ID A0A2I4GAD8_JUGRE Unreviewed; 1995 AA.
AC A0A2I4GAD8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Endoribonuclease Dicer homolog 1 {ECO:0000313|RefSeq:XP_018840835.1};
GN Name=LOC109006086 {ECO:0000313|RefSeq:XP_018840835.1};
GN ORFNames=F2P56_014678 {ECO:0000313|EMBL:KAF5464610.1};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018840835.1};
RN [1] {ECO:0000313|EMBL:KAF5464610.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5464610.1};
RA Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA Stevens K., Paul R., Butterfield T., Britton M., Reagan R., Chakraborty S.,
RA Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R., Pratt K.,
RA Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M., Salzberg S.L.,
RA Wegrzyn J.L., Langley C.H., Neale D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF5464610.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5464610.1};
RA Marrano A., Britton M., Zimin A.V., Zaini P.A., Workman R., Puiu D.,
RA Bianco L., Allen B.J., Troggio M., Leslie C.A., Timp W., Dendekar A.,
RA Salzberg S.L., Neale D.B.;
RT "Walnut 2.0.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_018840835.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018840835.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; LIHL02000007; KAF5464610.1; -; Genomic_DNA.
DR RefSeq; XP_018840835.1; XM_018985290.2.
DR STRING; 51240.A0A2I4GAD8; -.
DR EnsemblPlants; Jr07_10040_p1; cds.Jr07_10040_p1; Jr07_10040.
DR GeneID; 109006086; -.
DR Gramene; Jr07_10040_p1; cds.Jr07_10040_p1; Jr07_10040.
DR KEGG; jre:109006086; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000235220; Chromosome 7.
DR Proteomes; UP000619265; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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; IBA:GO_Central.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR CDD; cd18034; DEXHc_dicer; 1.
DR CDD; cd19869; DSRM_DCL_plant; 1.
DR CDD; cd02844; PAZ_CAF_like; 1.
DR CDD; cd00593; RIBOc; 2.
DR CDD; cd18802; SF2_C_dicer; 1.
DR Gene3D; 3.30.160.20; -; 2.
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; PF00035; 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; 2.
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; 2.
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; 2.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000235220};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00657};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158}.
FT DOMAIN 340..517
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 739..900
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 928..1023
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 1296..1410
FT /note="PAZ"
FT /evidence="ECO:0000259|PROSITE:PS50821"
FT DOMAIN 1453..1615
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1656..1804
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1830..1893
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 1917..1992
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 168..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1995 AA; 223878 MW; 7908EC0021E172D0 CRC64;
MENEAKVSGN SGGELIRASS ADDMRPSYWL DACEDITYDL VDFDSCTVPD SVDNISNQDG
LGSDFFGGLD HILESIKNGG GLPLPPVAET NSSGNGNCTA GGDGCFQNGR SRDSKMQAED
PFLQSDETQK ETTENIVLVA AEGCGNGSDA CKRYQGDNGN TVVDVNGERR LVQYPSEDGV
PKLERRGTEG SRERGMDMEE RGSKRARLGN YNSERCHLSR GQYHSKDRER GSGRKRPRDW
EEIDRRDRDI ARRREHYGCK RRDGRDRDCR DREPKGYWER DRLASSEMVF RLGTWEADRH
KEAKVVNEKN QECNGRAERK SEEPKEKIPQ EKARQYQLDV LEQAKKKNTI AFLETGAGKT
LIAVLLIKSV SDDLQRENKK MLAVFLVPKV PLVYQQAEVI RERTGYQVGH YCGEMGQDFW
DARRWQREFE TKQVLVMTAQ ILLNILRHSI IKMEAINLLI LDECHHAVKK HPYSLVMSEF
YHTTAKDKRP SVFGMTASPV NLKGVSSQVD CAIKIRNLES KLDSIVCTIK DRRELEKHVP
TPSEVVVEYD KAASLWSLHE QIKQMEAEVE EAAKSSSRRS KWQFMGARDA GAKEELRQVY
GVSERTESDG AANLIQKLRA INYALGELGQ WCAYKVAQSF LTALQNDERA NYQLDVKFQE
SYLNKVVSLL QCQLSEGAVS EKDTKVAHSE SNVAHDGIDA DDIEEGELPD SHVVSGGEHV
DVIIGAAVAD GKVTPKVQSL IKILLKYQNT EDFRAIIFVE RVVSALVLPK VFAELPSLSF
IKCASLIGHN NSHEMRTCQM QDTISKFRDG RVTLLVATSV AEEGLDIRQC NVVIRFDLAK
TVLAYIQSRG RARKPGSDYI LMVERGNLSH EAFLRNARNS EETLRKEAIE RTDLSHLKDI
SRLISVDTSP GTVYQVESTG AVVSLNSAVG LIHFYCSQLP SDRYSILRPE FIMEQHEKSG
GPTEYSCKLQ LPCNAPFEKL EGPVCSSIRL AQQAVCLAAC KKLHEMGAFT DMLLPDKGSG
EEREKVDQND EGDPLPGTAR HREFYPEGVA DILKGQWILS GRDVCDYSTL LHLYVYSVKC
VNIGSSKDPF LTQVLDFAVL FGNELDAEVL SMSMDLFIAR TMSTKASLTF RGSIDITESQ
LASLKSFHVR LMSIVLDVDV EPSTTPWDPA KAYLFVPVVG DKNVDPMREI DWDLIEKIIN
TDAWNNPLQR ARPDVYLGTN ERTLGGDRRE YGFGKLRNGM AFGQKSHPTY GIRGAVAKFD
VVKASGLVPG RDARDLQTHM DLTRGKLMMA DACMSAEDLV GRIVTAVHSG KRFYVDSIHY
DMTAENSFPR KEGYLGPLEY SSYADYYKQK YGVELIYKQQ PLIRGRGVSY CKNLLSPRFE
HKEAHEGEAE ENLDKTYYVF LPPELCLVHP LPGSLVRGAQ RLPSIMRRVE SMLLAIQLKD
IINYPVPVSK ILEALTAASC QETFCYERAE LLGDAYLKWV VSRFLFLKYP QKHEGQLTRM
RQQMVSNMVL YQYALSKGLQ SYIQADRFAP SRWAAPGVLP VFDEDAKDGE TSLFDQDRSL
AETQHGMGRC IDAYEDDEME DGELESDSSS YRVLSSKTLA DVVEALIGVY YVEGGKNAAN
HLMKWIGIQV EFDADEIDCM PRPSNVPESI LRSVNFEALE GALNINFKDR GLLVEAITHA
SRPSSGVSCY QRLEFVGDAV LDHLITRHLF FTYTDLPPGR LTDLRAAAVN NENFARVAVK
HNLHVHLRHG SSALEKQIRD FVKEAQDELL KPGFNSFGLG DCKAPKVLGD IVESIAGAIF
LDGERDTAVV WKVFQPLLHP MVTPETLPMH PVRELQERCQ QQAEGLEYKA SRSGNLATVE
VFIDGVQVGI AQNPQKKMAQ KLAARNALAA LKEKETAEAK EKSDENGKKK KNGNQTFTRQ
TLNDICLRRN WPMPFYRCVN EGGPAHAKRF TFSVRVNTTD RGWTDECVGE PMPSVKKARD
SAAVLLLELI NKLYS
//
