ID DICER_CHICK Reviewed; 1921 AA. AC Q25BN1; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 3. DT 23-FEB-2022, entry version 103. DE RecName: Full=Endoribonuclease Dicer; DE EC=3.1.26.3; GN Name=DICER1; Synonyms=DICER; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=15247924; DOI=10.1038/ncb1155; RA Fukagawa T., Nogami M., Yoshikawa M., Ikeno M., Okazaki T., Takami Y., RA Nakayama T., Oshimura M.; RT "Dicer is essential for formation of the heterochromatin structure in RT vertebrate cells."; RL Nat. Cell Biol. 6:784-791(2004). CC -!- FUNCTION: Double-stranded RNA (dsRNA) endoribonuclease playing a CC central role in short dsRNA-mediated post-transcriptional gene CC silencing. Cleaves naturally occurring long dsRNAs and short hairpin CC pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three CC nucleotides with 3' overhang of two nucleotides, producing respectively CC short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs CC serve as guide to direct the RNA-induced silencing complex (RISC) to CC complementary RNAs to degrade them or prevent their translation. Gene CC silencing mediated by siRNAs, also called RNA interference, controls CC the elimination of transcripts from mobile and repetitive DNA elements CC of the genome but also the degradation of exogenous RNA of viral origin CC for instance. The miRNA pathway on the other side is a mean to CC specifically regulate the expression of target genes (By similarity). CC {ECO:0000250}. 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; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Component of the RISC loading complex (RLC), or micro-RNA CC (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and CC TARBP2; DICER1 and TARBP2 are required to process precursor miRNAs CC (pre-miRNAs) to mature miRNAs and then load them onto AGO2. Note that CC the trimeric RLC/miRLC is also referred to as RISC (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00657}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator. CC {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; AB253768; BAE87103.1; -; mRNA. DR RefSeq; NP_001035555.1; NM_001040465.1. DR SMR; Q25BN1; -. DR STRING; 9031.ENSGALP00000036777; -. DR PaxDb; Q25BN1; -. DR GeneID; 423437; -. DR KEGG; gga:423437; -. DR CTD; 23405; -. DR eggNOG; KOG0701; Eukaryota. DR InParanoid; Q25BN1; -. DR OrthoDB; 1337630at2759; -. DR PhylomeDB; Q25BN1; -. DR PRO; PR:Q25BN1; -. DR Proteomes; UP000000539; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016442; C:RISC complex; ISS:UniProtKB. DR GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB. DR GO; GO:0030422; P:production of siRNA involved in RNA interference; ISS:UniProtKB. DR GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; ISS:UniProtKB. DR CDD; cd10843; DSRM_DICER; 1. DR CDD; cd00593; RIBOc; 2. DR Gene3D; 1.10.1520.10; -; 2. DR Gene3D; 3.30.160.380; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR038248; Dicer_dimer_sf. DR InterPro; IPR005034; Dicer_dimerisation_dom. DR InterPro; IPR044441; DICER_DSRM. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003100; PAZ_dom. DR InterPro; IPR036085; PAZ_dom_sf. DR InterPro; IPR000999; RNase_III_dom. DR InterPro; IPR036389; RNase_III_sf. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF02170; PAZ; 1. DR Pfam; PF04851; ResIII; 1. DR Pfam; PF00636; Ribonuclease_3; 2. