ID A0A167UPI9_9BACI Unreviewed; 187 AA.
AC A0A167UPI9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=AS29_004565 {ECO:0000313|EMBL:KZZ86515.1};
OS Bacillus sp. SJS.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423321 {ECO:0000313|EMBL:KZZ86515.1, ECO:0000313|Proteomes:UP000028527};
RN [1] {ECO:0000313|EMBL:KZZ86515.1, ECO:0000313|Proteomes:UP000028527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJS {ECO:0000313|EMBL:KZZ86515.1,
RC ECO:0000313|Proteomes:UP000028527};
RA Newman J.D., Stropko S.J., Pipes S.E.;
RT "Bacillus sp. SJS genome.";
RL Submitted (APR-2016) 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:KZZ86515.1}.
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DR EMBL; JAQV02000001; KZZ86515.1; -; Genomic_DNA.
DR RefSeq; WP_035412578.1; NZ_JAQV02000001.1.
DR AlphaFoldDB; A0A167UPI9; -.
DR STRING; 1423321.AS29_004565; -.
DR eggNOG; COG1658; Bacteria.
DR OrthoDB; 9791329at2; -.
DR Proteomes; UP000028527; 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; PF13662; Toprim_4; 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:UP000028527};
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 4..90
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 187 AA; 20804 MW; 2C8D182BF831B2E6 CRC64;
MKIKEIIVVE GRDDTVAIKR AVTADTIETN GSAIGEDVIE RVKLAAAGRG VIIFTDPDFP
GEKIRKTVAE AVPGCKHAFI EKSDARPKKG RGIGVEHASP DAIRAALSEV KEEMPDLPSE
WTQDDLLDYG LIGHPMAKER RQKLGTELKI GYTNGKQLLK RLQMFQIPKS DYENAMNRIL
QEEEKHD
//
