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RNM5_FUSNN
ID   RNM5_FUSNN              Reviewed;         183 AA.
AC   Q8RH71;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=FN0039;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL94252.1; -; Genomic_DNA.
DR   RefSeq; NP_602953.1; NC_003454.1.
DR   AlphaFoldDB; Q8RH71; -.
DR   SMR; Q8RH71; -.
DR   STRING; 190304.FN0039; -.
DR   EnsemblBacteria; AAL94252; AAL94252; FN0039.
DR   KEGG; fnu:FN0039; -.
DR   PATRIC; fig|190304.8.peg.632; -.
DR   eggNOG; COG1658; Bacteria.
DR   HOGENOM; CLU_109405_0_0_0; -.
DR   InParanoid; Q8RH71; -.
DR   OMA; RLQMFQI; -.
DR   BioCyc; FNUC190304:G1FZS-652-MON; -.
DR   Proteomes; UP000002521; 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; 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..183
FT                   /note="Ribonuclease M5"
FT                   /id="PRO_0000416747"
FT   DOMAIN          6..90
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT   BINDING         12
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         59
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         59
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT   BINDING         61
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
SQ   SEQUENCE   183 AA;  20454 MW;  E5ADE0A5EC70D6A3 CRC64;
     MKKKIKEVIV VEGKDDISAV KNAVDAEVFQ VNGHAVRKNK SIEILKLAYE NKGLIILTDP
     DYAGEEIRKY LCKHFPNAKN AYISRVSGTK DGDIGVENAS PEDIITALEK ARFSLDNSVN
     IFNLDLMMDY NLIGKDNSAD LRSLLGAELG IGYSNGKQFM AKLNRYGISL EEFKKAYEKI
     NMK
 
 
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