ID W4EFQ1_9BACL Unreviewed; 145 AA.
AC W4EFQ1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=C173_02022 {ECO:0000313|EMBL:ETT79054.1};
OS Paenibacillus sp. FSL R7-277.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT79054.1, ECO:0000313|Proteomes:UP000019051};
RN [1] {ECO:0000313|EMBL:ETT79054.1, ECO:0000313|Proteomes:UP000019051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT79054.1,
RC ECO:0000313|Proteomes:UP000019051};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT79054.1}.
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DR EMBL; ASPX01000004; ETT79054.1; -; Genomic_DNA.
DR RefSeq; WP_036721873.1; NZ_ASPX01000004.1.
DR AlphaFoldDB; W4EFQ1; -.
DR PATRIC; fig|1227352.4.peg.398; -.
DR eggNOG; COG1939; Bacteria.
DR OrthoDB; 46571at2; -.
DR Proteomes; UP000019051; 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 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 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 DOMAIN 27..124
FT /note="RNase III"
FT /evidence="ECO:0000259|Pfam:PF00636"
FT ACT_SITE 33
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01468"
SQ SEQUENCE 145 AA; 16497 MW; 0CF3B1A699EDE8FC CRC64;
MNGLFDLNRA WFPYEPSKPA HLLPPIVLAY AGDAIYEVAV RQYLISLPNL RPQHLHRSAT
GLVSARAQSN ILAYLDPVLT EDEKDVVRRG RNAKSGSIPK NADVLEYRHA TAFECMIGYL
YYTGQQARIQ ELVHSSIEYM MHRPK
//