ID   RNC_CAEEL               Reviewed;        1086 AA.
AC   O01326; A8WI03; O01327; Q9U9Q8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Ribonuclease 3;
DE            EC=3.1.26.3;
DE   AltName: Full=Protein drosha;
DE   AltName: Full=Ribonuclease III;
DE            Short=RNase III;
GN   Name=drsh-1; ORFNames=F26E4.10;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 227-1086 (ISOFORM A).
RX   PubMed=10713462; DOI=10.1016/s0378-1119(99)00571-5;
RA   Filippov V., Solovyev V., Filippova M., Gill S.S.;
RT   "A novel type of RNase III family proteins in eukaryotes.";
RL   Gene 245:213-221(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15531879; DOI=10.1038/nature03049;
RA   Denli A.M., Tops B.B.J., Plasterk R.H.A., Ketting R.F., Hannon G.J.;
RT   "Processing of primary microRNAs by the Microprocessor complex.";
RL   Nature 432:231-235(2004).
CC   -!- FUNCTION: Executes the initial step of microRNA (miRNA) processing in
CC       the nucleus, that is the cleavage of pri-miRNA to release pre-miRNA.
CC       Involved in pre-rRNA processing. Cleaves double-strand RNA and does not
CC       cleave single-strand RNA. Involved in fertility. Required for the
CC       function or synthesis of the let-7 miRNA.
CC       {ECO:0000269|PubMed:15531879}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRR4};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRR4};
CC       Note=Each RNase III domain binds at least one Mg(2+) or Mn(2+) ion.
CC       {ECO:0000250|UniProtKB:Q9NRR4};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=O01326-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=O01326-2; Sequence=VSP_043603, VSP_034688;
CC   -!- DISRUPTION PHENOTYPE: Sterility. {ECO:0000269|PubMed:15531879}.
CC   -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
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DR   EMBL; AF160248; AAD45518.1; -; mRNA.
DR   EMBL; Z81070; CAB03006.3; -; Genomic_DNA.
DR   EMBL; Z81070; CAP19331.2; -; Genomic_DNA.
DR   PIR; T21420; T21420.
DR   RefSeq; NP_001122460.2; NM_001128988.2. [O01326-2]
DR   RefSeq; NP_492599.1; NM_060198.3. [O01326-1]
DR   AlphaFoldDB; O01326; -.
DR   SMR; O01326; -.
DR   BioGRID; 38253; 5.
DR   STRING; 6239.F26E4.10a.1; -.
DR   EPD; O01326; -.
DR   PaxDb; 6239-F26E4-10a; -.
DR   PeptideAtlas; O01326; -.
DR   EnsemblMetazoa; F26E4.10a.1; F26E4.10a.1; WBGene00009163. [O01326-1]
DR   EnsemblMetazoa; F26E4.10b.1; F26E4.10b.1; WBGene00009163. [O01326-2]
DR   GeneID; 172830; -.
DR   KEGG; cel:CELE_F26E4.10; -.
DR   UCSC; F26E4.10a; c. elegans.
DR   AGR; WB:WBGene00009163; -.
DR   WormBase; F26E4.10a; CE29039; WBGene00009163; drsh-1. [O01326-1]
DR   WormBase; F26E4.10b; CE46611; WBGene00009163; drsh-1. [O01326-2]
DR   eggNOG; KOG1817; Eukaryota.
DR   GeneTree; ENSGT00730000111052; -.
DR   InParanoid; O01326; -.
DR   OMA; NDGPECR; -.
DR   OrthoDB; 5486676at2759; -.
DR   PhylomeDB; O01326; -.
DR   PRO; PR:O01326; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00009163; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0070877; C:microprocessor complex; ISS:WormBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004525; F:ribonuclease III activity; IMP:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR   GO; GO:0031054; P:pre-miRNA processing; IBA:GO_Central.
DR   GO; GO:0031053; P:primary miRNA processing; IMP:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0019953; P:sexual reproduction; IMP:UniProtKB.
