ID H9N4C6_NICAT Unreviewed; 1690 AA.
AC H9N4C6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Dicer-like 1 protein {ECO:0000313|EMBL:AFD22618.1};
DE Flags: Fragment;
GN Name=DCL1 {ECO:0000313|EMBL:AFD22618.1};
OS Nicotiana attenuata (Coyote tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=49451 {ECO:0000313|EMBL:AFD22618.1};
RN [1] {ECO:0000313|EMBL:AFD22618.1}
RP NUCLEOTIDE SEQUENCE.
RA Bozorov T.A.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFD22618.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22313877; DOI=10.1111/j.1744-7909.2012.01104.x;
RA Ahmadovich Bozorov T., Prakash Pandey S., Dinh S.T., Kim S.G., Heinrich M.,
RA Gase K., Baldwin I.T.;
RT "DICER-like Proteins and Their Role in Plant-herbivore Interactions in
RT Nicotiana attenuata.";
RL J. Integr. Plant Biol. 54:189-206(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000256|ARBA:ARBA00035116, ECO:0000256|PROSITE-ProRule:PRU00657}.
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DR EMBL; JN032013; AFD22618.1; -; mRNA.
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-UniRule.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd18034; DEXHc_dicer; 1.
DR CDD; cd19869; DSRM_DCL_plant; 1.
DR CDD; cd00593; RIBOc; 2.
DR CDD; cd18802; SF2_C_dicer; 1.
DR Gene3D; 3.30.160.20; -; 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; 2.170.260.10; paz domain; 1.
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; IPR014720; dsRBD_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
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; PF14709; DND1_DSRM; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF101690; PAZ domain; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 2.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00657};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158}.
FT DOMAIN 37..215
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 436..596
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 624..719
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 991..1105
FT /note="PAZ"
FT /evidence="ECO:0000259|PROSITE:PS50821"
FT DOMAIN 1148..1310
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1351..1499
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1612..1687
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFD22618.1"
SQ SEQUENCE 1690 AA; 189632 MW; 34CAFF8FF970601B CRC64;
KLPTERSLEP SGAIEKKDVK PKEQAPKEQA RKYQLDVLEH ARKKXTIAFL ETGAGKTLIA
ILLMKSLCND LHKQNKKMLA VFLVPKVPLV YQQAEVIREQ TGYQVGHYCG EMGPRIFGIA
RRWQREFETK QVLVMTAQIL LNILRHSIIK MEAINLLIMD ECHHAVKKHP YSLVMSEFYH
TTQKAKGHLF LAMTASPVNL KGVSSQVDCA IKIRNLETKL DSVVFTIKDR KDLEKHVPMP
SEVVVEYDKA ASLWSLHEQI KQMESAVEEA AQSSSRRSKW QFMGARDAGA REELRQVYGV
SERTESDGAA NLIQKLRAIN YALGELGQWC AYKVARSFLT ALQNDERASY QLDVKFQESY
LDKVVSLLQC QLSEGAVAEN GKMDEGNNPN NDCDRPDEME EGELLESHVV SSGEHVDATL
GAAVADGKVT PKVQSLIKIL LKYQHTEDFR AIIFVERVVT ALVLPKVFEE LPSLSFITSS
SLIGHNNSQE MRTGQMQDTI AKFRDGRMNL LVATSVAEEG LDIRQCNVVI RFDLAKTILA
YIQSRGRARK PGSDYILMVE RDNLSHEAFL RNARNSEETL RKEAIERTDI SHLKGASKLI
SGEAPTDSVY QVESTGAVVS LNSAVGLIHF YCSQLPSDRY SILRPEFIME RHEKPGGPTE
YSCRLQLPCN APFEKLEGPV CSSMRLAQQA VCLDACKKLH QMGAFTDMLL PDKGSGAELE
KVEQDDEGDP IPGTSRHREF YPEGVADILK GEWILSGKDS CDSSKLVHLY MYAIKCVNIG
TSKDPFLTDV SEFAILFGNE LDAEVLSMSM DLFIARTVET KATLVFRGPI EVTESKLASL
KSFHVRMMSI VLDVDVEPST TPWDPAKAYL FAPVTGDESG DPIKDINWDL IKKITKTDVW
SNPLQKARPD VYLGTSERAL GGDRREYGFA KLRHGMAFGL KSHPTYGVRG AIANFDVVKA
SGLVPHRSSL DLVEVDLSKD KIMMADCCLR AEDIVGRIVT AAHSGKRFYV DCIPNDMTAE
NSFPRKEGYL GPLEYSSYAA YYKQKYGVDL VYKKQPLLRG RGVSYCKNLL SPRFEHSEEH
EGELEEATDK TYYVFLPPEL CFLHPLPGSL VRGAQRLPSI MRRVESMLLA VQLKDMIGYP
VPALKILEAL TAASCQETFC YERAELLGDA YLKWVVSRYL FLKYPQKHEG QLTRMRQQMV
SNMVLYQYAL NKGLQSYIQA DRFSPSRWAA PGVLPVYDED TNEEESSMFG NEIIENGTVA
AKTLAADEFE DEEAEEGELD TDSGSYRVLS SKTMADVVEA LIGVYYVDGG KYAANHFMKW
IGVEVDFDFK ETEYSIRPYS IPENVLRSVD FDKLQGALNI SFNDKGLLLE AITHASRPSS
GVSCYQRLEF VGDAVLDHLI TRHLFFTYTD LPPGRLTDLR AAAVNNENFA RVAVKHGLHL
HLRHGSSALE KQIRDFVIEV KNELSKPGFN SFGLGDCKAP KVLGDIFESI AGAIFLDSGC
DTAVVWKVFQ PLLHPMVTPE TLPMHPVREL QERCQQQAQG LEYKASRSGN IATVEVYVDG
IQVGMAQNPQ KRKMAQKVGC QECPCCVEKR GRKPKLRRLK MGRKKKNGNP SYTRQTLNDI
CLRRNWPMPL YRSVHEGGPA HAKRFTYGVR VNTSDKGWTD ECIGEPMPSV KKAKDSAASL
LLELLNRWYS
//
