ID W6Q961_PENRF Unreviewed; 1488 AA.
AC W6Q961;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Dicer-like protein 1 {ECO:0000256|ARBA:ARBA00020797};
GN Name=dcl1 {ECO:0000313|EMBL:CDM30739.1};
GN ORFNames=PROQFM164_S02g000889 {ECO:0000313|EMBL:CDM30739.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM30739.1};
RN [1] {ECO:0000313|EMBL:CDM30739.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM30739.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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.
CC {ECO:0000256|ARBA:ARBA00025403}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000256|PROSITE-ProRule:PRU00657}.
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DR EMBL; HG792016; CDM30739.1; -; Genomic_DNA.
DR STRING; 1365484.W6Q961; -.
DR OMA; YHVNRMC; -.
DR OrthoDB; 342391at2759; -.
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:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; cd18034; DEXHc_dicer; 1.
DR CDD; cd00593; RIBOc; 2.
DR Gene3D; 3.30.160.380; Dicer dimerisation domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 2.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_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 PANTHER; PTHR14950:SF62; DICER-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR14950; DICER-RELATED; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 2.
DR PROSITE; PS51327; DICER_DSRBF; 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 {ECO:0000256|ARBA:ARBA00023118};
KW Antiviral protein {ECO:0000256|ARBA:ARBA00022721};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00657}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 86..267
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 403..569
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 602..692
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 1002..1154
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1205..1356
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1488 AA; 168531 MW; 5260FC94D31E9A4D CRC64;
MEAEDTSSDL SGDEAATPQL KVSHRHRTQN AMFNALLEDH VVNGPKDGPN ASHIELSDAE
LSTARLLANT EPGGGVLDPR EYQIELFERA RASNTIAVLD TGSGKTLVAV LLLKHILQIE
LNKRANGASP RVAFFLVDSV TLVFQQSAVL RNNLDQRVAH FYGNLGPDLW DQQTWNKHLE
KYMVIVCTAE ILNQSLLNGH IRIDQINLLI FDEAHHAKKE HPYARIIRDS YLKADPEKRP
RIFGMTASPV DAKCDIAEAA IQLETLLDSR IATTSDLTLL RNFVNKPMEE EWVYDKLPPP
FETNLHGTLK VKYGDMPILE GAFRFASVAS SELGAWCADQ VWALALADEV LPKLEGSIGK
VTDSDPQDSE KASEDIKRIQ EANQLVKEYI ENQAFTPADL SSKVELLMRK LQEQFAKSPD
TKCIVFTQRR NTAKIMLQLC EKLQLPNLRP DALVGVRKGD ALGMNSTFRR QFLVLVKFRK
SEVNCLFATS VAEEGLDIPD CNLVQRFDLF DTVIQYVQSR GRARSADSVY ATMVESGNHN
HSMRLQEVRR AEHLMKNFCN LLPENRKLYG ADHDTKGLIH EEDRKRTYTI PNTGAMLTCR
HAIGVLARFA SSLQYENEIS ASVTYIVMSE NESFSCEIIM PEKSPVRRVI GRSESKKSLA
KQSAAFDACM LLRQKNLLDE HFNSIYHKRL PAMRNAKLAI TSKRTDQYRM RTKPSIWARL
QGTVPTRLYA IVIRLIPSKP LARAHGSIVL LTRERITTIP TFPVFLDKDI ETTVQSLCID
DGLEVASKDL EYLTVFTLAV FHDVFHKTYK HVSEQFPYWL APAREDVDIG TSTSIFDIID
WEALQYVRDN PKLMWSSDME PESLLTRFIY DDWNGKYRYF PLAIDPNLRP SDPPPSYAPS
RKWSDNIMNW SLSLSKNSRP KFFNRCIWTQ PVFQAELICL RRNFLDKAAE EEKASNSRCV
ICPQPLAISA ISTSVAATCF VFPAIITRME SYLIAQEGCN MLGLGGIKLE YALEAFTKDS
DNTEEHRSLQ IHVQRGMGKN YERLELLGDS VLKMATSISL FIQNPEDDEY DYHVNRMCLI
CNKNLFRNAI ELKLYEYIRS RGFSRHMWYP PGLSLEYGRD HAKFFASEGK HSLAEKTIAD
VCEALIGASL LSGGDDNRYD MAIKAVTVFV NSHNHTATSW EDYLSAYSMP LYQNRAADGF
EKNLAQQIFE KVGYEFKYPR LLRSAFTHPS YPLAWAKVPC YQRLEFLGDA LLDMVCVEHL
FHRFPNRDPQ WLTEHKMAMV SNKFLGALAV KLGLHVHLQH FSNPLMIQNN KYAEEIQLAE
SEGNGEVDYW LSTSDSPKCL PDMLEAYLGA IFVDSGFDFT VIEAFFNMHI LPFFHDMSIY
DTFANRHPTT FLHSQMTHSY QCTDYCLKSA EVPAVEGETP RVFAAVMVHG QSIASAVASS
SRYAKVRAST RALAVIDGMS LSEFREKYHC ACQGGQATVD RASIGTAI
//