DR   CDD; cd19877; DSRM_RNAse_III_meta_like; 1.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 2.
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; IPR044442; RNAse_III_DSRM__animal.
DR   InterPro; IPR036389; RNase_III_sf.
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   Pfam; PF00636; Ribonuclease_3; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF69065; RNase III domain-like; 2.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS00517; RNASE_3_1; 2.
DR   PROSITE; PS50142; RNASE_3_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein; Differentiation; Endonuclease;
KW   Gonadal differentiation; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nuclease; Nucleus; Reference proteome; Repeat; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN           1..1086
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_0000180469"
FT   DOMAIN          607..781
FT                   /note="RNase III 1"
FT   DOMAIN          833..957
FT                   /note="RNase III 2"
FT   DOMAIN          984..1059
FT                   /note="DRBM"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         694
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O67082"
FT   BINDING         767
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O67082"
FT   BINDING         770
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O67082"
FT   BINDING         873
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O67082"
FT   BINDING         943
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O67082"
FT   BINDING         946
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O67082"
FT   SITE            939
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         668..669
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_043603"
FT   VAR_SEQ         1072..1074
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034688"
SQ   SEQUENCE   1086 AA;  125334 MW;  4A478120F88F8FB8 CRC64;
     MSDEKISMTL NFPKHKRARR KKYQKEYQER HKEEMMQQLG RRFQNQPSTS SAPPDTVEKI
     PLPTESTSAL PFGDSPRLTE KDYETNYMID PPVVSTHSAE LIKSNRVVIK AEEAEKYMMI
     KAKSTTSKIL QDFQTKILET VKTKRRLQAD VPYIIHPCHS MKGRKTPKQK GGDESFTASD
     VSDDSNDSQD EASTSEPTNR QAPEADKTGE VKDEKQTCNR RNQQRKAKRL RNFEEKERQI
     TLLKKGIDRK KTHPNGIHPD ISFNEKGLGN EGPECRCPEP IKTCGLKHGY YAGEDKAIDC
     KKSNGENLHY YTLRVTPLPS ENQLYRTHMA INGEEFEFEG FSLITHAPLP DCMTRAPICK
     YSMDYEFQLV EEFMPDECFD PEDCDMLFEY IFHEIFEMLD FELRPKHIPS DVESCPMIHI
     MPRFVQTKDD LVQLWSSKTV LAYFTSKGSS EIMSPEDVNR LCDAQIDQFT RNTSKHKQSI
     VLNTKFKPSA IRADWFERDE EKKEVYVVHN AIRAQTYTAI SLPRIAFLEK TLNKMIQEKQ
     SSGVYNKDFE KTKNELEHLK RENRSARNLK LREPVAGFIE TGLKPDVAAH VVMTILACHH
     IRYNFSLDVF EEVIEYKFND RRVIELALMH SSFKSHYGTP IDHVKNMITN CGYRRKYGAE
     DKREKKRVAG IMSLFNIMKG TSGGEPILHN ERLEYLGDAV VELIVSHHLY FMLTHHFEGG
     LATYRTALVQ NRNLATLAKN CRIDEMLQYS HGADLINVAE FKHALANAFE AVMAAIYLDG
     GLAPCDVIFS KAMYGHQPVL KEKWDHINEH ELKREDPQGD RDLSFITPTL STFHALEERL
     GIQFNNIRLL AKAFTRRNIP NNDLTKGHNQ RLEWLGDSVL QLIVSDFLYR RFPYHHEGHM
     SLLRTSLVSN QTQAVVCDDL GFTEFVIKAP YKTPELKLKD KADLVEAFIG ALYVDRGIEH
     CRAFIRIVFC PRLKHFIESE KWNDAKSHLQ QWCLAMRDPS SSEPDMPEYR VLGIEGPTNN
     RIFKIAVYYK GKRLASAAES NVHKAELRVA ELALANLESM SFSKMKAKNN SWFQNMRRRL
     EQDTSD
//