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Database: UniProt
Entry: W0V317_9BURK
LinkDB: W0V317_9BURK
Original site: W0V317_9BURK 
ID   W0V317_9BURK            Unreviewed;       269 AA.
AC   W0V317;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ECO:0000313|EMBL:CDG82271.1};
GN   ORFNames=GJA_1627 {ECO:0000313|EMBL:CDG82271.1};
OS   Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG82271.1, ECO:0000313|Proteomes:UP000027604};
RN   [1] {ECO:0000313|EMBL:CDG82271.1, ECO:0000313|Proteomes:UP000027604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX   PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA   Graupner K., Lackner G., Hertweck C.;
RT   "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT   agaricidamnosum.";
RL   Genome Announc. 3:e00277-e00277(2015).
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|ARBA:ARBA00001946,
CC         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}.
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DR   EMBL; HG322949; CDG82271.1; -; Genomic_DNA.
DR   RefSeq; WP_038490629.1; NZ_HG322949.1.
DR   AlphaFoldDB; W0V317; -.
DR   STRING; 1349767.GJA_1627; -.
DR   KEGG; jag:GJA_1627; -.
DR   PATRIC; fig|1349767.4.peg.3313; -.
DR   eggNOG; COG0571; Bacteria.
DR   HOGENOM; CLU_000907_1_1_4; -.
DR   OrthoDB; 9805026at2; -.
DR   Proteomes; UP000027604; Chromosome I.
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|HAMAP-Rule:MF_00104};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00104, ECO:0000313|EMBL:CDG82271.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00104};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00104};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP-
KW   Rule:MF_00104}; Nuclease {ECO:0000256|HAMAP-Rule:MF_00104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027604};
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          3..125
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          152..222
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   ACT_SITE        42
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ   SEQUENCE   269 AA;  29528 MW;  7DECD35688E16D90 CRC64;
     MNLQLLQTRL GYTFQDAGLL QQALTHRSHS SLHNERLEFL GDSILNCVVA SILYERFHAI
     DEGDLSRLRA NLVKQQSLYE IAQKLELSQF LRLGEGELKS GGFRRPSILA DTLEALLGAI
     FLDTGFNAAR DVIRAFYIPI LDSVDPQTLG KDAKTLLQEF LQSKKISLPQ YNVVATHGAA
     HSQEFEIECL VPKLNIQVYG RGGSRRAGEQ AAAKLALEVA EQALLKTPAA SRKAKPRTAQ
     LKLAGIATNQ SDAADSVAAI AINTQQNRH
//
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