位置:首页 > 蛋白库 > RLMC_VIBC3
RLMC_VIBC3
ID   RLMC_VIBC3              Reviewed;         375 AA.
AC   A5F0U5; C3M6M2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=23S rRNA (uracil(747)-C(5))-methyltransferase RlmC {ECO:0000255|HAMAP-Rule:MF_01012};
DE            EC=2.1.1.189 {ECO:0000255|HAMAP-Rule:MF_01012};
DE   AltName: Full=23S rRNA(m5U747)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01012};
GN   Name=rlmC {ECO:0000255|HAMAP-Rule:MF_01012}; Synonyms=rumB;
GN   OrderedLocusNames=VC0395_0309, VC395_A0954;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
CC   -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 747
CC       (m5U747) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-
CC         methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42628, Rhea:RHEA-COMP:10154, Rhea:RHEA-COMP:10155,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.189;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01012};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. RlmC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01012}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000626; ABQ18716.1; -; Genomic_DNA.
DR   EMBL; CP001236; ACP11785.1; -; Genomic_DNA.
DR   RefSeq; WP_001149825.1; NZ_JAACZH010000003.1.
DR   AlphaFoldDB; A5F0U5; -.
DR   SMR; A5F0U5; -.
DR   STRING; 345073.VC395_A0954; -.
DR   EnsemblBacteria; ABQ18716; ABQ18716; VC0395_0309.
DR   GeneID; 57742296; -.
DR   KEGG; vco:VC0395_0309; -.
DR   KEGG; vcr:VC395_A0954; -.
DR   PATRIC; fig|345073.21.peg.3681; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_0_0_6; -.
DR   OMA; YCGVGGF; -.
DR   Proteomes; UP000000249; Chromosome 1.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01012; 23SrRNA_methyltr_RlmC; 1.
DR   InterPro; IPR011825; 23SrRNA_MeTrfase_RlmC.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02085; meth_trns_rumB; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..375
FT                   /note="23S rRNA (uracil(747)-C(5))-methyltransferase RlmC"
FT                   /id="PRO_1000072919"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         3
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         11
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         14
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         87
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         212
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         241
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         262
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         307
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
SQ   SEQUENCE   375 AA;  41981 MW;  BA5072091D5C1E4A CRC64;
     MQCEFFIQKR CTSCHQCAQP YSQQVENKDQ QLRELIAPAM DVQWLPPVTS ADTAFRNKAK
     MVVLGAAHAP ILGIEDAQGQ PLSLVTCPLY PQPMQELLAY LENWIRIAGI PPYNKLKKKG
     ELKFILLTRS ENSGQFMLRF VARSHAVLER IERNLPTLIA AFPTIEVVSV NIQPVHMARL
     EGEEEIFLTE TQSLLEQFND VPMVIRPKSF FQTNPQVAEQ LYATARAWVR EIAPTQMWDL
     FCGVGGFALH CAAPNTAVTG IEIEPEAIAS AQRSAQMMGI DNLSFAALDS AKFSQSQMSA
     PELVLVNPPR RGLGSELTAQ LEALAPQHIL YSSCNPQTMV KDIAELASYQ MSRVQWFDMF
     PHTDHAEVLT LLVRK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024