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Database: UniProt
Entry: A0A0U3MYF5_9LACT
LinkDB: A0A0U3MYF5_9LACT
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ID   A0A0U3MYF5_9LACT        Unreviewed;       188 AA.
AC   A0A0U3MYF5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=NY10_1845 {ECO:0000313|EMBL:ALV22439.1};
OS   Carnobacterium sp. CP1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV22439.1, ECO:0000313|Proteomes:UP000064734};
RN   [1] {ECO:0000313|EMBL:ALV22439.1, ECO:0000313|Proteomes:UP000064734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP1 {ECO:0000313|EMBL:ALV22439.1,
RC   ECO:0000313|Proteomes:UP000064734};
RA   Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT   "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT   Amanda bay, East Antarctic.";
RL   Submitted (FEB-2015) 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}.
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DR   EMBL; CP010796; ALV22439.1; -; Genomic_DNA.
DR   RefSeq; WP_058919652.1; NZ_CP010796.1.
DR   AlphaFoldDB; A0A0U3MYF5; -.
DR   STRING; 1564681.NY10_1845; -.
DR   KEGG; carc:NY10_1845; -.
DR   PATRIC; fig|1564681.3.peg.1850; -.
DR   OrthoDB; 9791329at2; -.
DR   Proteomes; UP000064734; 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   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:UP000064734};
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          5..88
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   188 AA;  20935 MW;  D2421CF1B2C816D6 CRC64;
     MEKVKEIIVV EGRDDTRRIH ESLEADTIET NGSAINEETL QLIAKAQATR GVIVFTDPDF
     PGEKIRKTIS RAVPGVKHAF LTIDEAKPKG SGSLGIEHAS PEAIRAALAK SYTETLEQES
     LISRELLIDA GLIMGAFAKK RREKLGERLN IGYTNGKQLQ KRLQMFQISP EEVIQAMQQI
     LEEEHDKS
//
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