ID B8NIA3_ASPFN Unreviewed; 1339 AA.
AC B8NIA3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=RNA helicase/RNAse III, putative {ECO:0000313|EMBL:EED49777.1};
GN ORFNames=AFLA_065990 {ECO:0000313|EMBL:EED49777.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED49777.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED49777.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963479; EED49777.1; -; Genomic_DNA.
DR RefSeq; XP_002380158.1; XM_002380117.1.
DR STRING; 332952.B8NIA3; -.
DR EnsemblFungi; EED49777; EED49777; AFLA_065990.
DR VEuPathDB; FungiDB:AFLA_008535; -.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_6_1; -.
DR OMA; CCVNLIR; -.
DR Proteomes; UP000001875; 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; cd18034; DEXHc_dicer; 1.
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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EED49777.1};
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 23..203
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 368..531
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 561..655
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 925..1052
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1081..1237
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT COILED 516..543
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1339 AA; 151400 MW; F2C855535A1874BB CRC64;
MAQLNGSNGT GLLYKPRQYQ YEMFEASLKE NIIVAMDTGT GKTQIALLRI AHQLEGGGPQ
KLTWFLTPTV ALCLQQYEVI RSHLPAVRAC TITGLDKVER WKSQYIWDEL LKDKQVVVST
HAVLFEALTH GFVRISQLGL LIFDEAHHCM RRHPANMIML DFYHPTLRKH GRDSVPCILG
LTASPVVRSK SQEMKTLESN LDSICKTPQV HKQELTTYAH RPELLPIIYK AIDEGPGGRA
LQALEHAWDT ADIDGDPDAI PQNGSLLNGS GEYKALMVRK TLCNEQIKRF VDRSRHIFAE
LGEWAADYYI CTSVEQLRTT IRDQSLTMDW EDEERAYLSN FLSKLPVAEV QANLADPNNF
TMSPKLAALI NFLDKFDDPE FSGLIFVKQR VTVSVLARLL SLHPQTRDRF RCAAYVGMSV
GSCRQDMVGD WHNAKKQRGT MDDFRSGRKN LIVTTSVLEE GIDVTACRVV VCFDKPANLK
SFIQRRGRAR QQKSTYAIMF STADEHGDLR RWQILEQAMV EAYQDEERRL REAEAQEAVD
ENVPEMITVE ATGAVITPDS VVTHLYHFCA VLPEERYVDN RPEFSFEKDR QGLIKGTVIL
PSCVHPKVRR IQGKLWWKSE RAAVKETAFQ AYRALYEFGL LNDHLLPLTK NPEMRPTDHT
TLPSLLDVSE QYDPWTDWAN SWSCPDVHQM RIALESNGHP ADGLIMKLIG PTNLPPLAPI
TLFWDRDTRL TLSFDVPERI TTVTDNCIAN MRTVTALYIQ APRSRNLLNN DDFVTLFGPD
LPSTELADWL LRNAGYETAH EAYSRGTMPG TMGIIRDLSR YDEPFFCHRW IESETGLIEI
ECRPIPRRRN FLHPPALDNG QADAIVESEH GSAKVHMVAA ESCTVDKLPV STAIFGLFIP
HIVDRLESTL IANRLCATIL CDVGFADIQH VITAIMAPSA QGVTNYQRYE FLGDSILKYI
VSCQLFFQNL NWPEGFLTEG RTTIVQNPRL TRAALDAGLD SFIITKALTP RRWIAPLIST
RVGAAPVKRQ MSAKVLADVI EALIGAAYLD GGHSKAQICT HCFLPEVNRQ PLDIPSLITQ
TEHGRTARQI IDEFLGDAIL DMVIVPIIFQ YSNKISPGDM TLIKHAVVNA NLLGFFCMEF
SIEQDKTKVE KTPDGRFAVK SETQHVELWR FMRFNSLDLQ TSRDAALDRH RRLRNKILTS
LYHGPSYPWQ SLSQLYADKF FSDIVESVLG AIYVDSGGDL SACERFLEQI GLLSYVRRVL
LDGINVTHPR NIAQRLSKGD ALFNLRRVSD EKGRSMYRCT VTMNDAQIVL VEGCQCGEEA
EVRAANETIE FLQRRQEVV
//