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Database: UniProt
Entry: A0A1I0NDL9_9GAMM
LinkDB: A0A1I0NDL9_9GAMM
Original site: A0A1I0NDL9_9GAMM 
ID   A0A1I0NDL9_9GAMM        Unreviewed;       714 AA.
AC   A0A1I0NDL9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=SAMN04515660_1590 {ECO:0000313|EMBL:SEV99178.1};
OS   Luteibacter sp. 329MFSha.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1798239 {ECO:0000313|EMBL:SEV99178.1, ECO:0000313|Proteomes:UP000199162};
RN   [1] {ECO:0000313|EMBL:SEV99178.1, ECO:0000313|Proteomes:UP000199162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=329MFSha {ECO:0000313|EMBL:SEV99178.1,
RC   ECO:0000313|Proteomes:UP000199162};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOJE01000001; SEV99178.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0NDL9; -.
DR   STRING; 1798239.SAMN04515660_1590; -.
DR   Proteomes; UP000199162; 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; 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          43..154
FT                   /note="THUMP"
FT                   /evidence="ECO:0000259|PROSITE:PS51165"
SQ   SEQUENCE   714 AA;  79747 MW;  4771136688494F7F CRC64;
     MSAFFATCPK GLEYLLKDEL VALGATDVRE ALAGVSFAGT IETAYRACLW SRMASRVLLP
     LAEFDAADPD ALYAGVQSID WSEHLAAHGT LAVDANTAQS KLTHSQFIAL KTKDAIVDQF
     RAASGARPDV DPEEPDLRVN VRLRRDRATL SIDLSGSPLH RRGWREQQGE APLKENLAAA
     MLVRAQWPRI YAEGGALVDP MCGSGTLLIE GALMAAGVAP GLRRDYFGFL GWLKHDYALW
     RTIYDEAKAR ADEGLRGLRP VFFGSDADPH MVQTAKRNAQ SAGVAGFVHL DKRDAVHVAP
     PPDTPLGLVI TNPPYGERLG DRAELPVLYR DLGQALKDRF AGWRAAVLAG DEELGRALRL
     SPDKRYALYN GALETPLLTF ALRARDEAPR EAKPLSDGAQ MLKNRLEKNV RHLRKRLARE
     GITCWRAYDQ DLPEYAAAID VYEEWLHIQE YKAPQDVPVD VARIRMREIV RVAGEVFGIP
     RDRIAVKTRE RGKGGSKYGQ FDQKGEFIEV HEGGLSFLIN PTDYLDTGLF LDHRLVRAKI
     RELAAGKHFL NLFAYTGTAS VYAAAGDARD TTTVDLSGTY LDWASRNLAL NGFTGNRHRL
     VQEDSLTFLE KRSMQYGLIY VDPPTFSNSK KADDFDVQRD HVKLLMLCAD RLLPDGVIVF
     SNNFRRFQLD RAALEPHFSI EDWSAPSIPF DFARRHDIHG CWLLRKPFVN PWKT
//
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