ID A0A164VLB4_DAUCS Unreviewed; 1986 AA.
AC A0A164VLB4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZM90516.1};
GN ORFNames=DCAR_022119 {ECO:0000313|EMBL:KZM90516.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM90516.1};
RN [1] {ECO:0000313|EMBL:KZM90516.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM90516.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM90516.1}.
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DR EMBL; LNRQ01000006; KZM90516.1; -; Genomic_DNA.
DR STRING; 79200.A0A164VLB4; -.
DR EnsemblPlants; KZM90516; KZM90516; DCAR_022119.
DR Gramene; KZM90516; KZM90516; DCAR_022119.
DR OMA; LCAIHPF; -.
DR Proteomes; UP000077755; Chromosome 6.
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; -; 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; 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; 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; 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:UP000077755};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00657};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158}.
FT DOMAIN 314..491
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 708..869
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 897..988
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 1266..1402
FT /note="PAZ"
FT /evidence="ECO:0000259|PROSITE:PS50821"
FT DOMAIN 1445..1607
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1648..1796
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1822..1885
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 1908..1983
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 139..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1986 AA; 223463 MW; 81D81BA81210BA65 CRC64;
MDDNGDEASN SNRKIASSSY WLDACEEDMC CDDLITFPSD FHPPPPPVSS SLDQQPEDSV
LDPCFFGGID GILDSIRKGA GFTPPPPQSQ FNNELEMEEV DKSFHSNDET IIHLNHSFLP
DDNALATSKA LPVKSTHESY SSSVLNNDHN KVSSTHPPDV NCVKWQTDEA HHRSSGIIHR
ADRIDKKPQL HHQQDHYLAR KNKNNNHNPR ERKRSRDWEE SDRRDRSRIR RSERNNGSVN
GKKDFRENRG YWERDRSKGS GEMVYRPGSW EPDQTREFKA LSNKTHDNSG EVKKAIEPKE
KVIEEHARKY QLDVLQQAEN RNTIAFLETG AGKTLIAVLL IKSLCSRLQK INKKFLAVFL
VPKVPLVYQQ AEVIRDRTGY QVGHYCGEMG QDFWDARRWQ HEFETKQVLV MTAQILLNIL
RHSIIKMESI NLLILDECHH AVKKHPYSLV MSEFYHTTPK MKRPSVFGMT ASPVNLKGVS
SQEDCAIKIR NLETKLDSIV CTIKDRKELE KHVPMPSETV VLYDKAASLC YLHEQIKQME
VAVEQAALSS SRRSKWQFMG ARDAGAKEQL RQVYGVSERT ESDGAANLIQ KLRAINYALG
ELGQWCAFKV AQSFLTALQN DERANYQLDV KFQETYLDKV VSLLQCQLSE GAVPDNLEDA
LKNGVDVGGL DEEVEEGELP AIVSGGEHVD VIIGGAVADG KVTPKVQSLV KILHRYQSTG
DFRAIIFVER VVTALVLPKV FAELPSLSFI RSASLIGHNN SHEMRTSQMQ DTISKFRDGR
VTLLVATSVA EEGLDIRQCN VVIRFDLAKT VLAYIQSRGR ARKPGSDYIL MAERGNLSHE
AFLRNARNSE ETLRKEAIER TDLSHLKDNS RLISADSSPG SFYQVESTGA IVSLNSAVGL
IHFYCSQLPS DRYSILRPEF IMERHEKLGG PPEYSCRLQL PCNAPFENLE GPICISMRAV
CLLACKKLHE MGAFTDMLLP DKGSGGDGEK PEQNDEDALP GTARHREFYP EGIANILEEW
LVCAPSHIPQ LVFIINSELV HLYMYALRCS NVGSSKDNHI TNVSEFAVIF GKELDAEVLS
MSMDLFVART MITKASLVFQ GPIEITENQL VSLKSFHVRL MSIVLDVDVE PATTPWDSAK
AYLFVPLLSN KCRNLGEEID WNLVEQIVKT DAWNNPLQRA RPDVYLGTNE RTLGGDRREY
GFGKLRHGMA FGQKYHPTYG IRGAVAQFDV VKASGLLPNQ GIVEMPNHMN LTKVKLMMAD
SYTTPEDLVG RIVTAAHSGK RFYVDSVRSD MTAENSFPRK EGYLGPLEYS SYADYYKQKT
GQLQCTSVDV HGKLYSVRIS NRYGVDLKCK QQPLLRCRGV SYCKNLLSPR FVHSEAHDGE
SEEALDKTYY VYLPPELCFV HPLPGSLVRG AQRLPSIMRR VESMLLAVQL KNMIGYSVPS
LKILEALTAA SCQEPFCYER AELLGDAYLK WVVSRYLFLK YPQKHEGQLT RMRQQMVSNM
VLYQFALNKG LQSYIQADRF APSRWSAPGV PPVFDEDTKE EDLPFPDQER VLDTYLSGID
SSKGISEDDE MEDGELESDL SSYRVLSSKT LADVVEALIG VYYVEGGKIA ANHLMKWVGI
QVDFDVKELD FSSKVSHVSD SVLKSVNFEA LEGALHFKFK DRGLLIEAIT HASRPSSGVS
CYQRLEFVGD AVLDHLITRH LFFTYTDLPP GRLTDLRAAA VNNENFARVA VKHNLHVHLR
HGSNALEKQI RDFVKEVQNE LLKQGFNCFG LGDCKAPKVL GDIVESIAGS IFLDSGHDTG
VVWQVFKPLL EPMVTPETLP MHPVRELQER CQQQAEGLEY KATRSGNVAT VEVYIDGVQV
GAAQNQQKKM AQKLAARNAL IALKEKETIE ADEKRDEDGK KGNGSHTFTR QTLNDICLRR
NWPMPSYRCV NEGGPAHAKK FTFAVRVNTS DRGWTDECIG EPMPSVKKAK DSAAVLLLEL
LNNWYA
//
