ID A0A0M9WJ03_9EURO Unreviewed; 1352 AA.
AC A0A0M9WJ03;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Dicer-like protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACN38_g2334 {ECO:0000313|EMBL:KOS46715.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS46715.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS46715.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS46715.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS46715.1}.
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DR EMBL; LHQQ01000025; KOS46715.1; -; Genomic_DNA.
DR STRING; 229535.A0A0M9WJ03; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000037696; 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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000037696};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00657}.
FT DOMAIN 1..182
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 341..520
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 537..631
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 898..1028
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1067..1250
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
SQ SEQUENCE 1352 AA; 152507 MW; 474BEAC2A45B2D25 CRC64;
MLEASLKENT IVAMDTGSGK THIAILRIIH ELENCSSPDK LIWFLTPTVA LSLQQHEVIT
SQILSVKTKV LTGLDNVDRW TEQGVWDKVL KDVRVVVSTY AVLADALGHG FVRMSRLALI
IFDEAHHCTR RHPANKIMQN HYHPTLLRSG PNAVPRILGL TASPIVRSSQ NELETIESNL
NAVCKTPRVY RTELLENTHR PHLERLNYMP FNEAQYGFGS QLLSSLIECC RAYNIEDDPW
IESLRSKNQT VELTKALTTG KTFCREQLNN FQARARHIYE ELGGWAADFF ISASIDQLQC
SIQDASEMSH LDQMERIYLL ELLLAMPAPV SAEESSHISI KLEVLLNFLE KMDRPGLSGL
LFAKQRATVS VLARILSLHP KTRDRFQCAS YVGWSSDRNR KGCLGDLLHR DMQRDTLDEF
KAGRKNLIVT TDVLEEGIDI SACSLVICYD NPANLKSFVQ RRGRARHRES TYAVMISNEG
QLLSLHKWQE LENAMIKAYQ DDERQRREAF ELEAAEEHVK ERLWVEKTNA LLTADDAVQH
LHHFCAVLPV DEYSDNRPMF SFQENSAGLL LGTVTLPNSV HPTVRRANGK SWWRTERAAR
KETAFQAYKA LYSYGLINDN LLPLTRKPEL RFSEQTTLPS ILQVAEQYDP YVDLAKAWAL
GQLCQTRLKI YSNGSMDEDL AICLILPRLT PMPHPIPLYW DTETPLELHF EPQMSIFETT
EETLDQMRRI TTLYLRAPSS RQRGDNRDFA ALFIPDISHE HLGQWLAMYE GKEPALEVYS
RNPTTAPMGI VRDQSKFSEP RTFNKWIVPA QVTKASPIEV ECSSFPRRRN LLQVRTMNVT
DDGETDAPKK SYVLPAAACV IDKLPAKQGL FGLFISAILD RLEASLVAHR LNDTILKGVG
IENIDHVITA ISAPIAQAST NYQRFEFFGD SVLKFTVSCQ LFFRNTNWHE GYLSESRDKH
IQNNRLARAA LDTGIDCFIL TSRFTPRKWT VPLIRNKLEP STAKRNISIK VLADVVESLI
GAAYVDGGIR KAQACLHRFL PEIDLFTNEI SPLILPPGKG VSNLINHHRL AGLIGYTFKD
PALLTEALTH ASCEYDTSTQ SYQRLEFLGD AVLDMVVMAV IAAHPVEMDQ GPMTLLKHSV
VNGNLLAFFC MELCAPDEPS HMTQCANGEV SLIPHYDNIH LWRFLRSHGP NIKAAREACL
ERHQGLHIEI RDALEHGSQY PWELFARLRA DKFLSDIIES VLGAIFIDCG GNLDVCHAFV
ERIGLVWYIQ RVIADGVNVV HPRNIAQNMV KGAGTLVFKR KRVESGGTAT YRCSAVVNQT
EIALVEGCAS AEEAEVKVAN VAIEHLTLHP LA
//
