ID A0A2V3VXR9_9PROT Unreviewed; 731 AA.
AC A0A2V3VXR9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=C8R34_11370 {ECO:0000313|EMBL:PXW86797.1};
OS Nitrosomonas sp. Nm84.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=200124 {ECO:0000313|EMBL:PXW86797.1, ECO:0000313|Proteomes:UP000248024};
RN [1] {ECO:0000313|EMBL:PXW86797.1, ECO:0000313|Proteomes:UP000248024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm84 {ECO:0000313|EMBL:PXW86797.1,
RC ECO:0000313|Proteomes:UP000248024};
RA Wagner M.;
RT "Active sludge and wastewater microbial communities from Klosterneuburg,
RT Austria.";
RL Submitted (MAY-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}.
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:PXW86797.1}.
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DR EMBL; QJJP01000013; PXW86797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3VXR9; -.
DR Proteomes; UP000248024; 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.
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:UP000248024};
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 45..157
FT /note="THUMP"
FT /evidence="ECO:0000259|PROSITE:PS51165"
SQ SEQUENCE 731 AA; 82501 MW; 578AACEA80814DDB CRC64;
MTQYQLFATT PKAMEGILAN EIQALGGKNV QQKMAGVAFQ GDLAMAYTAC LWLRTASRVL
LLLSSFEVKS QQDLYDGIQC IDWSEHLNAD DSLAVSFSSK NNAAINNTHF GALKVKDAIV
DQMRAKFGSR PNVDTERPSI RVNVYLHNDT AQLSLDLSGE SSHKRGYREV SIAAPIKENL
AAAILLRAGW PEIAQQGGSL LDPMCGSGTL LVEGALIAGD IAPGLQRDYF GFLGWKQHDA
TRWQSVLDEA QQRREIGLNK LPAIVGFDQD RHTVTAALQH IENAGLQGKI HIERRDITDA
AAKESWHKGL IVCNPPYGER LGDEEQAALL YRQFGEVLKQ RFVGWQVAII IANPELGFKL
GIRSHKPITL FNGALECKLL RLTIEEKAFF EPKAKSQQER IEHISRRAQA GQLDNQAEMF
ANRLRKNLKK LTKWAKQNQV HCYRLYDADL PEYAVAVDVY QGEQTWVNVQ EYESPKTIDP
AKANQRLAGV MAEIPKVLEI PAEQVFLKIR RKQKSTDQYE KQGNSRHFHV VEESGCKFWV
NFEDYLDTGL FLDHRPLRLL IQQQARGKRF LNLFAYTGSA TVHAAIGGAA SSVTVDMSNT
YVDWARRNFV LNGIRDDHKL VRANCLQWLT EQASAKQKLQ FDLIFLDPPT FSNSKKMDEV
FDIQKDHVQL IRNAVTLLAR GGNLYFSTNF RRFKMDQAAL ADLIIEDISA AMIPEDFARD
AKIHYCWRIS R
//
