ID A0A0D2DAE4_9EURO Unreviewed; 1351 AA.
AC A0A0D2DAE4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Dicer-like protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z517_11291 {ECO:0000313|EMBL:KIW74521.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW74521.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW74521.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW74521.1,
RC ECO:0000313|Proteomes:UP000053029};
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 Fonsecaea pedrosoi CBS 271.37.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN846976; KIW74521.1; -; Genomic_DNA.
DR RefSeq; XP_013278329.1; XM_013422875.1.
DR AlphaFoldDB; A0A0D2DAE4; -.
DR STRING; 1442368.A0A0D2DAE4; -.
DR GeneID; 25310781; -.
DR VEuPathDB; FungiDB:Z517_11291; -.
DR HOGENOM; CLU_000907_4_6_1; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000053029; 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; 2.
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:UP000053029};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00657}.
FT DOMAIN 15..188
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 339..504
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 534..630
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 908..1036
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1071..1256
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
SQ SEQUENCE 1351 AA; 153386 MW; AD7120F5DC322B4C CRC64;
MDQITARTRS YQLEMFERSM QENIIVAMDA GSGKTHILGY NRLTITLLIW FLAPHVALCE
QQYNALRIGL PSVRIKLLIG NDNVDRWSEQ RIWDAALDGV RVMVSTHKIL EEALAHSFVK
IKDLALLVFD EAHHCIRKHP ANKIMANFYY PKKSEHPDQV PHVLGLTATP IVRSKLHEMN
TVERNLDAIA VTTKLHRDEL FRFVHRPDLV PLVYKIDCLA NASTALERLR QICSAQAVSP
APTDASRSKS IPQPPWKEQL AKFRTKAHHV LNELGPWATD LFILGSIKVL EKSGGHNTSL
LFSWTDQEHR VLTKLLCKDP VLSQLQYDIA PSHNNVSKKM ACLLSFLGSR DASQSTAIIF
VQQRVITGLL SQLLSAHPST SGSFQCAAFV GMSQNRGKKY NLPELLDMKE QLQTLASFRA
RAKNVIVATN ALEEGIDVRA CNLVICFDLP QNLKSFIQRR GRARQEKSVF ALMFSEEESQ
DRLAEWKTLE EDLQRLYQDA SRLRVTTLHL EQSERVDYSL KSSTTGATLT AEDTMAHLHH
FCAKLPVEPF SDMRPMFSYK QEPPGSEEIT AVVTLPNCVD ASVRVATSLH KWKTEKNAAK
DAAFQAYAGL YSAGLLNENL LPLSHDFEMQ LDVLDKLGSQ VDIDLEYSPW QLVAQAWSST
YVYDLAVQFN FHERTERPPV TMKLAFPCEL PDLQPLRVQL TADATVYMTF QHDRRRRFIT
PTDRDLMRKV THIISRSTHS DYSSDDRIDF LALFAPVMED MMLQTWLTAN KGRIKALELV
SVSRSLIPRG FVRHTTEGRQ PQIFNSWTVN KDTATSNLHQ ITCTPLPSRR NFRISPPENS
GAGKLKIRSD NKEEHPKLNY YPLEECTIDR LPVGIARLNL LLPTILQHIA NAWIADRMCQ
TVLKEIPFRS LDLVITAITP PSVQWCTNYE TLEFLGDSIL KLVVSIQLYD RHKNWPEGYL
TLKRAVLVSN QYLAKAALKA GLSAFIRTTP ISWKRWSPIF ISDMMAKSSC AARTVRMKVL
ADVVEALIGA AFVDGGFGSA ETCIRHLLPG LDNEKLSFAV QTDKGQMIAN QDRFESVIGY
EFRHPCLLVE ALTHPSCERD RFSQSYQRLE FLGDAVLDSI IASQLMTHKV SSRSPGVMTR
VKSAMVNAHL LGFFCMEFYR TEEFEFVQQQ QPDGKFNIET ETTNIYLWQL MRSHNDVVRD
RRIDSLDRFE KLGGSIRRQL DDSSEYPWLD LSMLRPEKFF SDIIESLVGA IYVDSKGSLE
KCSTWLDYIG LIKYLRRVLD ENIDVVHPRT KVDWKTGAQT TEYKVSKMAD PAEKFQCILL
VDEKTCVQVD GYDTSDVAIV AAAQKALSIL P
//
