ID A0A094L4X0_9GAMM Unreviewed; 711 AA.
AC A0A094L4X0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ORFNames=IDAT_01120 {ECO:0000313|EMBL:KFZ29733.1};
OS Pseudidiomarina atlantica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ29733.1, ECO:0000313|Proteomes:UP000053718};
RN [1] {ECO:0000313|EMBL:KFZ29733.1, ECO:0000313|Proteomes:UP000053718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ29733.1,
RC ECO:0000313|Proteomes:UP000053718};
RA Du J., Lai Q., Shao Z.;
RT "Draft genome sequence of Idiomarina sp. MCCC 1A10513.";
RL Submitted (JUN-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:KFZ29733.1}.
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DR EMBL; JPIN01000001; KFZ29733.1; -; Genomic_DNA.
DR RefSeq; WP_034729417.1; NZ_JPIN01000001.1.
DR AlphaFoldDB; A0A094L4X0; -.
DR STRING; 1517416.IDAT_01120; -.
DR eggNOG; COG0116; Bacteria.
DR eggNOG; COG1092; Bacteria.
DR OrthoDB; 9809404at2; -.
DR Proteomes; UP000053718; 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}; 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 46..158
FT /note="THUMP"
FT /evidence="ECO:0000259|PROSITE:PS51165"
SQ SEQUENCE 711 AA; 80733 MW; FFE655B274785427 CRC64;
MTAALQLFAT CAKGLEPLLF DELKQLGLSE VQQTIAGCRF QASLPEAYRV CLWSRLASRI
LLQLGQTEVG FKLESTTAAI AATPWHEHFT ANESFVVDFT GQNQQIRHTQ FGAQLVKDGV
VDHFRAQGLE RPSIDKAEPD IRIHAHLHHN ILTWYLDLSG DALHRRGYRL AQGAAPVRET
LAAAIAMRAG VDESTQLLVD PFCGSGTLLL EAAMIVLDHA PGLLRERWGF NAWLQHDDVT
WHALVAEAQQ RLTNAKAARS LKILGADNDP KVLAIADQNA QRLGFTDFCE WRAQDATQFT
LPEELAGQTG LLLCNPPYGE RLGEEVETLL LYRRFGQRLR TSFAGWQIAI LAGDESLLKR
LKLRSHKKYK LFNGALDVIL ALYDLNKEQI EFTKEQSSDL ANRLKKNYQK LEKWAAKEGV
SAWRVYDADL PEYNAAVDVY NDHLVIQEYA APKDIPPAVA KERLWFLLDT LAEVLPFTAA
NMHLKVRQKQ SGKSQYQRQQ LRNITTVVHE YEAQFLVNLS DYLDTGLFLD HRWARRQLAK
MSAGKNILNL FAYTCTASVH AALAGAKQVT SVDLSKTYLA WGEQNFQLNG LQPRQHPLVQ
ADCLQWLQEQ RPQQRFDVIF LDPPTFSNSK RMHDVLDIQR DHVMLLKLAA RLLKDDGVIL
FSNNKRKFKL DEEGLAEAFL RAENWTERSI STDFARHKGI HHLFKVTHWH D
//
