DCL1_CHAGB
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 03-AUG-2022, entry version 81.
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 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; 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 globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- FUNCTION: Dicer-like endonuclease involved in cleaving double-stranded
CC RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs
CC (siRNAs) which target the selective destruction of homologous RNAs
CC leading to sequence-specific suppression of gene expression, called
CC post-transcriptional gene silencing (PTGS). Part of a broad host
CC defense response against viral infection and transposons (By
CC 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};
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DR EMBL; CH408032; EAQ88115.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001223948.1; XM_001223947.1.
DR AlphaFoldDB; Q2H0G2; -.
DR SMR; Q2H0G2; -.
DR STRING; 38033.XP_001223948.1; -.
DR PRIDE; Q2H0G2; -.
DR EnsemblFungi; EAQ88115; EAQ88115; CHGG_04734.
DR GeneID; 4392482; -.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_3_1; -.
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:0031047; P:gene silencing by RNA; IEA:UniProt.
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 Gene3D; 3.40.50.300; -; 2.
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; 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; Helicase; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; RNA-binding; Zinc.
FT CHAIN 1..1607
FT /note="Dicer-like protein 1"
FT /id="PRO_0000306778"
FT DOMAIN 142..324
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 461..632
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 665..755
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 1063..1219
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1272..1447
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1478..1556
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 267..270
FT /note="DEAH box"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1570
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT SITE 1429
FT /note="Important for activity"
FT /evidence="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
