LRLNGLSGRA HRLIQADCLS
     WLREANEQFD LIFIDPPTFS NSKRMDEAFD VQRDHLQLMK DLKRMLRKGG TIMFSNNKRG
     FRMDHEGIAA LGLQAQEITQ KTQSQDFARN RHIHNCWLVT HAGKE
//
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