ID A0A0H4BYT6_9ACTN Unreviewed; 268 AA.
AC A0A0H4BYT6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=QR97_09505 {ECO:0000313|EMBL:AKN70038.1};
OS Streptomyces sp. PBH53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1577075 {ECO:0000313|EMBL:AKN70038.1, ECO:0000313|Proteomes:UP000036399};
RN [1] {ECO:0000313|EMBL:AKN70038.1, ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|EMBL:AKN70038.1,
RC ECO:0000313|Proteomes:UP000036399};
RX PubMed=26227608;
RA Gosse J.T., Hill P., Dowd S.E., Boddy C.N.;
RT "Draft Genome Sequence of Streptomyces sp. Strain PBH53, Isolated from an
RT Urban Environment.";
RL Genome Announc. 3:e00859-e00815(2015).
RN [2] {ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|Proteomes:UP000036399};
RA Gosse J.T., Boddy C.N., Hill P.B.;
RT "Draft Genome Sequence of Streptomyces sp. strain PBH53, isolated from
RT urban environment.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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|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; CP011799; AKN70038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4BYT6; -.
DR STRING; 1577075.QR97_09505; -.
DR PATRIC; fig|1577075.3.peg.1943; -.
DR Proteomes; UP000036399; 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; PTHR11207:SF0; RIBONUCLEASE 3; 1.
DR PANTHER; PTHR11207; RIBONUCLEASE III; 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|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00104};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00104};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00104};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00104};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP-
KW Rule:MF_00104};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00104};
KW Reference proteome {ECO:0000313|Proteomes:UP000036399};
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 16..142
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 169..237
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 242..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 59
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT ACT_SITE 131
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ SEQUENCE 268 AA; 28419 MW; B87FC7E9E4D7182B CRC64;
MSTPKKNSAD NQASSHTLLE GRLGYQVESA LLVRALTHRS YAYENGGLPT NERLEFLGDS
VLGLVVTDTL YRTHPDLPEG QLAKLRAAVV NSRALAEVGR GLDLGSFIRL GRGEEGTGGR
DKASILADTL EAVIGAVYLD QGLDAASELV HRLFDPLIEK SSNLGAGLDW KTSLQELTAI
EGLGVPEYLV TETGPDHEKT FTAAARVGGV SYGTGTGRSK KEAEQQAAES AWRSIRAAAD
ERAKVAKEPV RETADEAVRG GDTSSATA
//
