ID A0A165WUP1_DAUCS Unreviewed; 754 AA.
AC A0A165WUP1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZM97681.1};
GN ORFNames=DCAR_014957 {ECO:0000313|EMBL:KZM97681.1};
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:KZM97681.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM97681.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM97681.1};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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:KZM97681.1}.
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DR EMBL; LNRQ01000004; KZM97681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165WUP1; -.
DR STRING; 79200.A0A165WUP1; -.
DR EnsemblPlants; KZM97681; KZM97681; DCAR_014957.
DR Gramene; KZM97681; KZM97681; DCAR_014957.
DR Proteomes; UP000077755; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR Gene3D; 2.20.25.80; WRKY domain; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003657; WRKY_dom.
DR InterPro; IPR036576; WRKY_dom_sf.
DR PANTHER; PTHR47985; OS07G0668900 PROTEIN; 1.
DR PANTHER; PTHR47985:SF23; OS07G0695300 PROTEIN; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF03106; WRKY; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00774; WRKY; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF118290; WRKY DNA-binding domain; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50811; WRKY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 186..243
FT /note="WRKY"
FT /evidence="ECO:0000259|PROSITE:PS50811"
FT DOMAIN 380..445
FT /note="WRKY"
FT /evidence="ECO:0000259|PROSITE:PS50811"
FT DOMAIN 498..754
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 114..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 754 AA; 84019 MW; D119D4D5A94AD9A2 CRC64;
MEERTGIVKP VACRPTVRAI SVLLSANINA STSNSTSQPV VLATRPKTVR VKPVVKLISS
KDKALGTTVS SSLDRDLKVE NKSTVVYKPL AKLVSKRTIS LLANMENSCF QHHEALPQSD
PCSPSPNQVH CHLKSENNLN GSSNKTTTSE SKREIKPLQR MVAEDSSKEY KDKLLPTNTV
DRPSYDGYNW RKYGQKHVKG SEYPRSYYKC THPNCPVKKK VERSLDGQIA EIVYQGEHHH
SKPKLHKRNT LEGEGQGFVS GATGQESNYS LSNSNLNEKN EGSECRSDDQ NGAEVPSSSS
NISKGLSCCD PMKALAIGGR SISTNDLHAL TRDCEEYTEG AEVEGDEPTS KRRKNKNKLY
EAGIQEEGLQ ISNGVVQSSN DSELIGDGFR WRKYGQKIVK GNPNPRSYYR CTGLRCNVRK
HVERASDDPT AFITTYEGKH NHHKPPVNNK NLVASGPDSK DNLKPSIKMK EASKEGGSDH
MAARTFPFRD LAAATKNFRA DYLLGEGGFG RVYKGRLENS NQVVAIKQLD RNGLQGNREF
LVEVLMLGLL HHDHLVNLIG YCADGDQRLL VYEYMPLGSL DDHLHDPSPD KRRLDWNTRM
KIAAGAAKGL EYLHDKASPP VIYRDLKCSN ILLGRKAVES TKTAGDHTLV AWARPLFKDR
RKFSQIADPM LQGEYPTRGL YQALAVAAMC VQEQPNMRPA IADVVTALSY LSSQKFDPRT
HPQQSSQWSP ATPPRTKRDG DRRRYDDGGC ERRY
//
