ID A0A379C7L1_9PAST Unreviewed; 715 AA.
AC A0A379C7L1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:SUB58201.1};
GN ORFNames=NCTC12872_00151 {ECO:0000313|EMBL:SUB58201.1};
OS Phocoenobacter uteri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Phocoenobacter.
OX NCBI_TaxID=146806 {ECO:0000313|EMBL:SUB58201.1, ECO:0000313|Proteomes:UP000255417};
RN [1] {ECO:0000313|EMBL:SUB58201.1, ECO:0000313|Proteomes:UP000255417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12872 {ECO:0000313|EMBL:SUB58201.1,
RC ECO:0000313|Proteomes:UP000255417};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UGTA01000001; SUB58201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A379C7L1; -.
DR OrthoDB; 9809404at2; -.
DR Proteomes; UP000255417; 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.
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:UP000255417};
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 46..157
FT /note="THUMP"
FT /evidence="ECO:0000259|PROSITE:PS51165"
SQ SEQUENCE 715 AA; 81276 MW; EF0C17AC96CBFDAC CRC64;
MTKQTTYFAT TARGFEEMLK TELTQMGIEQ CKIAQGGVHF TTDQKGVYTA LLYSRLASRI
LLPLTQAKVF DDIDLYSAVV GYAWEDLFDE RDTIFIDFNG TNDAIRHSQF GAMRVKDGIV
DHFERAGFNR PSVDKDQADI RIHAYLNREE LILSLDLSGD ALHLRNYRTD TGKAPLRETL
AAAIVLRSGW QKGTPLVDPM CGAGTLLIEA AQMALNIPAQ INRLHWGFDS WKGHQPAVWQ
AVVSEAKNAI LSSDEIQFYG FDLDRRVIEK AKQNAENAGV GDVIQFKHGD VAALKNPVEN
KKGTLICNPP YGERLGTTPE LIALYTVFGQ RLKQHFAGWN ASIFSSEADL LNCLRLRSHR
QFKAKNGPLD CIQKNYLLSD RKREESEITQ LKFDADAQLA PDFANRLKKN IKKIDKWAKQ
QGLDCYRLYD ADLPEYNLAV DRYGDHIVVQ EYAAPKTIDE QKARQRLLDA VAATLSVTGI
ETNKLVLKVR QKQKGTNQYE KLANKGEYFH VTEYGAKLWV NLTDYLDTGL FLDHRLTRRM
VGEMAKGKTF LNLFAYTGSA TVHAALHGAK ATTTVDMSNT YLNWAEQNLD LNDFDLRNHR
LIQADCLQWL SECRERFEVI FVDPPTFSNS KRMEDSWDVQ RDHLELFTKL KRILTKDGTI
IFSNNKRNFK MNIDGLTELG LVAENITEKT IPLDFERNKH IHNCWIVKNS ESVSG
//
