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Database: UniProt
Entry: A0A1R4H5P0_9GAMM
LinkDB: A0A1R4H5P0_9GAMM
Original site: A0A1R4H5P0_9GAMM 
ID   A0A1R4H5P0_9GAMM        Unreviewed;       745 AA.
AC   A0A1R4H5P0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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   ECO:0000313|EMBL:SJM91499.1};
GN   ORFNames=CRENPOLYSF1_190118 {ECO:0000313|EMBL:SJM91499.1};
OS   Crenothrix polyspora.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Crenotrichaceae; Crenothrix.
OX   NCBI_TaxID=360316 {ECO:0000313|EMBL:SJM91499.1, ECO:0000313|Proteomes:UP000195667};
RN   [1] {ECO:0000313|EMBL:SJM91499.1, ECO:0000313|Proteomes:UP000195667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSM_CP1 {ECO:0000313|EMBL:SJM91499.1};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUKI01000092; SJM91499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4H5P0; -.
DR   OrthoDB; 9809404at2; -.
DR   Proteomes; UP000195667; 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}; Reference proteome {ECO:0000313|Proteomes:UP000195667};
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          47..159
FT                   /note="THUMP"
FT                   /evidence="ECO:0000259|PROSITE:PS51165"
SQ   SEQUENCE   745 AA;  84324 MW;  DE37A7FB31045339 CRC64;
     MPTPTYELFA STPKAMEDIL AEELKSLGVT HTKTTVAGVA FQGDLETAYR TCLWSRTANR
     ILLILSTFSV TSQDDLYNGI AKINWFEHLE PTGTFAVTFN VKNSEVINNS HFGALKVKDA
     IVDQMRKKFE IRPSIDTERP SIRINVHLHG EKAQLSLDLS GESLHRRGYR DISISAPIKE
     NLAAAMLLRS GWPAIAKQGG TLLDPMCGSG TLLLEGAMMA ADFAPGLLRD YFGFLGWKKH
     DATCWEKLIG EAEQRKWVGM AKKMPVIVGF DQDRQTVHAA LGHINNARLH NKIHIERRDI
     SDAKPAEAWQ PGLVICNPPY GERLGDEQET AELYTHFGET LKTQFIGWKA ALIISNPELG
     FRLGIRSQKP ITLYNGALEC RLLRLNIEEK AFFTPKAQTQ EERIALVTAA VNAPEPDQEG
     AKVSAEMFAN RLKKNLKKWR QWAKQNQIRC YRVYDADLPE YAVAVDVYEA EQTWINVQEY
     EPPKSIDQHK ADQRLAGVMA EIPGVFGVSR DHVFLKIRRR QRKTDQYEKF SELGRFHTVE
     EGGCKLRVNF EDYLDTGLFL DHRPIRMLIQ QQAQGKRFLN LFAYTGSATV HAALGGAKQT
     TTIDMSNTYI NWAKANMALN NQVDENQHQY IQADCLEWLE TEARQAYKKR FDLIFLDPPT
     FSNSKRMEDA FDIQENHVAL INNALALLAV GGMLYFSTNF RRFKFDHAAF SAFTVTDISA
     ATVPADFTRN SKIHYCWSIK NDATS
//
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