ID A0A0N9IE96_9PSEU Unreviewed; 251 AA.
AC A0A0N9IE96;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=AOZ06_45055 {ECO:0000313|EMBL:ALG13083.1};
OS Kibdelosporangium phytohabitans.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kibdelosporangium.
OX NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG13083.1, ECO:0000313|Proteomes:UP000063699};
RN [1] {ECO:0000313|EMBL:ALG13083.1, ECO:0000313|Proteomes:UP000063699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG13083.1,
RC ECO:0000313|Proteomes:UP000063699};
RA Qin S., Xing K.;
RT "Genome sequencing of Kibdelosporangium phytohabitans.";
RL Submitted (JUL-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; CP012752; ALG13083.1; -; Genomic_DNA.
DR RefSeq; WP_054294973.1; NZ_JADBEI010000001.1.
DR AlphaFoldDB; A0A0N9IE96; -.
DR STRING; 860235.AOZ06_45055; -.
DR KEGG; kphy:AOZ06_45055; -.
DR OrthoDB; 9805026at2; -.
DR Proteomes; UP000063699; 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:UP000063699};
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 27..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 210..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT ACT_SITE 131
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT BINDING 52
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 251 AA; 26553 MW; B919E4F20F584436 CRC64;
MGGRGGRNGA GDPSSLRDAL GVELGSDLLQ LALTHRSYAY ENGGLPPNER LEFLGDSVLG
MVITDHLYRT HSDLPEGQLA RLRASVVNMH ALARVARGLG AGGLGAHLLL GRGEELTGGR
DKASILADTL EAVIGAVYLQ EGIDVARNVV HKLFDQLLDE APRRGAGLDW KTSLQELCAS
AGLGVPEYRV EEEGPDHRKE FKATVVVAGQ SYGSGDGRTK KEAEQKAAEG AYRELSEIHL
PPENGAGDNG A
//
