ID DICER_CHICK Reviewed; 1911 AA. AC Q25BN1; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 16-JUN-2009, entry version 25. DE RecName: Full=Endoribonuclease Dicer; DE EC=3.1.26.-; GN Name=DICER1; Synonyms=DICER; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; OC Neognathae; Galliformes; Phasianidae; 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: Required for formation of the RNA induced silencing CC complex (RISC). Component of the RISC loading complex (RLC), also CC known as the micro-RNA (miRNA) loading complex (miRLC), which is CC composed of DICER1, EIF2C2/AGO2 and TARBP2. Within the RLC/miRLC, CC DICER1 and TARBP2 are required to process precursor miRNAs (pre- CC miRNAs) to mature miRNAs and then load them onto EIF2C2/AGO2. CC EIF2C2/AGO2 bound to the mature miRNA constitutes the minimal RISC CC and may subsequently dissociate from DICER1 and TARBP2. Also CC cleaves double-stranded RNA to produce short interfering RNAs CC (siRNAs) which target the selective destruction of complementary CC RNAs (By similarity). CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By CC similarity). CC -!- SUBUNIT: Component of the RISC loading complex (RLC), or micro-RNA CC (miRNA) loading complex (miRLC), which is composed of DICER1, CC EIF2C2/AGO2 and TARBP2. Note that the trimeric RLC/miRLC is also CC referred to as RISC (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily. CC -!- SIMILARITY: Contains 1 Dicer dsRNA-binding fold domain. CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC -!- SIMILARITY: Contains 1 PAZ domain. CC -!- SIMILARITY: Contains 2 RNase III domains. 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 IPI; IPI00818350; -. DR RefSeq; NP_001035555.1; -. DR UniGene; Gga.33735; -. DR Ensembl; ENSGALG00000010999; Gallus gallus. DR GeneID; 423437; -. DR KEGG; gga:423437; -. DR HOVERGEN; Q25BN1; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016442; C:RNA-induced silencing complex; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro. DR GO; GO:0031054; P:pre-microRNA processing; ISS:UniProtKB. DR GO; GO:0030422; P:RNA interference, production of siRNA; ISS:UniProtKB. DR GO; GO:0030423; P:RNA interference, targeting of mRNA for des...; ISS:UniProtKB. DR InterPro; IPR014001; DEAD-like_N. DR InterPro; IPR005034; Dicer_dsRNA_binding_fold. DR InterPro; IPR001650; DNA/RNA_helicase_C. DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N. DR InterPro; IPR001159; Ds-RNA_bd. DR InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd. DR InterPro; IPR003100; PAZ. DR InterPro; IPR000999; RNase_III. DR Gene3D; G3DSA:1.10.1520.10; RNase_III; 2. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00035; dsrm; 1. DR Pfam; PF03368; dsRNA_bind; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF02170; PAZ; 1. DR Pfam; PF00636; Ribonuclease_3; 2. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00358; DSRM; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00535; RIBOc; 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; KW Phosphoprotein; Repeat; RNA-binding; RNA-mediated gene silencing. FT CHAIN 1 1911 Endoribonuclease Dicer. FT /FTId=PRO_0000373984. FT DOMAIN 41 217 Helicase ATP-binding. FT DOMAIN 423 592 Helicase C-terminal. FT DOMAIN 620 712 Dicer dsRNA-binding fold. FT DOMAIN 881 1032 PAZ. FT DOMAIN 1267 1394 RNase III 1. FT DOMAIN 1655 1813 RNase III 2. FT DOMAIN 1838 1903 DRBM. FT NP_BIND 54 61 ATP (By similarity). FT MOTIF 165 168 DECH box. FT COMPBIAS 596 599 Poly-Asp. FT COMPBIAS 1405 1410 Poly-Asp. FT METAL 1307 1307 Magnesium or manganese 1 (By similarity). FT METAL 1386 1386 Magnesium or manganese 1 (By similarity). FT METAL 1389 1389 Magnesium or manganese 1 (By similarity). FT METAL 1694 1694 Magnesium or manganese 2 (By similarity). FT METAL 1799 1799 Magnesium or manganese 2 (By similarity). FT METAL 1802 1802 Magnesium or manganese 2 (By similarity). FT SITE 1795 1795 Important for activity (By similarity). SQ SEQUENCE 1911 AA; 217567 MW; 364D474B60E1A21E CRC64; 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 //