RNC_PSEAE
ID RNC_PSEAE Reviewed; 229 AA.
AC Q9XCX9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_00104};
DE EC=3.1.26.3 {ECO:0000255|HAMAP-Rule:MF_00104};
DE AltName: Full=Ribonuclease III {ECO:0000255|HAMAP-Rule:MF_00104};
DE Short=RNase III {ECO:0000255|HAMAP-Rule:MF_00104};
GN Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104}; OrderedLocusNames=PA0770;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAK;
RX PubMed=10438789; DOI=10.1128/jb.181.16.5111-5113.1999;
RA Powell B.S., Peters H.K. III, Nakamura Y., Court D.L.;
RT "Cloning and analysis of the rnc-era-recO operon from Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 181:5111-5113(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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:0000255|HAMAP-
CC Rule:MF_00104}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00104}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00104}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000255|HAMAP-
CC Rule:MF_00104}.
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DR EMBL; AF123492; AAD40229.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04159.1; -; Genomic_DNA.
DR PIR; E83548; E83548.
DR RefSeq; NP_249461.1; NC_002516.2.
DR RefSeq; WP_003085565.1; NZ_QZGE01000007.1.
DR AlphaFoldDB; Q9XCX9; -.
DR SMR; Q9XCX9; -.
DR STRING; 287.DR97_1213; -.
DR PaxDb; Q9XCX9; -.
DR PRIDE; Q9XCX9; -.
DR DNASU; 882139; -.
DR EnsemblBacteria; AAG04159; AAG04159; PA0770.
DR GeneID; 882139; -.
DR KEGG; pae:PA0770; -.
DR PATRIC; fig|208964.12.peg.800; -.
DR PseudoCAP; PA0770; -.
DR HOGENOM; CLU_000907_1_1_6; -.
DR InParanoid; Q9XCX9; -.
DR OMA; LTHKSCK; -.
DR PhylomeDB; Q9XCX9; -.
DR BioCyc; PAER208964:G1FZ6-783-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
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 PANTHER; PTHR11207; PTHR11207; 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; 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; Reference proteome; RNA-binding;
KW rRNA processing; rRNA-binding; tRNA processing.
FT CHAIN 1..229
FT /note="Ribonuclease 3"
FT /id="PRO_0000180419"
FT DOMAIN 5..127
FT /note="RNase III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT DOMAIN 154..224
FT /note="DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT ACT_SITE 44
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT ACT_SITE 116
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
SQ SEQUENCE 229 AA; 25506 MW; 9D884F21A0088B6E CRC64;
MSNSLDRLER KLGYTFKDRD LMVLALTHRS YAGRNNERLE FLGDAILNFV IGEALFHHFP
QAREGQLSRL RARLVKGETL ALLARGFEVG DYLRLGSGEL KSGGFRRESI LADAMEALIG
AIYLDTGMDS ARERIIAWLG PQLRELTPVD TNKDPKTRLQ EFLQSRGCDL PRYEVVDIQG
EPHCRTFFVD CEVALLSDKT HGHGGSRRIA EQVAAAAALV ALGVENGHD
