ID A0A0D2C2K0_9EURO Unreviewed; 1579 AA.
AC A0A0D2C2K0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Dicer-like protein 1 {ECO:0000256|ARBA:ARBA00020797};
GN ORFNames=PV06_05017 {ECO:0000313|EMBL:KIW43972.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW43972.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW43972.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW43972.1,
RC ECO:0000313|Proteomes:UP000053342};
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 Exophiala oligosperma CBS72588.";
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 -!- 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};
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DR EMBL; KN847335; KIW43972.1; -; Genomic_DNA.
DR RefSeq; XP_016264188.1; XM_016405982.1.
DR STRING; 215243.A0A0D2C2K0; -.
DR GeneID; 27357091; -.
DR VEuPathDB; FungiDB:PV06_05017; -.
DR HOGENOM; CLU_000907_4_3_1; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000053342; 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:0004525; F:ribonuclease III activity; IEA:InterPro.
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; 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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 121..301
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 441..606
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1097..1216
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1270..1422
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1474..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1579 AA; 179590 MW; F106854B997C6FAC CRC64;
MWARKPKPKP KSEEPSTEEL LMTLMDDPAS TDNQQGIQLS PESDLMDLNA DEADEVAESD
EESQDGSSFS TTAAEVTKEA DKAILKEHIR KQASNERHVT SSDNAESDSI INRARDYQQE
LFERAMDENV IAVLDTGSGK TLIAALLIRH FLEQELFDRN NGKPHKIVFF LVNSVHLARQ
QTRFLNNNLP HNAMALFGET NEDLWKKAQW EDIFVKNRVI VCTAAILDQC LMHSFLTIGQ
ISLLIFDEAH HCKKSHPYAI IIRDYYLKWK GEKPRIFGMT ASPVDSKRDI SRVTSELEEL
LQSKIITTKD ASVFEFAPRA RDIRWTYSPM RMEFDTELTH SLRPLCGFIE DLQKYFTFSK
YAARQLGTWA ADRVWKYAIA VTDHGATAVI RKFEQSKVYN EDSDSDRRRA KLAKAQQAFS
LVRGHYFGPP RFDVDREVSP KVKCLFTELE RRFAESKATR AIVFVAQRIT AYILCDLFES
SAIPNLRPGV LVGVHPQSIE SSHWRDQATV MDQFRSGIIN VMFSTSVAEE GIDIPQCNLV
VRFDLYDTPI QYMQSRGRAR MKNSEYAHMI EKGNQSHVST VNYAIEMDEY IRLFCQSLPP
DRLLGSGTKL KQLMAKDASC PRFKTPTGAV ASHTNSLLLL SRYVDSLERV EARSREIYEE
IIDAEKNTFQ YKVILPTTND PRAAQVKGAL GDHKANKVLA RRSAAWRCCV KLRKAELLDT
NLDSVFGKVK PHNHNARLAV DERKEIYPKK LKPDFWRDSG VGTESLPAKL FVTRVAVGTL
STSTATNSLL LFTRAPLPTI PKFPVFVDEN VEKSIFFDRM QEPVQINERQ IQALTDFTVN
AVLKDLFQKT FASDPNFMSY WLAPPACTPL GSSFETFVNM DELLLAGHTQ RRRWIPATSP
DDGLKQAAEW CQAFLVDPGS GKFRYFTRNI DHAKTIWDVP PEPSIRLGKK FKNSIIAFSD
STYGKRRKDA ALCATRYDPY QPVIKAKVVL AGRNFLQKYG PGEQRFDECD IAPQPLNIGR
ISVDTAVFGQ MWPSILHRLE SYLIVREPYL KLGLPEVPLD LALESFTMEN SAITDITTAG
EPGVDESDAL PKKAPLNYER LEFIGDSLLK MMTTIAVFIH TTCNEEGMHC KRMEMLANRR
LCSTASKPEY ELFQYIRAAS EPHWATTWYP EFIEQIPDRA ERRIVVKSGF KSHPLGMKTI
ADVCEAMIGA CIMTSQNLPV EEKLDLGIRA ITKLVDDPYH DFQSWRDVRA LYKRPTWCLQ
MNDPVADDLA TTVEQITGYK FKYPRLLRSA FTHSSDQNST VPDLQRMEFL GDACLDWVSI
WWLFSKNATR GPQWLTEHKM AMVSNRFLSA LAVVLGFHKL IYAESMKVYE DIGRYSAMVQ
EKYEQGPVER DFWTRLDPGS SPPKALADLV ESYLGAVLLD SNFNLREIEI FFEKHVKWFF
ENIETYDSFA KLHPTTHLLK LLIHRFQCHD NSSTTIEETT TTTTRGDHDE DDDDEGAGDQ
SIGGITAHVA WIVHGRVVAT GKGHGVGCAK LKASRVALKI LSKLSVDEFR RKWGCNCDLR
CKGSKKKGDR TDVMHDEVE
//
