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Database: UniProt
Entry: Q25BN1
LinkDB: Q25BN1
Original site: Q25BN1 
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   31-JUL-2019, entry version 94.
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;
OC   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: 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
CC       hairpin pre-microRNAs (miRNA) into fragments of twenty-one to
CC       twenty-three nucleotides with 3' overhang of two nucleotides,
CC       producing respectively short interfering RNAs (siRNA) and mature
CC       microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-
CC       induced silencing complex (RISC) to complementary RNAs to degrade
CC       them or prevent their translation. Gene silencing mediated by
CC       siRNAs, also called RNA interference, controls the elimination of
CC       transcripts from mobile and repetitive DNA elements of the genome
CC       but also the degradation of exogenous RNA of viral origin for
CC       instance. The miRNA pathway on the other side is a mean to
CC       specifically regulate the expression of target genes (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
CC         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.
CC       {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
CC       and TARBP2; DICER1 and TARBP2 are required to process precursor
CC       miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2.
CC       Note that the trimeric RLC/miRLC is also referred to as RISC (By
CC       similarity). {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}.
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   PRIDE; Q25BN1; -.
DR   GeneID; 423437; -.
DR   KEGG; gga:423437; -.
DR   CTD; 23405; -.
DR   eggNOG; KOG0701; Eukaryota.
DR   eggNOG; COG0571; LUCA.
DR   eggNOG; COG1111; LUCA.
DR   HOGENOM; HOG000001567; -.
DR   InParanoid; Q25BN1; -.
DR   KO; K11592; -.
DR   OrthoDB; 1337630at2759; -.
DR   PhylomeDB; Q25BN1; -.
DR   PRO; PR:Q25BN1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004530; F:deoxyribonuclease I activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
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; cd00048; DSRM; 1.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   Gene3D; 3.30.160.380; -; 1.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
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; PF03368; Dicer_dimer; 1.
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; Complete proteome; Cytoplasm; Endonuclease; Helicase;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   RNA-binding; RNA-mediated gene silencing.
FT   CHAIN         1   1921       Endoribonuclease Dicer.
FT                                /FTId=PRO_0000373984.
FT   DOMAIN       51    227       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      433    602       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      630    722       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      891   1042       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN     1277   1404       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1665   1823       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1848   1913       DRBM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00266}.
FT   NP_BIND      64     71       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
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. {ECO:0000250}.
FT   METAL      1396   1396       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL      1399   1399       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL      1704   1704       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL      1809   1809       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL      1812   1812       Magnesium or manganese 2. {ECO:0000250}.
FT   SITE       1805   1805       Important for activity. {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
//
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