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DCL2_ASPCL
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   03-AUG-2022, entry version 84.
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; 5057.CADACLAP00005115; -.
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; HFCAVIP; -.
DR   OrthoDB; 1337630at2759; -.
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: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..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
 
 
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