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Entry: A0A2G2KG66_9PROT
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ID   A0A2G2KG66_9PROT        Unreviewed;       223 AA.
AC   A0A2G2KG66;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=COA89_01685 {ECO:0000313|EMBL:PHS09562.1};
OS   Acidithiobacillus sp.
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=1872118 {ECO:0000313|EMBL:PHS09562.1, ECO:0000313|Proteomes:UP000221235};
RN   [1] {ECO:0000313|Proteomes:UP000221235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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:PHS09562.1}.
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DR   EMBL; NVVQ01000003; PHS09562.1; -; Genomic_DNA.
DR   Proteomes; UP000221235; 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   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00104}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_00104};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00104};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00104}.
FT   DOMAIN          5..127
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          154..223
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         113
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ   SEQUENCE   223 AA;  24265 MW;  E7130845DB84E7AD CRC64;
     MASNQDKLES VIGYQFLDSG LLDRALTHRS FSALNNERLE FLGDSVLGXI VSAVLYRLYT
     ESEEGELTRM RAQVVKKDTL AQIARRLQLG SYLKLGGSXV KGGGADIDSI LADALEALIG
     AVYLDAGLEQ AQISVAEIFK EELDAIDPGC MAKDPKTELQ ELLQSKGMLL PKYIVESMSG
     SSHEPNFVVS CHVEDDQLVK SGTGPSRKSA EQAAARKLLR ILR
//
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