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Database: UniProt
Entry: P0C5H7
LinkDB: P0C5H7
Original site: P0C5H7 
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   31-JUL-2019, entry version 68.
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
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Dicer-like endonuclease involved in cleaving double-
CC       stranded RNA in the RNA interference (RNAi) pathway. Produces 21
CC       to 25 bp dsRNAs (siRNAs) which target the selective destruction of
CC       homologous RNAs leading to sequence-specific suppression of gene
CC       expression, called post-transcriptional gene silencing (PTGS).
CC       Part of a broad host defense response against viral infection and
CC       transposons (By 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};
DR   EMBL; AACD01000052; EAA62953.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001306; CBF83228.1; ALT_SEQ; Genomic_DNA.
DR   STRING; 162425.CADANIAP00009879; -.
DR   EnsemblFungi; EAA62953; EAA62953; AN3189.2.
DR   HOGENOM; HOG000048683; -.
DR   InParanoid; P0C5H7; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016442; C:RISC complex; IBA:GO_Central.
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; IBA:GO_Central.
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:0030422; P:production of siRNA involved in RNA interference; IBA:GO_Central.
DR   GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 3.
DR   Gene3D; 3.30.160.380; -; 1.
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; 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; 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; Complete proteome;
KW   Helicase; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat; RNA-binding.
FT   CHAIN         1   1429       Dicer-like protein 2.
FT                                /FTId=PRO_0000306793.
FT   DOMAIN       21    200       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      335    501       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      528    622       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      874   1014       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1056   1250       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   NP_BIND      34     41       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       141    144       DEAH box.
FT   METAL      1095   1095       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1236   1236       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1239   1239       Magnesium or manganese. {ECO:0000250}.
FT   SITE       1232   1232       Important for activity. {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
//
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