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00358; DSRM; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00949; PAZ; 1. DR SMART; SM00535; RIBOc; 2. DR SUPFAM; SSF101690; SSF101690; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF69065; SSF69065; 2. DR PROSITE; PS51327; DICER_DSRBF; 1. DR PROSITE; PS50137; DS_RBD; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50821; PAZ; 1. DR PROSITE; PS00517; RNASE_3_1; 1. DR PROSITE; PS50142; RNASE_3_2; 2. PE 2: Evidence at transcript level; KW ATP-binding; Cytoplasm; Endonuclease; Helicase; Hydrolase; Magnesium; KW Manganese; Metal-binding; Nuclease; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing. FT CHAIN 1..1921 FT /note="Endoribonuclease Dicer" FT /id="PRO_0000373984" FT DOMAIN 51..227 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 433..602 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT DOMAIN 630..722 FT /note="Dicer dsRNA-binding fold" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657" FT DOMAIN 891..1042 FT /note="PAZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142" FT DOMAIN 1277..1404 FT /note="RNase III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177" FT DOMAIN 1665..1823 FT /note="RNase III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177" FT DOMAIN 1848..1913 FT /note="DRBM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT NP_BIND 64..71 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT REGION 409..433 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 727..746 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1270..1289 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1782..1801 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 175..178 FT /note="DECH box" FT COMPBIAS 412..427 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 1317 FT /note="Magnesium 1" FT /evidence="ECO:0000250" FT METAL 1396 FT /note="Magnesium 1" FT /evidence="ECO:0000250" FT METAL 1399 FT /note="Magnesium 1" FT /evidence="ECO:0000250" FT METAL 1704 FT /note="Magnesium 2" FT /evidence="ECO:0000250" FT METAL 1809 FT /note="Magnesium 2" FT /evidence="ECO:0000250" FT METAL 1812 FT /note="Magnesium 2" FT /evidence="ECO:0000250" FT SITE 1805 FT /note="Important for activity" FT /evidence="ECO:0000250" SQ SEQUENCE 1921 AA; 218610 MW; E1F9C9BE1D8CD611 CRC64; MKSPALQSLS MAGLQLMTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE LLEAALDHNT IVCLNTGSGK TFIAVLLTKE LSYQIRGDFN KNGKRTVFLV NSANQVAQQV SAVRTHSDLK VGEYSSLEVT ESWTKEKWSQ EFSKHQVLVM TCHVALTVLR NEYLSLSNIN LLVFDECHLA IQDHPYREIM KICEDYPSCP RILGLTASIL NGKCDPAELE EKIKKLEKIL KSNAETATDL VVLDRYTSQP CEIVVDCGPY TDKSGLYGRL LRELDEALHF LNDCNISVHS KERDSTLISK QILSDCRAVL VVLGPWCADK VAGMMVRELQ KYIKHEQEEL HRKFLLFTDT FLRKIHALCE EHFSPASLDL KFVTPKVIKL LEILRKYKPY ERQQFESVEW YNNRNQDNYV SWSDSEDDDE DEEIEEKEKP ETNFPSPFTN ILCGIIFVER RYTAVVLNRL IKEAGKQDPE LAYISSNFIT GHGIGKNQPR NKQMEVEFRK QEEVLRKFRA HETNLLIATS IVEEGVDIPK CNLVVRFDLP TEYRSYVQSK GRARAPISNY IMLADTDKIK SFEEDLKTYK AIEKILRNKC SKSVDTSETE TEPIVDDDDV FPPYVLRTDE NSPRVTINTA IGHINRYCAR LPSDPFTHLA PKCKTRELPD HTFYSTLYLP INSPLRASIV GPPMSCARLA ERVVALICCE KLHKIGELDD HLMPVGKETV KYEEELDLHD EEETSVPGRP GSTKRRQCYP KAIPECLRDS YPKPDQPCYL YVIGMVLTTP LPDELNFRRR KLYPPEDTTR CFGILTAKPI PQIPHFPVYT RSGEVTISIE LKKSGFTLSL QMLELITRLH QYIFSHILRL EKPALEFKPT EADSAYCVLP LNIVDDSSTL DIDFKFMEDI EKSEARTGIP STQYTKEMPF IFKLEDYQDA VIIPRYRNFD QPHRFYVADV YTDLTPLSKF PSPEYETFAE YYKTKYNLDL TNLNQPLLDV DHTSSRLNLL TPRHLNQKGK ALPLSSAEKR KAKWESLQNK QILVPELCAI HPIPASLWRK AVCLPSILYR LHCLLTAEEL RAQTATDAGV GVKSLPADFR YPNLDFGWKK SIDSKSFISI PSSSLVENEN YCKHSTIVVP ENAAHQGANR TSSAEKHDQM SVSYRTLLDE SPSKLQIDVS AELAAINGVS YNKNLANGNC DLVNRDFCQG NQLNYCRQEI PVQPTTSYPI QNLYSSENQP KPSNECTLLS NKYLDGNANR STSDGCPKMT VTTSTSTALN LSKDKVDSEK NTSSGYSSKT LGPNPGLILQ ALTLSNASDG FNLERLEMLG DSFLKHAITT YLFCTYPDAH EGRLSYMRSK KVSNCNLYRL GKKKGLPSRM VVSIFDPPVN WLPPGYIVNQ DKSNTDKWEK EETTKENLLA NGKLDYDDDD EEDEDLMWRL PKEETDFEDD FLEYDQEHIK FIDSMLMGSG AFVKKISLSH FSTTDSNYEW KAPKKSSLGN VPFSSDFDDF DYSSWDAMCY LDPSKAVEED DFVVGFWNPS EENCGVDAGK QSISYDLHTE QCIADKSIAD CVEALLGCYL TSCGERAAQL FLCSLGLKVL PVIKKTDWES TLCATGENCN SEQKNLSPNS VSACIVNSEP SLYKDLEYGC LKIPPRCMFD HPDAEKTLNH LISGFENFEK KINYSFKNKA YLLQAFTHAS YHYNTITDCY QRLEFLGDAI LDYLITKHLY EDPRQHSPGV LTDLRSALVN NTIFASLAVK YDYHKYFKAV SPELFHVIDD FVQFQMEKNE MQGMDSELRR SEEDEEKEED IEVPKAMGDI FESLAGAIYM DSGMSLEMVW QVYYPMMRPL IEKFSANVPR SPVRELLEME PETAKFSPAE RTYDGKVRVT VEVVGKGKFK GVGRSYRIAK SAAARRALRS LKANQPQVPN S //