ID A0A0B0D511_9BACI Unreviewed; 230 AA.
AC A0A0B0D511;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=LD39_10800 {ECO:0000313|EMBL:KHE70981.1};
OS Halobacillus sp. BBL2006.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE70981.1, ECO:0000313|Proteomes:UP000030879};
RN [1] {ECO:0000313|EMBL:KHE70981.1, ECO:0000313|Proteomes:UP000030879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE70981.1,
RC ECO:0000313|Proteomes:UP000030879};
RA Kirchner G., Treves D., Francis J.III.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BBL2006.";
RL Submitted (SEP-2014) 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:KHE70981.1}.
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DR EMBL; JRNX01000339; KHE70981.1; -; Genomic_DNA.
DR RefSeq; WP_035546163.1; NZ_JRNX01000339.1.
DR AlphaFoldDB; A0A0B0D511; -.
DR OrthoDB; 9805026at2; -.
DR Proteomes; UP000030879; 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; PTHR11207:SF0; RIBONUCLEASE 3; 1.
DR PANTHER; PTHR11207; RIBONUCLEASE III; 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:UP000030879};
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 4..133
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 159..228
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT ACT_SITE 50
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT ACT_SITE 122
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ SEQUENCE 230 AA; 26138 MW; 0D323908D879B644 CRC64;
MDDFSSFQNN IDVQFNDVSL LEQAFTHSSY VNEHRKTDRE DNERLEFLGD AVLELGVSQY
LYREFPNMAE GELTKFRASI VCEVSLVQFA NELNFQDLIL LGKGEEMTGG RNRPALLADV
FEAFIGALYL DQGFETVVQF LRSYVYPKVK KGAFSHAMDF KSQLQEFIQR DKNSKIEYEI
VEERGPAHSR EFIAHVRIQG DIGGIGIGRT KKEAEQKAAQ QALENHGAIS
//
