ID A0A1W5DAN0_9LECA Unreviewed; 1321 AA.
AC A0A1W5DAN0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Dicer-like protein 1 {ECO:0000256|ARBA:ARBA00020797};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM40218.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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; FWEW01003658; SLM40218.1; -; Genomic_DNA.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000192927; 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: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; 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 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; 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 {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}.
FT DOMAIN 157..336
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 478..641
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 674..764
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 814..981
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1032..1183
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1214..1285
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1321 AA; 150265 MW; 8DD6C11D6CF5A930 CRC64;
MGVSIDIPYC RKEEQSHDEE SPAISRSSVE ESDIVPNSIF TLDSNEVLTH TSDKRPKRFT
DSGIEPSMED IEGYSTDSGS GDNNDAGPKS HRETERRRAQ NAIFNSWVAT CAERETKEEV
RAAAASAEDD QLSIRNLMSK QESTVIITDP REYQVELFEK AKRQNIIAVL DTGSGKTLIA
VLLLRFMLDQ ELTDRALGKR RRIAFFLVDC VTLVFQQFAV LECNLDQKVE RFCGDMGCDL
WKKEEWEKHF KENMVIVCTV EVLYNCLMHS FITIDQISLL IFDEAHHAKK NHAYARDFYL
AENDPAKRPK IFGMTASPVD ARVDVVQAAK ELETLLHSQI ATTSDLSLLR VSISRPDESI
AVYRKLVPPY ETSFCAEMKS KFGDLEGLSK LFQYSHEASS QLGEWCADQV WSLGLADEEA
GKVERKAERL FLAEKETRPI EVLDAEIAEL REAMSMVKNH TFVPPSTSGN STSPKVRFLQ
EYLQLVFEKP SDAKCIVFVK RRYTARLLGE LFARVGTPHL RLGILIGTRQ GEAGDIKVTF
RQQVVTLMKF RKGYLNCLFA TSIAEEGLDI PDCNLIIRFD LYDTLIQYIQ SRGRARHTNS
KYIHMIENGN KTHLQGIRDV RSGEVVMRRF CEALPADRLL QGNDCTLEGA LAKDRSMRTY
TEPLTGAKLT YGSSLSVLAH FVGCLPHDNE TILQATYIMN VENRQYICEV ILPQNSPIRS
AVGRPSSTKA IAKRSAAFEA CMLLRNGEYL DAHLLPTYHK HLPVMRNALL ALNMKKSNAY
DMRIKPDLWE ETRGAIPQLP TDVVAMAYMF PAIISRLESY LIVLEACSML HLDVKPHLAL
EAFTKDSDNT EDHRDEQIHY QRGMGKNYER LEFLGDCFLK MATSISLFSQ NPENDEFEYH
VKRMLLICNK NLYTTAVKTR LYEYIRSQSF SRRTWYPEGL KLLEGKGHKK TGKEIVKHHL
GDKTIADVCE AVIGAALLSW DGTANMDMAV KAVTALVASP DHDVSRWDDY YRLYTKPAYQ
LAQASASQLD LAAKVEQKHD YHFKYPRLLR SAFVHPSYPF SWEKVPCYQR LEFLGDSLLD
MACINFLFYR YPERDPQWLT EHKMAMVSNR FLGALCARLG FHKHIRYSSS LLELQIRDYV
TEIAEAEKES NGARDYWTAV KNPPKCLPDM VEAYIGAVFV DSEFNYSEVE RFFKTHIEWF
FEDMSIYDTF ANNHPTTYLN NLLTLTYGCT NYRVMANELP SCDGSPIRVI AAVMIHNEII
AEGTASSGKY AKVKASSNAL ELLKGLAPFE FRMQYRCNCT KAAEQDEGLG KKMEEVVGSA
I
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