ID   RNC_ACICP               Reviewed;         230 AA.
AC   F0KKL2;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Ribonuclease 3;
DE            EC=3.1.26.3;
DE   AltName: Full=Ribonuclease III;
DE            Short=RNase III;
GN   Name=rnc; OrderedLocusNames=BDGL_001989;
OS   Acinetobacter calcoaceticus (strain PHEA-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=871585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHEA-2;
RX   PubMed=21441526; DOI=10.1128/jb.00261-11;
RA   Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA   Yuan M., Zhou Z., Elmerich C., Lin M.;
RT   "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT   industry wastewater.";
RL   J. Bacteriol. 193:2672-2673(2011).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADY82575.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP002177; ADY82575.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_014207368.1; NC_016603.1.
DR   RefSeq; YP_004996257.1; NC_016603.1.
DR   AlphaFoldDB; F0KKL2; -.
DR   SMR; F0KKL2; -.
DR   STRING; 871585.BDGL_001989; -.
DR   GeneID; 11640182; -.
DR   KEGG; acc:BDGL_001989; -.
DR   PATRIC; fig|871585.3.peg.1988; -.
DR   eggNOG; COG0571; Bacteria.
DR   HOGENOM; CLU_000907_1_1_6; -.
DR   OrthoDB; 9805026at2; -.
DR   Proteomes; UP000007477; Chromosome.
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; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   mRNA processing; Nuclease; Reference proteome; RNA-binding;
KW   rRNA processing; rRNA-binding; tRNA processing.
FT   CHAIN           1..230
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_0000416603"
FT   DOMAIN          10..133
FT                   /note="RNase III"
FT   DOMAIN          161..230
FT                   /note="DRBM"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   230 AA;  26294 MW;  05A6A4A29EFC98B8 CRC64;
     MIKHQFKLSD PRLLSRIGYQ FKQLELLQLA LTHRSVSHKY NYERLEFLGD SLLGMIIANY
     LYHAYPNENE GRLTRMRATL VRQEALGKIA TDLQLSRCLI LSTGELKSGG HHRESILADT
     VEAIIGAIYL DSGDLNLLKD IVLKWYIPYL DHIEPTDQLK DPKSRLQEYL QARKKPLPVY
     EVVDIQGDAP HQHFKVECVV DGLPKIYGEG SSRRFAEQAA AAEILKLLEQ
//