ID   DCL2_EMENI              Reviewed;        1429 AA.
AC   P0C5H7; C8VIC3; Q5B8E1;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=AN10380;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBF83228.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA62953.1; Type=Erroneous gene model prediction; Note=The predicted gene AN3189 has been split into 2 genes: AN10378 and AN10380.; Evidence={ECO:0000305};
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; AACD01000052; EAA62953.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001306; CBF83228.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P0C5H7; -.
DR   STRING; 162425.CADANIAP00009879; -.
DR   EnsemblFungi; EAA62953; EAA62953; AN3189.2.
DR   eggNOG; KOG0701; Eukaryota.
DR   HOGENOM; CLU_000907_4_6_1; -.
DR   InParanoid; P0C5H7; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; 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:0031047; P:gene silencing by RNA; IEA:UniProt.
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; 1.10.1520.10; -; 2.
DR   Gene3D; 3.30.160.380; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF00270; DEAD; 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; SSF52540; 1.
DR   SUPFAM; SSF69065; SSF69065; 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..1429
FT                   /note="Dicer-like protein 2"
FT                   /id="PRO_0000306793"
FT   DOMAIN          21..200
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          335..501
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          528..622
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT   DOMAIN          874..1014
FT                   /note="RNase III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1056..1250
FT                   /note="RNase III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   MOTIF           141..144
FT                   /note="DEAH box"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         1095
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1236
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1239
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            1232
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1429 AA;  161279 MW;  252458B86DF397A7 CRC64;
     MASIPEERSA EHRARSYQLE MFEASLKGNI IVVMGTGSGK TQIALLRIIH ELENSDGKLI
     WFLAPTVPLC LQQHRVISQH IPAVKSRTLL GSDKVELWTE QAVWDAVLEG LQVIVSTPAV
     LHDAMTHGFV RISRLGLLIF DEAHHCIRKH PTNMIMRNFY HPALQEYGPG AVPRILGLTA
     SAGSSREGLQ TIEMNLNSVC TTPQAHRQEL LEYTHMPELR RVLYTPLMKE NASLWEGSTL
     QKLLERDNTY CSGQMKTFVC KAVHIFQELG IWAAEYFIRA SVEELLSHAY VHSKIDLDYD
     EREYLVNILS KSPVPDIDVH STDPKDFPVS PKFEALISFL MSTEDINFSG LIFVEQRAAV
     TVMSYLLSTH PSTRDRFRTG SFIGMSNSTN RKTMLGDLLS AKMQPDTLDD FRYGRKNLIV
     ATDVLKEGID VSACSVVICY NIPKGFESFI QRRGRARRQN STYSMMLSTE DDGSTLDKWQ
     KFEKIMEEAC LEDRRRTEEL RALGSLDEDV CTRFCVRSTG AILTAEYAMQ HLVHFCDTLP
     RQNYVEDKPE FSFERNDGGL LRAKVILPSS VNPKVRRAEG KAWWKTERAA KKEAAFYAYK
     ALYEHGLVND NLLPLTKSRE FTRKDISLLP AVQKVSEQYD PWVDWAHLWS STNLYQNRIL
     VRQNEEDTSM KFITPTATPP IAPMKLCWDS ETTYTLEFEA AGAVSLTAEN IERMRAATSL
     YLQATTSTPL AGNKDYIALF GPDLPWDELE TWLKKNQGHE PAIQVFSSQR PLDRMGVVRD
     RSRYGELLIF KRWLNRSGDL ELECDPYPSK RRNLLQRQTL AKKRPAEDEI LGSPTKKRIL
     SASHCTIDRL PASETVFGRF IPVILDRLEA ALVATRLCET VLRDIQFQDL RHVITAITMP
     LAQAPTDYQR YEFFGDSVLK FTVAASLFYN NPNWHEGYLT ETLHALVQNA RLTRAALDQG
     LDAYIISNRF TPRKWSAPLI SEKLYASAST RSMSAKVLAD VVEALIGAAY IDGGLHKAQS
     CIVRFLPEIE LPETKLPRPE SMPMSKDHKK PHLIQQENLE NHIGYTFKDK TLLMEALTHP
     SCPYDTSIQS YQRLEFLGDA VLDMLIVDLI RAHHVECQQG EMTKIKHAIV NGHLLAFLCM
     QFKWAMPSPL TPSIDTGTET ETEIISPPPK TLSLYSYLRY SPSRPLPLHV EPESGSSNAL
     TRHNLLCPSI LHALNNTTAY PWSLFSAIHA DKFFSDVVES IIGAIFVDSG GDLGACAGFI
     ERLGLVRIAK RILDERVDVT HPTQRAQIEL QKLAARLGCN DGFRFECRTV RDLSSGKRKT
     LEVDINDHYG DEDPAVLGAE GPELTYTCTI SLATLRTNQD FGRDLDDIVV TGCLSKEDAE
     IQAANLVIEL VGRLESGRLY KKNMDLDIDT GVQVDLDLDM NLDPGITTG