ID A0A1Y5ES63_9GAMM Unreviewed; 735 AA.
AC A0A1Y5ES63;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=A9Q82_03075 {ECO:0000313|EMBL:OUR83675.1};
OS Cycloclasticus sp. 46_120_T64.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=1856281 {ECO:0000313|EMBL:OUR83675.1, ECO:0000313|Proteomes:UP000195872};
RN [1] {ECO:0000313|Proteomes:UP000195872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hu P., Dubinsky E.A., Probst A.J., Wang J., Sieber C.M.K., Tom L.M.,
RA Gardinali P., Banfield J.F., Atlas R.M., Andersen G.L.;
RT "Simulation of Deepwater Horizon oil plume reveals substrate specialization
RT within a complex community of hydrocarbon-degraders.";
RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2017).
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:OUR83675.1}.
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DR EMBL; MAAM01000004; OUR83675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5ES63; -.
DR Proteomes; UP000195872; 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; 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; 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}; 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 735 AA; 83501 MW; 8AC01380B517DB17 CRC64;
MSEITTYFAS TAKGMELILA DELRALKADK VKDALGGVYF DGDMEMALRV CLWSRLANRV
LMPLAKYGAQ TPEQLYAGAM KIDWSQHFDV DKTFAIDASI RRSKINHSRY AEQVIKDAIV
DQFKERIDQR PDVQRDQPDI RINAYIHNDK VTLSLDLSGD SLHRRCYRAE SVEAPLKENL
AAAILIRAGW PTIAAAGGAL YDPMCGSGTL LTEAAMMAGD IAPGLLREYY GFLGWAQFSP
PIWQRLRKEA EYRRDQGIDN IPPIMGSDIS IKNAGIAKAN IKAANLLWQV KAVSLPLSKV
VPDEAWKPGL FIVNPPYGER LGDIKNLQPL YQEIGTILKA RFNGWQASVF TGNTDLAFNV
SLKSHKSYQL YNGAIACKVF NFSVEPERHF EGQQAGQQQV IGDNLKKSLL ASQGDWSEGA
TMLANRLRKN IKKLKPWVKN NAVSCYRVYD ADLPEYAIAI DLYQGEKTWL HVQEYEAPKS
IDEKKSIQRL RDALAVLPEV FAIPQQQVSL KIRRRQKGST QYEKQGTEGG FHQIKEGKAE
FLVNFRDYLD TGLFLDHRPI RQSIYQQANG KQFLNLFAYT GTASVHAILG GATTSTTVDM
SKTYLDWAQK NFELNEIKSD KHQLVRANCM EWLDTAISEQ KKYELIFIDP PTFSNSKRME
NVFDIQRDYI ELIHKSAELL TKKGLIIFST NFRKFKFDET QFPKLAVQDI SKQTLPKDFE
RNPRIHYCWN ISFNN
//
