ID A0A1V6V796_9EURO Unreviewed; 1348 AA.
AC A0A1V6V796;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Dicer-like protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENCOP_c001G02810 {ECO:0000313|EMBL:OQE46516.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE46516.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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 -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000256|PROSITE-ProRule:PRU00657}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE46516.1}.
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DR EMBL; MDDG01000001; OQE46516.1; -; Genomic_DNA.
DR STRING; 36646.A0A1V6V796; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000191500; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00593; RIBOc; 2.
DR CDD; cd18802; SF2_C_dicer; 1.
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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
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; DICER-RELATED; 1.
DR PANTHER; PTHR14950:SF37; ENDORIBONUCLEASE DICER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF03368; Dicer_dimer; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00657}.
FT DOMAIN 1..176
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 338..514
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 531..625
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 892..1022
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1061..1244
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
SQ SEQUENCE 1348 AA; 151340 MW; 38C1FB2BCB8BA4DF CRC64;
MDSTGLSGDG AAYRSRGYQL EMLEASRKEN IIVALVWFLA PTVALSLQQH EVITSQILSV
KTKVLTGLDN VDRWTEQGVW DKVLKDVRVV VSTYAVLADA LGHGFVRMSR LSLLIFDEAH
HCTRRHPANK IMQNHYHPTL LRSGPNAVPR ILGLTASPVV RSSNNELETI ESNLNAVCRT
PRVHRTELLE NTHLPHLERV NYIPFDEAQY GFGSQLLSSL IECCRAYNIE DDPWIESLRS
KGQTAELTKA LTAGKTFCSE QLRMFQARSR HIYEELGGWA ADFYISASID ELQRSIQDAS
EMSRLDQMER VYLLELLLAM PAAGSAEESY HISIKLEMLV DFLQKADKPG FSGLLFAKQR
ATVSMLARIL SLHPKTRDRF QCAAYVGWAS DRSRKGCLGD LLHRDMQRDT LDEFRAGRKN
LIVATDVLEE GIDISACSVV ICFDKPANLK SFVQRRGRAR HRESTYAVMI SNEDELLALH
KWQELEQAMI KAYQDDERQR RELYELETTE EDVKEILSVE KTSALLTADD AVQHLHHFCA
VLPVDEFSDN RPMFSFEENN VGLLLGTVTL PSSVHPTVRR AKGKSWWRTE RAARKETAFQ
AYKALYSYGL VNDNLLPLTR KPELRFSEQT TLPSIIPAAE QYDPYVELAQ GWASGQLCQT
RLKIYSNGSV DEDLAVSLIL PRSTPTPHPI SLYWEPETSL KLHFDLQIPN FETTAERLDQ
MRRITALYLH APSSRQRGDD RDFVALFVPD ISHERLGEWL AVYEGKEPAI EAYLRNPTSP
PTGIVRDQSK FSEPRTFSRW IVPAQVSKSS PIEIECCSLP RRRNLLQMRV ISVTEDGEAD
APKKSYVLPA SACVIDKLPA KQGLFGLLIS AILDRLEASL VAHRLNDTIL KGVGIQNIDH
VITAISAPIA QASTNYQRYE FFGDSVLKFT VSCQLFFRNT KWHEGYLSES RDKLIQNTRL
ARAALDTGID SFILTNRFTP RKWAAPLIRN KLDPSTAKRN ISTKVLADVV ESLIGAAYVD
GGIRKAQACL HRFLPEIDLF TNDISPHIFP EGKGVSSLID QHRLAGLIGY TFQDPALLTE
ALTHASCEYD TSTQSYQRLE FLGDAVLDMV VMAVIAAHPV EMDQGPMTLL KHSVVNANLL
AFFCMELCAS DIPSHTTQFV NGDVNLAPHY DQIHLWRFLR SHGPNIKSAR EACLERHEVL
RGEICDALEH GTQYPWELFA RLRADKFLAD IIESVLGAIF IDCGGDLDAC HAFVERIGLV
WYIQRVIADG VNVVHPRNTA QNMVKGAGTL VFKRKRVESG GVATYRCSAV VNQTEIALVE
GCASAEEAEV KVANVAIEHL TLHPIVSA
//
