ID DCL2_ASPCL Reviewed; 1389 AA.
AC A1C9M6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=Dicer-like protein 2;
DE Includes:
DE RecName: Full=Endoribonuclease dcl2;
DE EC=3.1.26.-;
DE Includes:
DE RecName: Full=ATP-dependent helicase dcl2;
DE EC=3.6.4.-;
GN Name=dcl2; ORFNames=ACLA_055980;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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 (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00657}.
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DR EMBL; DS027048; EAW13550.1; -; Genomic_DNA.
DR RefSeq; XP_001274976.1; XM_001274975.1.
DR AlphaFoldDB; A1C9M6; -.
DR SMR; A1C9M6; -.
DR STRING; 344612.A1C9M6; -.
DR EnsemblFungi; EAW13550; EAW13550; ACLA_055980.
DR GeneID; 4707091; -.
DR KEGG; act:ACLA_055980; -.
DR VEuPathDB; FungiDB:ACLA_055980; -.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_6_1; -.
DR OMA; IMNEEID; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000006701; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; Antiviral protein; ATP-binding; Helicase; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1389
FT /note="Dicer-like protein 2"
FT /id="PRO_0000306785"
FT DOMAIN 23..203
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 368..537
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 564..658
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 920..1060
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1099..1282
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT MOTIF 144..147
FT /note="DEAH box"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 1264
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1389 AA; 156806 MW; EA8AAF2FA35F7D55 CRC64;
MSSAVPTNSD AAAYQARNYQ LEMLEASMKE NIIVAMDTGS GKTHIAVLRI KAELDSCPPD
KIIWFLAPTV ALCTQQHKVI ASNLPAVQTR TLTGLDKVEL WTEQAIWDAI LKDVRVVVST
YAVLADALSH GFMRMSRLAL IIFDEAHHCM RKHAANKIMQ DFYHPTVSKF GPSAVPRIMG
LTASPVVRSN REELFTIETN LDAVCKTPRA HRQELLKFSH RPELKQLLYE PPDPMGLQVS
SQTLRALIEA WETLDIEDDP YVKRLRKSSL DGGALEKALM TGKTFCREQL KRFVDRSRHI
FEELGEWAAD YYIYTSIQHL KTRVQTSYMT GDWDEAERAY LVSFLSKLPA ADIQITLSDA
ACLRISPKLE ALIGFLDAMD DPEFSGLIFV KQRATVSVMT DLLAVHPRTR ERFRSAAYVG
WSNSSGSKDF LGNLLSMHGQ LSTLDDFRSG HKNLIIATDV LEEGIDISAC SVVVCYDKPP
NLKSFVQRRG RARQKQSTYA IMFPAEDSAF DLAKWQTLEQ AMIEAYQDDE RHLQSAIELE
RVNEEVVERF TVESTSAVLT ADTAMAHLHH FCAVLPSQPY VDMRPVFSVE TDIANLRRGI
VILPNCVHPK VRRSEGQRWW RTERAAMKEA AFQAYKSLYE FGLVNDNLLP LTNKPELKVN
KLGSIPSIME ASEQYDPWVD WAYSWSSPDI HQSRVVVRLN GAKDRELCMR LAGPTVLPPL
APMTLFWDSE TTFTVAFEAP ERVPHVPLSS VEDMRTSTVV YLQATSSRLL STKQDFTALF
GPDLPHTDLK AWLQMYEGNE PAVEVYSRRR DPMLMGVVRD CSRYNEPLLF RRWVESGDSP
TTSVVEMECD PFPRRRNLLH RQTLATKKLE NDKEDTPEPV NKMRTVAADQ CTIDRLPFSN
AILGLFISVV VQQLETELIA TKLYETILRD VGFTSTQHII TAISAPSAQA LTNYQRYEFL
GDSILKFSVS CQLFFKHPNW HEGYLSEGRD EIVQNPRLTK AALDTGLDAF VITKMFTPRK
WSAPLISERL ERVAGKRQVS SKVLADVVEA LIGAAYMDGG HAAAQACIRR FLPEINLHSL
DTRTLSRSVA PEGARQTIHD RLKRHISYTF ENESLLVEAL THPSCDYDAS TQSYQRLEFL
GDAVLDMIIV SAIFNHPVQM PQGHMTKIKH ALVNANLLAF LCMEFAIPEE RASVEQISTL
QFEVISNEEL VELWRFMRYR GLDLNNARDA SLARHRALRD EILHSLQHDP HYPWQALSRL
SADKFFSDIM ESILGAIFVD SGGDLAPCEA FVERIGLMSY LRRILDENIE VTHPRNVAQQ
LAKSNIQFLA QRMPDEEGGA SYQCAVRIEE VEAFVVRGCL TAEEAEVTAA IDAIDLLMER
VNGSASVAS
//
