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Database: UniProt
Entry: B8NIA3_ASPFN
LinkDB: B8NIA3_ASPFN
Original site: B8NIA3_ASPFN 
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
//
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