RNC_CAEEL
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 03-AUG-2022, entry version 148.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 4.
DR STRING; 6239.F26E4.10a; -.
DR EPD; O01326; -.
DR PaxDb; O01326; -.
DR PeptideAtlas; O01326; -.
DR PRIDE; 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 CTD; 172830; -.
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; EPDIPEY; -.
DR OrthoDB; 212036at2759; -.
DR PhylomeDB; O01326; -.
DR PRO; PR:O01326; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009163; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0070877; C:microprocessor complex; ISS:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; 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: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; IEA:InterPro.
DR GO; GO:0031053; P:primary miRNA processing; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
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; 1.10.1520.10; -; 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; PTHR11207; 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; SSF69065; SSF69065; 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
