RNM5_CLOBH
ID RNM5_CLOBH Reviewed; 181 AA.
AC A5HXX7; A7G000;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Ribonuclease M5 {ECO:0000255|HAMAP-Rule:MF_01469};
DE EC=3.1.26.8 {ECO:0000255|HAMAP-Rule:MF_01469};
DE AltName: Full=RNase M5 {ECO:0000255|HAMAP-Rule:MF_01469};
DE AltName: Full=Ribosomal RNA terminal maturase M5 {ECO:0000255|HAMAP-Rule:MF_01469};
GN Name=rnmV {ECO:0000255|HAMAP-Rule:MF_01469};
GN OrderedLocusNames=CBO0080, CLC_0127;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- FUNCTION: Required for correct processing of both the 5' and 3' ends of
CC 5S rRNA precursor. Cleaves both sides of a double-stranded region
CC yielding mature 5S rRNA in one step. {ECO:0000255|HAMAP-Rule:MF_01469}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 21 and 42
CC nucleotides, respectively, from the 5'- and 3'-termini of a 5S-rRNA
CC precursor.; EC=3.1.26.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01469};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01469};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_01469};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01469}.
CC -!- SIMILARITY: Belongs to the ribonuclease M5 family. {ECO:0000255|HAMAP-
CC Rule:MF_01469}.
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DR EMBL; CP000727; ABS37483.1; -; Genomic_DNA.
DR EMBL; AM412317; CAL81636.1; -; Genomic_DNA.
DR RefSeq; WP_003356126.1; NC_009698.1.
DR RefSeq; YP_001252628.1; NC_009495.1.
DR RefSeq; YP_001386038.1; NC_009698.1.
DR AlphaFoldDB; A5HXX7; -.
DR SMR; A5HXX7; -.
DR GeneID; 5184335; -.
DR KEGG; cbh:CLC_0127; -.
DR KEGG; cbo:CBO0080; -.
DR PATRIC; fig|413999.7.peg.80; -.
DR HOGENOM; CLU_109405_0_0_9; -.
DR OMA; RLQMFQI; -.
DR PRO; PR:A5HXX7; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043822; F:ribonuclease M5 activity; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR CDD; cd01027; TOPRIM_RNase_M5_like; 1.
DR HAMAP; MF_01469; RNase_M5; 1.
DR InterPro; IPR004466; RNase_M5.
DR InterPro; IPR025156; RNase_M5_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034141; TOPRIM_RNase_M5-like.
DR Pfam; PF13331; DUF4093; 1.
DR Pfam; PF13662; Toprim_4; 1.
DR SMART; SM00493; TOPRIM; 1.
DR TIGRFAMs; TIGR00334; 5S_RNA_mat_M5; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing;
KW rRNA-binding.
FT CHAIN 1..181
FT /note="Ribonuclease M5"
FT /id="PRO_0000416745"
FT DOMAIN 3..86
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
SQ SEQUENCE 181 AA; 20470 MW; ECADB8FBEE22A560 CRC64;
MIKEVIVVEG RDDITAVKRA VDAEMIAVGG FGINSKVIKK IREAQKRQGV IVLTDPDYAG
EKIRKYICNR VKGVKHAYIS QEEGTKEDDI GVENAAPEAI IRALNLAKCE VKQERKEFDM
NDMIFFKLTA NEESKERREK LGMALGIGYC NTNQFIKRLN NFGITKEEFI KAIKDLDKGN
E
