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Database: UniProt
Entry: R6AE28_9FIRM
LinkDB: R6AE28_9FIRM
Original site: R6AE28_9FIRM 
ID   R6AE28_9FIRM            Unreviewed;       182 AA.
AC   R6AE28;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Ribonuclease M5 {ECO:0000256|HAMAP-Rule:MF_01469};
DE            EC=3.1.26.8 {ECO:0000256|HAMAP-Rule:MF_01469};
DE   AltName: Full=RNase M5 {ECO:0000256|HAMAP-Rule:MF_01469};
DE   AltName: Full=Ribosomal RNA terminal maturase M5 {ECO:0000256|HAMAP-Rule:MF_01469};
GN   Name=rnmV {ECO:0000256|HAMAP-Rule:MF_01469};
GN   ORFNames=BN678_00707 {ECO:0000313|EMBL:CDA47004.1};
OS   Dialister sp. CAG:486.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Dialister; environmental samples.
OX   NCBI_TaxID=1262870 {ECO:0000313|EMBL:CDA47004.1, ECO:0000313|Proteomes:UP000017985};
RN   [1] {ECO:0000313|EMBL:CDA47004.1, ECO:0000313|Proteomes:UP000017985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:486 {ECO:0000313|Proteomes:UP000017985};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01469};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01469}.
CC   -!- SIMILARITY: Belongs to the ribonuclease M5 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01469}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDA47004.1}.
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DR   EMBL; CBBY010000025; CDA47004.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6AE28; -.
DR   STRING; 1262870.BN678_00707; -.
DR   Proteomes; UP000017985; Unassembled WGS sequence.
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   Gene3D; 3.40.1360.10; -; 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   NCBIfam; TIGR00334; 5S_RNA_mat_M5; 1.
DR   PANTHER; PTHR39156; RIBONUCLEASE M5; 1.
DR   PANTHER; PTHR39156:SF1; RIBONUCLEASE M5; 1.
DR   Pfam; PF13331; DUF4093; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF110455; Toprim domain; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01469};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_01469};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01469};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01469};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017985};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW   Rule:MF_01469};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01469};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_01469};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01469}.
FT   DOMAIN          3..88
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   182 AA;  20273 MW;  7EA611F0EEEF2C92 CRC64;
     MIRQVIVVEG KSDIARVSHA VEADMIATEG FGIRRETLEQ IRLAYEKRGI IILTDPDGPG
     ERIRQRLTRL FPKALHAFVP KSEASTENDV GIEDASPESI RKALSCLRVQ YQEDSEEFSM
     GDIFAAGLTG RPDSSEKRAR VGALLGIGYG NGKQFLKRLN HFGIIRSEWE KALEACQKEP
     TC
//
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