RLMKL_ALLVD
ID RLMKL_ALLVD Reviewed; 735 AA.
AC Q1W3E0; D3RVT1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase K/L {ECO:0000255|HAMAP-Rule:MF_01858};
DE Includes:
DE RecName: Full=23S rRNA m2G2445 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01858};
DE EC=2.1.1.173 {ECO:0000255|HAMAP-Rule:MF_01858};
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmL {ECO:0000255|HAMAP-Rule:MF_01858};
DE Includes:
DE RecName: Full=23S rRNA m7G2069 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01858};
DE EC=2.1.1.264 {ECO:0000255|HAMAP-Rule:MF_01858};
DE AltName: Full=rRNA (guanine-N(7)-)-methyltransferase RlmK {ECO:0000255|HAMAP-Rule:MF_01858};
GN Name=rlmL {ECO:0000255|HAMAP-Rule:MF_01858}; OrderedLocusNames=Alvin_2173;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16995898; DOI=10.1111/j.1365-2958.2006.05408.x;
RA Hensen D., Sperling D., Trueper H.G., Brune D.C., Dahl C.;
RT "Thiosulphate oxidation in the phototrophic sulphur bacterium
RT Allochromatium vinosum.";
RL Mol. Microbiol. 62:794-810(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
CC -!- FUNCTION: Specifically methylates the guanine in position 2445
CC (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
CC {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01858};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01858}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmKL family.
CC {ECO:0000255|HAMAP-Rule:MF_01858}.
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DR EMBL; DQ441405; ABE01365.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC63094.1; -; Genomic_DNA.
DR RefSeq; WP_012971366.1; NC_013851.1.
DR AlphaFoldDB; Q1W3E0; -.
DR SMR; Q1W3E0; -.
DR STRING; 572477.Alvin_2173; -.
DR EnsemblBacteria; ADC63094; ADC63094; Alvin_2173.
DR KEGG; alv:Alvin_2173; -.
DR eggNOG; COG0116; Bacteria.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_2_0_6; -.
DR OMA; WIRGYEA; -.
DR OrthoDB; 307177at2; -.
DR Proteomes; UP000001441; Chromosome.
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-KW.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 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; RNA_methylase_dom.
DR InterPro; IPR019614; SAM-dep_methyl-trfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004114; THUMP_dom.
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; SSF53335; 2.
DR PROSITE; PS51165; THUMP; 1.
DR PROSITE; PS01261; UPF0020; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..735
FT /note="Ribosomal RNA large subunit methyltransferase K/L"
FT /id="PRO_0000366729"
FT DOMAIN 45..156
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ SEQUENCE 735 AA; 82627 MW; FF10C9FDC9052A93 CRC64;
MSDHIFFASA PKHLGSLLAE ELTRLGMAGA AETRGGARFS GRIEDGYRAC LWSRIANRIL
LPLAQVSLGG PDEIHDSALE IPWEDHLTPD RTFAIQFDGQ LQGVTNPHFA ILQVKDAIAD
RFNRLYGRRP SVDPDDPDLR IHLYGNRDSL SFSLDLSGES LHQRGYRDAG SAAPLKENLA
AALLLRAGWP EIAAEGGALL DPMCGSGTLI IEGALIAADI APGLLRERFG FHGWTQHDEP
AWQRLLAEAR LRRTAGLKRL GSLRGYDVNP NAIRTSLHHL ERAGLAGLAH FERRELSDCH
PGREDDEGLV IVNPPYGERL GADEDLTQLY ARLGSVLKER FVGWRAAVFT SSPELGKSLG
LRATRIHSLY NGPIECRLLS FQIEPRYFVS HLPRPLPPEE RSPGAAMFAN RLSKNLKALR
KWRQRDGIDC LRIYDADLPE YALAIDLYEG ERRWVHVQEY AAPPSVDPKR ARQRLREALG
LIPEVLEVPG EQVFLKVRRQ QKGRAQYERL AETGRFHEVS EYGLRFLVNF EDYLDTGLFL
DHRDVRRLIG SLSDGKRFLN LFAYTGTATV HAAKGGAAST TTVDLSRTYL EWAGRNLELN
GIRGPNHQLI QADCLRWIDS MAGQRRFDLI FLDPPSFSTS KRMHGTLDIQ RDHVDIIQAT
MRLLEPGGRL IFSNNLRRFR IDLEGLAPFE VSDISAQTLP RDFARNPRIH NCWVIQHPES
ASNRRNGSDD EDRHA
