ID   RNC_ACIB3               Reviewed;         230 AA.
AC   B7GYT0;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Ribonuclease 3;
DE            EC=3.1.26.3;
DE   AltName: Full=Ribonuclease III;
DE            Short=RNase III;
GN   Name=rnc; OrderedLocusNames=ABBFA_000926;
OS   Acinetobacter baumannii (strain AB307-0294).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=557600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB307-0294;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(2008).
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=ACJ56668.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001172; ACJ56668.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000160699.1; NZ_CP001172.1.
DR   AlphaFoldDB; B7GYT0; -.
DR   SMR; B7GYT0; -.
DR   GeneID; 66396309; -.
DR   HOGENOM; CLU_000907_1_1_6; -.
DR   Proteomes; UP000006924; 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; cd00593; RIBOc; 1.
DR   Gene3D; 1.10.1520.10; -; 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   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF14622; Ribonucleas_3_3; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF69065; SSF69065; 1.
DR   TIGRFAMs; TIGR02191; RNaseIII; 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; RNA-binding; rRNA processing; rRNA-binding;
KW   tRNA processing.
FT   CHAIN           1..230
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_0000416602"
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;  26285 MW;  2AABC50C891B3120 CRC64;
     MTKHQFKLSD PRLLSRIGYQ FKQPELLQLA LTHRSVSHKY NYERLEFLGD SLLGMIIANY
     LYHAYPHENE GRLTRMRATL VRQEALGKIA TDLQLSRCLI LSTGELKSGG HHRESILADT
     VEAIIGAIYL DSSDLNLLKD IVLKWYTPYL DHIEPTDQLK DPKSRLQEYL QARKKPLPVY
     EVVDIQGDAP HQHFKVECLV DGLSKIHGEG SSRRFAEQAA AAEILKLLEQ