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Database: UniProt
Entry: A0A0J6D5T3_9BACI
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ID   A0A0J6D5T3_9BACI        Unreviewed;       240 AA.
AC   A0A0J6D5T3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Ribonuclease 3 {ECO:0000256|HAMAP-Rule:MF_00104};
DE            EC=3.1.26.3 {ECO:0000256|HAMAP-Rule:MF_00104};
DE   AltName: Full=Ribonuclease III {ECO:0000256|HAMAP-Rule:MF_00104};
DE            Short=RNase III {ECO:0000256|HAMAP-Rule:MF_00104};
GN   Name=rnc {ECO:0000256|HAMAP-Rule:MF_00104};
GN   ORFNames=AB986_05390 {ECO:0000313|EMBL:KMM39644.1};
OS   Alkalihalobacillus macyae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=157733 {ECO:0000313|EMBL:KMM39644.1, ECO:0000313|Proteomes:UP000035996};
RN   [1] {ECO:0000313|EMBL:KMM39644.1, ECO:0000313|Proteomes:UP000035996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16346 {ECO:0000313|EMBL:KMM39644.1,
RC   ECO:0000313|Proteomes:UP000035996};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Che J., Ge C., Shi H.,
RA   Pan Z., Liu X.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Digests double-stranded RNA. Involved in the processing of
CC       primary rRNA transcript to yield the immediate precursors to the large
CC       and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when
CC       they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA
CC       of type II CRISPR loci if present in the organism. {ECO:0000256|HAMAP-
CC       Rule:MF_00104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000109, ECO:0000256|HAMAP-
CC         Rule:MF_00104};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00104};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00104}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00104}.
CC   -!- SIMILARITY: Belongs to the ribonuclease III family.
CC       {ECO:0000256|ARBA:ARBA00010183}.
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:KMM39644.1}.
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DR   EMBL; LELK01000001; KMM39644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6D5T3; -.
DR   STRING; 157733.AB986_05390; -.
DR   PATRIC; fig|157733.3.peg.3316; -.
DR   Proteomes; UP000035996; 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:0004525; F:ribonuclease III activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd10845; DSRM_RNAse_III_family; 1.
DR   CDD; cd00593; RIBOc; 1.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 1.
DR   HAMAP; MF_00104; RNase_III; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   NCBIfam; TIGR02191; RNaseIII; 1.
DR   PANTHER; PTHR14950; DICER-RELATED; 1.
DR   PANTHER; PTHR14950:SF37; ENDORIBONUCLEASE DICER; 1.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF14622; Ribonucleas_3_3; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF69065; RNase III domain-like; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS00517; RNASE_3_1; 1.
DR   PROSITE; PS50142; RNASE_3_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00104};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00104};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00104};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00104};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00104};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP-
KW   Rule:MF_00104};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035996};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00104};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_00104}; rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00104};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00104}.
FT   DOMAIN          10..139
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          165..234
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         125
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ   SEQUENCE   240 AA;  27096 MW;  F3109C0DA6F411AB CRC64;
     MVGDATRSQF AAFQEEIGVS FENEQLLFQA FTHSSYVNEH RLHPQMDNER LEFLGDAVLE
     LTISRYLYEK YPNMSEGQLT KLRAAIVCEP SLVQFANDLN FGHLVLLGKG EEMTGGRMRP
     ALLADVFESF VCALYLDRGL EVVFEFLEKF VYPKINAGAF SHVMDYKSQL QEVIQREGLG
     GIDYVITDEK GPAHNREFSS KVMLNGNDLG VGIGRSKKEA EQMAAQKALL NLKERNEKES
//
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