UniProt: A0A378BLV7

Database: UniProt
Entry: A0A378BLV7_KLEPO

LinkDB:  A0A378BLV7_KLEPO 
Original site:  A0A378BLV7_KLEPO

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (16)   

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ID   A0A378BLV7_KLEPO        Unreviewed;       400 AA.
AC   A0A378BLV7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
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:STV46293.1};
GN   Synonyms=rlmI {ECO:0000256|HAMAP-Rule:MF_01857};
GN   ORFNames=NCTC5050_05294 {ECO:0000313|EMBL:STV46293.1};
OS   Klebsiella pneumoniae subsp. ozaenae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=574 {ECO:0000313|EMBL:STV46293.1, ECO:0000313|Proteomes:UP000255382};
RN   [1] {ECO:0000313|EMBL:STV46293.1, ECO:0000313|Proteomes:UP000255382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC5050 {ECO:0000313|EMBL:STV46293.1,
RC   ECO:0000313|Proteomes:UP000255382};
RG   Pathogen Informatics;
RA   Doyle S.;
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}.
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DR   EMBL; UGLZ01000005; STV46293.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A378BLV7; -.
DR   Proteomes; UP000255382; 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}; Reference proteome {ECO:0000313|Proteomes:UP000255382};
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;  44687 MW;  9E9228969B1BD77F CRC64;
     MTDSLFPRLV LAKGREKSLL RRHPWIFSGG VARMEGKARS GETIDIVDHQ GKWLARGAYS
     PSSQIRARVW TFDRNEAIDS AFFERRLQQV QTWRAWLAER DGLDSYRLIA GESDGLPGVT
     IDRFGNFFVL QLLSAGAEYQ RAAIISALQN LFPDCAIYDR SDVAVRKKEG LELAQGPVVG
     ELPPALLPIT EHGMKLLVDI QGGHKTGYYL DQRDSRLATR RYVADKRVLN CFSYTGGFAV
     SALMGGCRQV TSVDTSQEAL DVARQNVEIN GLDLSKAEFV RDDVFKLLRK YRDQGEKFDV
     IVMDPPKFVE NKSQLMGACR GYKDINMLAI QLLNPGGVLL TFSCSGLMTT DLFQKIIADA
     AIDAGRDVQF IEQFRQAADH PVIATYPEGL YLKGFACRVM
//

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