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 10-AUG-2010, entry version 34. 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 -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator. 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 ProteinModelPortal; Q25BN1; -. DR SMR; Q25BN1; 38-215, 43-554, 1293-1369, 1653-1915. DR STRING; Q25BN1; -. DR Ensembl; ENSGALT00000037569; ENSGALP00000036777; ENSGALG00000010999; Gallus gallus. DR GeneID; 423437; -. DR KEGG; gga:423437; -. DR CTD; 423437; -. 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:0046872; F:metal 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:production of siRNA involved in RNA interfe...; ISS:UniProtKB. DR GO; GO:0030423; P:targeting of mRNA for destruction involved ...; 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; 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 SUPFAM; SSF69065; RNase_III; 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 1921 Endoribonuclease Dicer. FT /FTId=PRO_0000373984. FT DOMAIN 51 227 Helicase ATP-binding. FT DOMAIN 433 602 Helicase C-terminal. FT DOMAIN 630 722 Dicer dsRNA-binding fold. FT DOMAIN 891 1042 PAZ. FT DOMAIN 1277 1404 RNase III 1. FT DOMAIN 1665 1823 RNase III 2. FT DOMAIN 1848 1913 DRBM. FT NP_BIND 64 71 ATP (By similarity). FT MOTIF 175 178 DECH box. FT COMPBIAS 606 609 Poly-Asp. FT COMPBIAS 1415 1420 Poly-Asp. FT METAL 1317 1317 Magnesium or manganese 1 (By similarity). FT METAL 1396 1396 Magnesium or manganese 1 (By similarity). FT METAL 1399 1399 Magnesium or manganese 1 (By similarity). FT METAL 1704 1704 Magnesium or manganese 2 (By similarity). FT METAL 1809 1809 Magnesium or manganese 2 (By similarity). FT METAL 1812 1812 Magnesium or manganese 2 (By similarity). FT SITE 1805 1805 Important for activity (By similarity). 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 //