ID   RNC_CAEBR               Reviewed;        1061 AA.
AC   Q61XX9; A8WWR6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 103.
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 {ECO:0000250|UniProtKB:O01326}; ORFNames=CBG03798;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC         Evidence={ECO:0000255};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NRR4}.
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; HE600906; CAP24627.1; -; Genomic_DNA.
DR   RefSeq; XP_002639240.1; XM_002639194.1.
DR   AlphaFoldDB; Q61XX9; -.
DR   SMR; Q61XX9; -.
DR   STRING; 6238.Q61XX9; -.
DR   GeneID; 8581234; -.
DR   KEGG; cbr:CBG_03798; -.
DR   CTD; 8581234; -.
DR   WormBase; CBG03798; CBP41277; WBGene00026581; Cbr-drsh-1.
DR   eggNOG; KOG1817; Eukaryota.
DR   HOGENOM; CLU_004383_1_0_1; -.
DR   InParanoid; Q61XX9; -.
DR   OMA; NDGPECR; -.
DR   OrthoDB; 5486676at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0070877; C:microprocessor complex; IBA:GO_Central.
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; ISS: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; ISS:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0019953; P:sexual reproduction; ISS: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   3: Inferred from homology;
KW   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..1061
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_0000309457"
FT   DOMAIN          586..759
FT                   /note="RNase III 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          811..935
FT                   /note="RNase III 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          962..1037
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         851
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         921
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         924
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            917
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1061 AA;  122481 MW;  796401EAD0B5138E CRC64;
     MDFTEIHKRS RRKKFQQIHQ DRKDEMIQQL GRRFHNQPST SATYPSAVED IPLPSEVPNV
     FGAPPPLTNA DFHRNFLVDP DVVVSHSASL IRSNRHIVKA EDAEQYMMVS RERVGTTAER
     VLEDFNSRVI KPLKAKRRLQ IDVPYIDHPL HSMRSKTPER KENEEDSDSE IRSSDSSSDA
     EYGSDVEEEP DSCRRKKRTH KIQKADSSQT KVEEKERQNT LLRMGIERKR NHPNAIDPHI
     SYNEKGLGND SPECRCPFPI RNRGLKHGYY AGENQVLKCS KNDRANLHYY TLHVTPAPNE
     SQIQKTQMLI NGMEYHFEGF TMVTHAPLPD CMTRRPVFKY SIDYEFQLIE EFMPTECFDP
     EDCNSIFEYI FHDIFELLDF DLYPKHLPPG TASCPTIHIV PRFVAMENNT TFIWSSKTVL
     AFFLLHGKNN MFSPEDVEKN CAMSDDAFGR TIAKLKQSIV LNPMKKPSAL RADWFSRDLE
     NKEMFLIQNT IRSQNFASPF LPQIAALEKK MSRLKQEKKD SGNKNPHYEN LKAELIVLKD
     KHREARQLKL KLPVKDYIDT GLKPDVVAHV AMAIIASHHI RYNFSLSVFE KVIEYKFNDR
     RIVELALIHS SFRSYYGTTP DHVKNMISNC GYRKKYGAEE RREKKKGIIS LFNIMGGETS
     GGEPILHNER LEYLGDAVVE LIASHHLFFI LNHHFEGGLA TYRTALVQNR NLAKLAMNCR
     IDEMLQFAHG ADLINEAEWK HALANAFEAL MAGVFLDSGI APCDAIFSKA MYGKDPEMKK
     VWDHLNEHEL KIEDPLGDRD LSRITPALTD FHRLEQIIGI EFNNIRLLAK AFTRRNVPFN
     DLTKGHNQRL EWLGDSVLQL IISDYLYRNF PLHHEGHMSL LRTSLVSNQT QSVVCDDLGF
     QEFVIKAPHR KNDLKMKDKA DLVEAFIGAL YVDKGLEYCR SFIRTVFCPR LKHFINSEKW
     NDAKSHLQQW CLAIRDSRNP NPAMPEYRLL GIQGPTNNRI FRVAVYFRGE RLSSAAASNM
     HTAELKAAEN ALAALEKASF SRMREKYMSG RQHRLHRIFF S
//