ID A0A2X2E2P0_RAOPL Unreviewed; 400 AA.
AC A0A2X2E2P0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase I {ECO:0000256|HAMAP-Rule:MF_01857};
DE EC=2.1.1.191 {ECO:0000256|HAMAP-Rule:MF_01857};
DE AltName: Full=23S rRNA m5C1962 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01857};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RlmI {ECO:0000256|HAMAP-Rule:MF_01857};
GN Name=yccW {ECO:0000313|EMBL:SBM36444.1};
GN Synonyms=rlmI {ECO:0000256|HAMAP-Rule:MF_01857};
GN ORFNames=DN603_08925 {ECO:0000313|EMBL:RWT23774.1}, SAMEA2273876_03915
GN {ECO:0000313|EMBL:SBM36444.1};
OS Raoultella planticola (Klebsiella planticola).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX NCBI_TaxID=575 {ECO:0000313|EMBL:RWT23774.1, ECO:0000313|Proteomes:UP000288843};
RN [1] {ECO:0000313|EMBL:SBM36444.1, ECO:0000313|Proteomes:UP000078124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2880STDY5682802 {ECO:0000313|EMBL:SBM36444.1,
RC ECO:0000313|Proteomes:UP000078124};
RG Pathogen Informatics;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RWT23774.1, ECO:0000313|Proteomes:UP000288843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GEO_47_Down_B {ECO:0000313|EMBL:RWT23774.1,
RC ECO:0000313|Proteomes:UP000288843};
RA Mathys D.A., Mollenkopf D.F., Feicht S.M., Adams R.J., Albers A.L.,
RA Stuever D.M., Daniels J.B., Wittum T.E.;
RT "Carbapenemase-producing Enterobacteriaceae present in wastewater treatment
RT plant effluent and nearby surface waters in the US.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the cytosine at position 1962
CC (m5C1962) of 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_01857}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1962) in 23S rRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(1962) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42912, Rhea:RHEA-COMP:10382, Rhea:RHEA-COMP:10386,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.191;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01857};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01857}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI family.
CC {ECO:0000256|ARBA:ARBA00038091, ECO:0000256|HAMAP-Rule:MF_01857}.
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:RWT23774.1}.
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DR EMBL; QKOX01000007; RWT23774.1; -; Genomic_DNA.
DR EMBL; FLAC01000017; SBM36444.1; -; Genomic_DNA.
DR RefSeq; WP_032688490.1; NZ_VKNI01000005.1.
DR AlphaFoldDB; A0A2X2E2P0; -.
DR GeneID; 72406079; -.
DR KEGG; rpln:B1209_17760; -.
DR Proteomes; UP000078124; Unassembled WGS sequence.
DR Proteomes; UP000288843; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd21153; PUA_RlmI; 1.
DR CDD; cd11572; RlmI_M_like; 1.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR Gene3D; 3.30.750.80; RNA methyltransferase domain (HRMD) like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01857; 23SrRNA_methyltr_I; 1.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR023542; RLMI.
DR InterPro; IPR041532; RlmI-like_PUA.
DR InterPro; IPR019614; SAM-dep_methyl-trfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42873:SF1; METHYLTRANS_SAM DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42873; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE; 1.
DR Pfam; PF10672; Methyltrans_SAM; 1.
DR Pfam; PF17785; PUA_3; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01857};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01857};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01857};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01857};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01857};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01857}.
FT DOMAIN 7..92
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 400 AA; 44807 MW; 18ACCB88525051E8 CRC64;
MTDSIFPRLV LTKGREKSLL RRHPWIFSGA VARMEGKARS GETIDIVDSQ GKWLARGAYS
PSSQIRARVW SFDRNEAIDN AFFERRLQQA QTWREWLAAR DGLDSYRLIA GESDGLPGVT
IDRFGNFFVL QLLSAGAEYQ RAAIISALQT LFPDCSIYDR SDVAVRKKEG LELAQGPVVG
ELPPALLPIT EHGMQLLVDI QGGHKTGYYL DQRDSRLATR RYVTDKRVLN CFSYTGGFAV
SALMGGCRQV ISVDTSQEAL DVAKQNVELN KLDLSRAEFV RDDVFKLLRK YRDQGEKFDV
IVMDPPKFVE NKNQLMGACR GYKDINMLAI QLLNPGGILL TFSCSGLMAT DLFQKIIADA
AIDAGRDVQF IEQFRQAADH PVIATYPEGL YLKGFACRIM
//
