ID A0A2G1XCR3_STRCJ Unreviewed; 280 AA.
AC A0A2G1XCR3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=BLA24_23420 {ECO:0000313|EMBL:PHQ49044.1}, CYQ11_22650
GN {ECO:0000313|EMBL:PPT15310.1};
OS Streptomyces cinnamoneus (Streptoverticillium cinnamoneum).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces cinnamoneus group.
OX NCBI_TaxID=53446 {ECO:0000313|EMBL:PHQ49044.1, ECO:0000313|Proteomes:UP000222531};
RN [1] {ECO:0000313|EMBL:PHQ49044.1, ECO:0000313|Proteomes:UP000222531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21532 {ECO:0000313|EMBL:PHQ49044.1,
RC ECO:0000313|Proteomes:UP000222531};
RX PubMed=29053243;
RA Patteson J., Cai W., Johnson R.A., Santa Maria K., Li B.;
RT "Identification of the Biosynthetic Pathway for the Antibiotic
RT Bicyclomycin.";
RL Biochemistry 0:0-0(2017).
RN [2] {ECO:0000313|EMBL:PPT15310.1, ECO:0000313|Proteomes:UP000239771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41675 {ECO:0000313|EMBL:PPT15310.1,
RC ECO:0000313|Proteomes:UP000239771};
RA Vior N.M., Lacret R., Chandra G., Dorai-Raj S., Trick M., Truman A.W.;
RT "Discovery and biosynthesis of the antibiotic bicyclomycin in distant
RT bacterial classes.";
RL Submitted (DEC-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHQ49044.1}.
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DR EMBL; NHZO01000154; PHQ49044.1; -; Genomic_DNA.
DR EMBL; PKFQ01000001; PPT15310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1XCR3; -.
DR OrthoDB; 9805026at2; -.
DR Proteomes; UP000222531; Unassembled WGS sequence.
DR Proteomes; UP000239771; Unassembled WGS sequence.
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:UP000222531};
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 26..152
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 179..247
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 69
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT ACT_SITE 141
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ SEQUENCE 280 AA; 29228 MW; BC3DEFA6F343E3D6 CRC64;
MSDASKSSRT RGNDTEPAPA DAASSHTLLE GRLGYRLETA LLVRALTHRS YAYENGGLPT
NERLEFLGDS VLGLVVTDTL YRIHPDLPEG QLAKLRAAVV NSRALAEVGR GLDLGSFIRL
GRGEEGTGGR DKASILADTL EAVIGAVYLD QGLDAAAELV HRLFDPLIEK SSNLGAGLDW
KTSLQELTAT EGLGVPEYLV SETGPDHEKT FTAAARVGGV AYGTGTGRSK KEAEQQAAES
AWRAINSAAE ARLAAEKAAA ESGAVPEGDT PSDSAQGAAS
//
