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Database: UniProt
Entry: A0A177HV70_9ACTN
LinkDB: A0A177HV70_9ACTN
Original site: A0A177HV70_9ACTN 
ID   A0A177HV70_9ACTN        Unreviewed;       282 AA.
AC   A0A177HV70;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   ECO:0000313|EMBL:OAH14805.1};
GN   ORFNames=STSP_18920 {ECO:0000313|EMBL:OAH14805.1};
OS   Streptomyces jeddahensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH14805.1, ECO:0000313|Proteomes:UP000077381};
RN   [1] {ECO:0000313|EMBL:OAH14805.1, ECO:0000313|Proteomes:UP000077381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA   Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA   Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT   "Genome sequence of Streptomyces sp. G25.";
RL   Submitted (DEC-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}.
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:OAH14805.1}.
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DR   EMBL; LOHS01000057; OAH14805.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177HV70; -.
DR   STRING; 1716141.STSP_18920; -.
DR   PATRIC; fig|1716141.3.peg.1985; -.
DR   Proteomes; UP000077381; 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:UP000077381};
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          41..160
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          187..255
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         73
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00104"
SQ   SEQUENCE   282 AA;  29402 MW;  70A7D2B04ACE8395 CRC64;
     MRGAVSIPKK ADDARKNGPR TGGGVPADNT ASSHTLLEGR LGYKLESALL VRALTHRSYA
     YENGGLPTNE RLEFLGDSVL GLVVTDTLYR THPDLPEGQL AKLRAAVVNS RALAEVGRGL
     DLGAFIRLGR GEEGTGGRDK ASILADTLEA VIGAVYLDQG LDVAAELVHR LFDPLIEKSS
     NLGAGLDWKT SLQELTATEG LGVPEYLVTE TGPDHEKTFT AAARVGGVSY GTGTGRSKKE
     AEQQAAESAW RAIRAAADER AKAAAAAGSD GAPDVTSAPT TA
//
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