RNC_STRCO
ID RNC_STRCO Reviewed; 276 AA.
AC Q9ZBQ7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Antibiotic biosynthesis protein B;
DE Short=AbsB;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc; Synonyms=absB; OrderedLocusNames=SCO5572; ORFNames=SC7A1.16;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PROCESSING OF RRNA,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-172.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=10498729; DOI=10.1128/jb.181.19.6142-6151.1999;
RA Price B., Adamidis T., Kong R., Champness W.;
RT "A Streptomyces coelicolor antibiotic regulatory gene, absB, encodes an
RT RNase III homolog.";
RL J. Bacteriol. 181:6142-6151(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP ROLE IN GLOBAL GENE REGULATION, AND MUTAGENESIS OF LEU-172.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=16313616; DOI=10.1111/j.1365-2958.2005.04879.x;
RA Huang J., Shi J., Molle V., Sohlberg B., Weaver D., Bibb M.J.,
RA Karoonuthaisiri N., Lih C.J., Kao C.M., Buttner M.J., Cohen S.N.;
RT "Cross-regulation among disparate antibiotic biosynthetic pathways of
RT Streptomyces coelicolor.";
RL Mol. Microbiol. 58:1276-1287(2005).
RN [4]
RP FUNCTION AS AN ENDORIBONUCLEASE, FUNCTION IN PROCESSING OF MRNA, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=21742867; DOI=10.1128/jb.00452-11;
RA Gatewood M.L., Bralley P., Jones G.H.;
RT "RNase III-dependent expression of the rpsO-pnp operon of Streptomyces
RT coelicolor.";
RL J. Bacteriol. 193:4371-4379(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). Also processes some mRNAs, and tRNAs
CC when they are encoded in the rRNA operon. May modulate key aspects of
CC gene expression as its absence has extensive effects on the abundance
CC of about 200 different transcripts. Probably processes pre-crRNA and
CC tracrRNA of type II CRISPR loci if present in the organism.
CC {ECO:0000269|PubMed:10498729, ECO:0000269|PubMed:16313616,
CC ECO:0000269|PubMed:21742867}.
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 -!- DISRUPTION PHENOTYPE: Not essential. Deficient in endogenous antibiotic
CC synthesis, able to form a sporulating aerial mycelium. Accumulates a
CC 30S rRNA precursor transcript. Leads to increased expression of pnp due
CC to increased transcript levels. {ECO:0000269|PubMed:10498729,
CC ECO:0000269|PubMed:21742867}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA22415.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL939124; CAA22415.1; ALT_INIT; Genomic_DNA.
DR PIR; T35656; T35656.
DR RefSeq; NP_629707.1; NC_003888.3.
DR RefSeq; WP_003973423.1; NZ_CP042324.1.
DR AlphaFoldDB; Q9ZBQ7; -.
DR SMR; Q9ZBQ7; -.
DR STRING; 100226.SCO5572; -.
DR GeneID; 1101013; -.
DR KEGG; sco:SCO5572; -.
DR PATRIC; fig|100226.15.peg.5661; -.
DR eggNOG; COG0571; Bacteria.
DR HOGENOM; CLU_000907_1_2_11; -.
DR InParanoid; Q9ZBQ7; -.
DR BRENDA; 3.1.26.3; 5998.
DR Proteomes; UP000001973; 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 1: Evidence at protein level;
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..276
FT /note="Ribonuclease 3"
FT /id="PRO_0000180440"
FT DOMAIN 31..157
FT /note="RNase III"
FT DOMAIN 184..252
FT /note="DRBM"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 74
FT /evidence="ECO:0000255"
FT ACT_SITE 146
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 172
FT /note="L->P: In strain C120; loss of endogenous antibiotic
FT synthesis, decrease in transcript abundance of genes
FT involved in secondary metabolism."
FT /evidence="ECO:0000269|PubMed:10498729,
FT ECO:0000269|PubMed:16313616"
SQ SEQUENCE 276 AA; 29141 MW; D0C69BEABF62313C CRC64;
MRGTVSVPKK AEDAKADPPA KKKADTQASS HTLLEGRLGY QLESALLVRA LTHRSYAYEN
GGLPTNERLE FLGDSVLGLV VTDTLYRTHP DLPEGQLAKL RAAVVNSRAL AEVGRGLELG
SFIRLGRGEE GTGGRDKASI LADTLEAVIG AVYLDQGLDA ASELVHRLFD PLIEKSSNLG
AGLDWKTSLQ ELTATEGLGV PEYLVTETGP DHEKTFTAAA RVGGVSYGTG TGRSKKEAEQ
QAAESAWRSI RAAADERAKA TADAVDADPD EASASA
