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Database: UniProt
Entry: A0A0D2FQK3_9EURO
LinkDB: A0A0D2FQK3_9EURO
Original site: A0A0D2FQK3_9EURO 
ID   A0A0D2FQK3_9EURO        Unreviewed;      1429 AA.
AC   A0A0D2FQK3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Dicer-like protein 2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV04_10473 {ECO:0000313|EMBL:KIW62289.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW62289.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW62289.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW62289.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KN846963; KIW62289.1; -; Genomic_DNA.
DR   STRING; 5601.A0A0D2FQK3; -.
DR   HOGENOM; CLU_000907_4_6_1; -.
DR   OrthoDB; 342391at2759; -.
DR   Proteomes; UP000054266; 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   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; 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   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}.
FT   DOMAIN          33..212
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          378..539
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          569..664
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000259|PROSITE:PS51327"
FT   DOMAIN          935..1057
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          1110..1294
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1408..1429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1429 AA;  160489 MW;  609F7620D5D14224 CRC64;
     MDPDSDETWS DTSEEDGSRN APPLQSRAYQ IEMFEHSMMG NIIAVMGTGS GKTQVAKLRI
     EAELERSPGK LVWFTAPSVV LAYQQYRFLS QQLPAYQFRL ITGMDNAEYW TSLDIWQKVL
     YHIHVVVSTP AILQQALNRG FVVMKGISLL VFDEAHHCVK DSSMNSIMRH HYHPKLTQES
     SHELPHILGL SASPITKKKA KEVAELEGNL NAICKSPMQQ LEEYTVFVNM PEPLILAHSP
     APTQPSALLD ILTAAVCAVS IEHDPIVAAL RRSKHPHAQE KLEKIQKEQR TPAMEEMQTV
     VRSCTELQQS LGTWACDMFI KKCVEKVELM SSRKLDFAAA GALYTDRSAF MASTLQPLLI
     PLCMADLDLN TPGSVSSKVT LLVEFLQKGY QSNLRCLIFV KTKVAAWLLT DIINSHPLTQ
     GQYCAFSFVG VSNPTRRGIC DFAELSEQHD NLESFRNGEL NVCVATSVLE EGVDIPAMNL
     VICFDERPNF RSFIQSRGRA RQRESRFVMF SDTALKTKQW QALEDEMNDE CQKSLESVRQ
     REEMEGFSQT DSEVFRIPST GAILTFSEAR QLLDRFCAKL PNKDKSEPMA PIFLLKAEPG
     VELRAKVYLP SSLPPSLRIA ESRSSWLTEK KAKQDAAFQA YRALHEAGLV TDLLLPLERP
     KEQEVSRDGD ELEKRDSVYD VQKQYDPWPN VMKLWKSPGS CRVYAHRLQL EAPDCFYPSM
     LLLLPVRLSK LTFSLFTTKT SIVRVNIGAG VEKQGFPLDI AQDITFLLLT IMLRRRLTGL
     RKEQLPSLFV PDIQQSSLQT WYKAASASIP MTDFGQTNSA SCRSYLVQSR RRNVPFLWQP
     DAVHGDGQQA CDPQAREGPS SIRATVLPRT LDYSRQVNLP DSVHESVRDL PVDECSVLGL
     PSDYGCLVLF IPSIMHMLEV ALRSAAACEG PLTTIGLNNL DLVSEALTLP GASHTRNYER
     LEFIGDTILK FYAALHVFAD HPIYPAHHLT RMRGKIINNA RLQRATRLLG LDQYLSRNSF
     ATKEWTAGVS GLRPLVKQPS KELSSKTLAD VVEAVIGVAS VSGFEGGVSE EKVLATLKVF
     IDEVAWRPLS EIVAQIHTPD RVSEEPADIL APVEVMISYS FQNRGLLAEA LTQSSLAGDS
     RSTYDRLEFL GDSILDYIVC PKLFHSPLQL SPGQMTVRRH ALVSHQTLAF FAQKASCTRS
     IFRVDTDPRT EKSNVKEEHE TIYLTDYIRQ LGQPQAPRER QATLSAFCAI QPSVLKLLES
     GARFPWTLLS RLGAPKSFSD IIESILAAVF IDSKGNLGAC EAVLETIGYM SLVRRFVNER
     DIDTRHPEAK LHELIHSQDH RGTVPPLEII TQERKKRGAG DASWRCKVML DDKLIARTKH
     ASCADEARYT AVERAVEVLR KKTKREFTEV QKNGPEERHD EMRKKQMAF
//
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