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Database: UniProt
Entry: Q2H0G2
LinkDB: Q2H0G2
Original site: Q2H0G2 
ID   DCL1_CHAGB              Reviewed;        1607 AA.
AC   Q2H0G2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   16-OCT-2019, entry version 72.
DE   RecName: Full=Dicer-like protein 1;
DE   Includes:
DE     RecName: Full=Endoribonuclease DCL1;
DE              EC=3.1.26.-;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase DCL1;
DE              EC=3.6.4.-;
GN   Name=DCL1; ORFNames=CHGG_04734;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC
OS   6347 / NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium
RT   globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- FUNCTION: Dicer-like endonuclease involved in cleaving double-
CC       stranded RNA in the RNA interference (RNAi) pathway. Produces 21
CC       to 25 bp dsRNAs (siRNAs) which target the selective destruction of
CC       homologous RNAs leading to sequence-specific suppression of gene
CC       expression, called post-transcriptional gene silencing (PTGS).
CC       Part of a broad host defense response against viral infection and
CC       transposons (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00657}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAQ88115.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAQ88115.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; CH408032; EAQ88115.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001223948.1; XM_001223947.1.
DR   STRING; 38033.XP_001223948.1; -.
DR   PRIDE; Q2H0G2; -.
DR   EnsemblFungi; EAQ88115; EAQ88115; CHGG_04734.
DR   GeneID; 4392482; -.
DR   InParanoid; Q2H0G2; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 2.
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; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF03368; Dicer_dimer; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF00636; Ribonuclease_3; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
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; PS00517; RNASE_3_1; 1.
DR   PROSITE; PS50142; RNASE_3_2; 2.
PE   3: Inferred from homology;
KW   Antiviral defense; Antiviral protein; ATP-binding; Complete proteome;
KW   Helicase; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat; RNA-binding; Zinc.
FT   CHAIN         1   1607       Dicer-like protein 1.
FT                                /FTId=PRO_0000306778.
FT   DOMAIN      142    324       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      461    632       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      665    755       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN     1063   1219       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1272   1447       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1478   1556       DRBM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00266}.
FT   NP_BIND     155    162       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       267    270       DEAH box.
FT   METAL      1312   1312       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1433   1433       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1436   1436       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1493   1493       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1527   1527       Zinc; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1568   1568       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1570   1570       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   SITE       1429   1429       Important for activity. {ECO:0000250}.
SQ   SEQUENCE   1607 AA;  181289 MW;  39C26A4BF0D8D922 CRC64;
     MNAEMREGSS ALPQLQAHSP VADNIDLMDI DEPASNGSFE ESPATPFDDD AFVNAGDTDQ
     EDDDPDTKKW IVNDSRKPRK ISEKKRADHA AFDVWIEENQ QDLSKGLDKF IVDDDGKTFQ
     SLIRDFENKR IITSPRDYQL ELFERAKTQN TIAVLDTGSG KTLIAALLLR WTIQNELEDR
     SKRLPKRIAF FLVDKVALVF QQHAVLACNL DYPLEKFCGD MVEDVTQDFW HKTFDENMAI
     VCTAEILYQC LTHSYIRMDQ VNLLVFDEAH HTKKNHPYAR IIKDFYAEVK DLNKRLRISR
     AMTASPVDAQ IDPKIARSPE LEGLLHSQIA TVADPTALHN SSTKLKREVT VEYGKCLPEF
     ETGLNRALKD LVGEHRLFQK PFAFTATAAS ELGPWCADRY WQLFFRGEEV VKLEAKTERE
     ILRKSAYSQE IAAQVNKVRE AHRLVGQHEF ASPSSDLLSS KVVILLRILR GEFRGVDHKR
     RCIVFVRQRN VASLLTDLLQ QPEMRIPGLE PGILVGGGRP EASYDNAKVT YRDQVLTIIK
     FKKGELNCIF ATSVAEEGLD IPDCNVIIRY DLNNTLIQYI QSRGRARQEG SIYIHMVESE
     NEEHVKKVCQ NQESEDALRK FCEALPADRK LTGNNFDMEY FLRKEKDQRQ YTVPETGARL
     NYKQSLICLA AFVASLPHPP EVNLTAGYLV LSVPGGYQCE VTLPESSPIR SATGKVYASK
     AVAKCSAAYE MCLMLIKGKY LDQHLRPTFT KQLPAMRNAR LAVSSKKKEQ YKMRIKPELW
     SVLGEPTELF AMALTLADPT ALARHSSPLL LLTRQPIPQI ASFPLYFGKN RSSAVHCVPV
     PGRVELDDNQ IQGLVAVTLA IFKDIFSKEY EATAAQLPYF LAPTLMQHGS DFTSVTDLSR
     IVDWGAVTFV RDNERVAYAL DDEADEFFKN KYVADPYDGS RKFFLRGRRH DMKPTDMVPE
     GIVTPGHRAW RVSCKTHDIL NYSLSAWSKS RAFLTPREDQ PVVEAEVLPI RRNLLDDHIG
     DDDLEPKPCF IVLEPLRISP LPVDLVAMAY NFPAIMHRID SNLVALEACK MLNLNVRPDL
     ALEAFTKDSD NSGEHDAEQI SFQSGMGNNY ERLEFLGDCF LKMATTISIF TLIPDKAEFE
     YHVERMLLIC NRNLFNNALE VKLEEHIRSM AFDRRSWYPE GLTLKKGKRK DLTRQHVLAD
     KTIADVCEAL IGAAYLTAQE QTPPNFDLAI RAVTVMVKDK NHTMTSYSDY YAAYSPPAWQ
     TAPCNSTQLD MAARFEARMG YAFTHPRLLR SAFQHPTYPS VYEKLPSYQR LEFLGDALLD
     MASVEFLFHR FPGADPQWLT EHKMAMVSNQ FLGCLAVYLG FHRAISYCAS AIQKEITEYV
     TEIEDALQSA RDDASKTPCN RHATTPSPGD LPAESFARDF WVRCSRPPKC LPDVVEAYVG
     AVFVDSRYDF ARVRAFFADH VRPFFEDMRL YDAFANKHPV TFLAGIMQGR MRCAEWRLLV
     KDLPPVVGAG AGTELETPQV VCAVRVHGLT LAHAVAASGR YGKIAAAKKA IQVLEGMDAE
     AFRKAYGCAC VLGEEEQQAA QTIATELEVF PAFSASGLEV AHHGSAV
//
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