ID T0D2U0_ALIAG Unreviewed; 136 AA.
AC T0D2U0; A0A9E6ZFS1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=K1I37_01580 {ECO:0000313|EMBL:UNO49275.1};
OS Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132
OS / NCIMB 13137 / GD3B).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1356854 {ECO:0000313|EMBL:UNO49275.1, ECO:0000313|Proteomes:UP000829401};
RN [1] {ECO:0000313|Proteomes:UP000829401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3922 {ECO:0000313|Proteomes:UP000829401};
RX PubMed=36240455; DOI=10.1093/g3journal/jkac225;
RA Leonardo I.C., Barreto Crespo M.T., Gaspar F.B.;
RT "Unveiling the complete genome sequence of Alicyclobacillus acidoterrestris
RT DSM 3922T, a taint-producing strain.";
RL G3 (Bethesda) 12:0-0(2022).
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}.
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DR EMBL; CP080467; UNO49275.1; -; Genomic_DNA.
DR RefSeq; WP_021296596.1; NZ_AURB01000132.1.
DR STRING; 1356854.N007_07660; -.
DR KEGG; aaco:K1I37_01580; -.
DR Proteomes; UP000829401; Chromosome.
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 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 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:UP000829401};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01468};
KW RNA-binding {ECO:0000256|HAMAP-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 ACT_SITE 20
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01468"
SQ SEQUENCE 136 AA; 15068 MW; 3FF5CBCF24C61D1E CRC64;
MKQVFTVAEL SPLGLAFIGD AIWEVYARQH CLNQGIRKPH ELHKRCTRYV SATAQAKALA
GIATDLSEDE ADVVRRGRNA KSAHARKNVD VIVYRHSTGF EALIGHLHGT GQQARLEDII
QRALAYLDEL AKESHG
//
