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RNM5_ENTFA
ID   RNM5_ENTFA              Reviewed;         190 AA.
AC   Q837A8;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=EF_0935;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AE016830; AAO80743.1; -; Genomic_DNA.
DR   RefSeq; NP_814673.1; NC_004668.1.
DR   RefSeq; WP_011109470.1; NZ_KE136527.1.
DR   AlphaFoldDB; Q837A8; -.
DR   SMR; Q837A8; -.
DR   STRING; 226185.EF_0935; -.
DR   EnsemblBacteria; AAO80743; AAO80743; EF_0935.
DR   KEGG; efa:EF0935; -.
DR   PATRIC; fig|226185.9.peg.870; -.
DR   eggNOG; COG1658; Bacteria.
DR   HOGENOM; CLU_109405_0_0_9; -.
DR   OMA; RLQMFQI; -.
DR   Proteomes; UP000001415; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
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; PF01751; Toprim; 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..190
FT                   /note="Ribonuclease M5"
FT                   /id="PRO_0000416746"
FT   DOMAIN          4..87
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT   BINDING         10
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         56
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         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT   BINDING         58
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
SQ   SEQUENCE   190 AA;  21221 MW;  EC3C6555C85091E5 CRC64;
     MKVAEIIVVE GKDDTRRIQE VVAADTIETI GSAINDEILT QIEHAQETRG VIIFTDPDYS
     GEKIRKTIME VVPDAKHAFL SRKVAVPKKN GGSLGVEHAS DEAIIEALKK VVTPVQADED
     YQEIPRQTLV EYGLIAGANA KKYRELLGDD LRIGYTNSKQ LVKRLSMFRI TEAELKESMT
     RILKELANEE
 
 
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