ID A0A0D6Z4K7_9BACI Unreviewed; 134 AA.
AC A0A0D6Z4K7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Mini-ribonuclease 3 {ECO:0000256|HAMAP-Rule:MF_01468};
DE Short=Mini-3 {ECO:0000256|HAMAP-Rule:MF_01468};
DE Short=Mini-RNase 3 {ECO:0000256|HAMAP-Rule:MF_01468};
DE EC=3.1.26.- {ECO:0000256|HAMAP-Rule:MF_01468};
DE AltName: Full=Mini-RNase III {ECO:0000256|HAMAP-Rule:MF_01468};
DE Short=Mini-III {ECO:0000256|HAMAP-Rule:MF_01468};
GN Name=mrnC {ECO:0000256|HAMAP-Rule:MF_01468};
GN ORFNames=UB32_18800 {ECO:0000313|EMBL:KIY20512.1};
OS Mesobacillus subterraneus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=285983 {ECO:0000313|EMBL:KIY20512.1, ECO:0000313|Proteomes:UP000032512};
RN [1] {ECO:0000313|EMBL:KIY20512.1, ECO:0000313|Proteomes:UP000032512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MITOT1 {ECO:0000313|EMBL:KIY20512.1,
RC ECO:0000313|Proteomes:UP000032512};
RA Peet K.C., Thompson J.R.;
RT "Draft genome sequences of the supercritical CO2 tolerant bacteria Bacillus
RT subterraneus MITOT1 and Bacillus cereus MIT0214.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in correct processing of both the 5' and 3' ends of
CC 23S rRNA precursor. Processes 30S rRNA precursor transcript even in
CC absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller
CC rRNA precursors. {ECO:0000256|HAMAP-Rule:MF_01468}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01468};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01468}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01468}.
CC -!- SIMILARITY: Belongs to the MrnC RNase family. {ECO:0000256|HAMAP-
CC Rule:MF_01468}.
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:KIY20512.1}.
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DR EMBL; JXIQ01000202; KIY20512.1; -; Genomic_DNA.
DR RefSeq; WP_044396697.1; NZ_JXIQ01000202.1.
DR AlphaFoldDB; A0A0D6Z4K7; -.
DR PATRIC; fig|285983.3.peg.3338; -.
DR OrthoDB; 46571at2; -.
DR Proteomes; UP000032512; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd00593; RIBOc; 1.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 1.
DR HAMAP; MF_01468; RNase_Mini_III; 1.
DR InterPro; IPR008226; Mini3_fam.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR34276; MINI-RIBONUCLEASE 3; 1.
DR PANTHER; PTHR34276:SF1; MINI-RIBONUCLEASE 3; 1.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR PIRSF; PIRSF005520; UCP005520; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01468};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01468};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01468};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01468};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01468};
KW Reference proteome {ECO:0000313|Proteomes:UP000032512};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01468};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01468};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01468}; rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01468}.
FT DOMAIN 1..134
FT /note="RNase III"
FT /evidence="ECO:0000259|SMART:SM00535"
FT ACT_SITE 23
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01468"
SQ SEQUENCE 134 AA; 15188 MW; 7A1160DE1872E204 CRC64;
MLHYEKTVDE KQLNSLALAY MGDAVYELYV RHHLLHSGKV RPNQLHKEAT AFVSAKAQAK
YLHKLMDMDE LSEEEMAIVR RGRNAKSGSV PKNTDVQTYR YSTAFEALIG SLHLAGNERR
IEELIAKVFA IAAE
//