DCL1_ASPFU
ID DCL1_ASPFU Reviewed; 1537 AA.
AC Q4WVE3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Dicer-like protein 1;
DE Includes:
DE RecName: Full=Endoribonuclease dcl1;
DE EC=3.1.26.-;
DE Includes:
DE RecName: Full=ATP-dependent helicase dcl1;
DE EC=3.6.4.-;
GN Name=dcl1; ORFNames=AFUA_5G11790;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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=EAL91433.2; Type=Erroneous gene model prediction; 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; AAHF01000003; EAL91433.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_753471.2; XM_748378.2.
DR AlphaFoldDB; Q4WVE3; -.
DR SMR; Q4WVE3; -.
DR STRING; 746128.CADAFUBP00005808; -.
DR GeneID; 3511514; -.
DR KEGG; afm:AFUA_5G11790; -.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_3_1; -.
DR InParanoid; Q4WVE3; -.
DR OrthoDB; 1337630at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
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:0003677; F:DNA binding; IEA:InterPro.
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; IBA:GO_Central.
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:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
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; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
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; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 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; Zinc.
FT CHAIN 1..1537
FT /note="Dicer-like protein 1"
FT /id="PRO_0000306774"
FT DOMAIN 133..314
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 459..618
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 651..741
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 1043..1202
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1253..1405
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1439..1507
FT /note="DRBM"
FT REGION 38..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 259..262
FT /note="DEAH box"
FT COMPBIAS 44..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 146..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1394
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1478
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1521
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT SITE 1387
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1537 AA; 175123 MW; 834EE8DBC39461A2 CRC64;
MAEQISLVDV SSSVSLRGED SSNVALLRDV FLPDVAASDP AESSVDVQDE HSSDDSDNEN
EVFPKQNDFS QRRRIQNAQF EALLSKCTDA DSNEAFDRAP IALSDGELSI AHLVKKQDLG
NGMLDPREYQ IELFERAKTQ NTIAVLDTGS GKTLIAVLLL RHTILNELDD RANGKTHRVS
FFLVDSVTLA YQQAAVLRNN IDQNVAHFFG AMGTDLWDKR TWDKHLQRNM VIVCTAEILN
QCLLNSYVRM DQINLLIFDE AHHAKKDHPY ARIIRDSYFK AQPSQRPRVF GMTASPIDTK
GDITEAATRL ETFLDSRIAT TSKITLLREV VSRPIEKVWA YNRLEPPFAT ELYKLMDTRY
GNIKVLEGVY RFAWNASSEL GKWCSDRAWW HALADDVLPK LEGNINKLIE SNTMKAEHGA
VFKDIIRIRE ASETVKNYFF TDPELPGELS PKVQRLRMEL SKHFNDTTGT KCIVFTQKRY
TAKILNELFT VLNIPNLRPG VLIGVRPGDI GGMNITFRQQ FLALVKFRTG EINCLFATSV
AEEGLDIPDC NLVIRFDLYR TLIQYVQSRG RARHCTSTYA IMVEKDNAEH EGRLKEIREA
ENIMRRFCEI LPEDRILHGN DHDLDSFLQE EEGRRTFTVK STGAKLTYHS AIAILARYAS
SLQYEKETVP QVTYVVTIAS NAYVCEVILP EKSPIRGLTG SPAMRKAVAK RSAAFDTCLL
LRKNRLLDGY FNSIYHRRLP AMRNAKLAIT CKRTNAYDML LKPSIWAKQR TTPTETFYGI
HMSLLPSKPL SRDHRPILLL TREKLPEFPA FSIYLDEDVE TKVLSYPLKH GLQISVDKLQ
SLTVFTLRIF RDIFHKVYEH EVQKMPYWLA PAEAIDGRGS GKNPRDCIDW DTVSFVHNND
EITFTRNLNP ESLVNRFIFD NWDGRFRYFT VAVADTLQPS DPPPPSVPRR RYMNNIMNYT
LSLSKNSRAR FLSSCDWNQP VLQAELVRLR RNLLDKMTTQ EKEMQTECFI CAEPLRISAL
PPSIVSTCLA FPAIISRLDS YLIALEACDE LELVIRPDFA LEAFTKDSDN TEEHRGQQIH
FQRGMGKNYE RLEFLGDCFL KMATSIALFS QNPNDDEFDY HVNRMCLICN KNLFNTAIKK
QIYRYIRSRG FSRHIWYPDG LTLLHGKDHS TKLLSEGKHA LGEKTIADVC EALIGASLLS
GGPEHRFDMA TKAVSALVDS PSHRVSCWKE YITLYTLPKY QTEKHRGSED DLARHVEEEL
GYHFTYPRLL ASAITHPSLP STWGYRVPCY QRLEFLGDSL LDMVCVEDLF RRFPDRDPQW
LSEHKMAMVS NKFLGALSVK LGFHRRIMAF SNPLQAQITH YVEEIETAQA ESQGAVDYWV
VAKDPPKCLP DMVEAYLGAI FVDSKFDFQV IEAFFERQIK PFFEDMSIYD TFANKHPTTF
LHNKLTNEYG CTNYCLKAGE LPTIDGAPAT VLAAVIVHGN VISEARSSSS RYAKITASEK
ALAVLDGLLP SEFCQKYRCD CKETKNSSSV VEIGTAI
