ID A0A175YIW1_DAUCS Unreviewed; 970 AA.
AC A0A175YIW1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=DCAR_028922 {ECO:0000313|EMBL:KZM83656.1};
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:KZM83656.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM83656.1, 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:KZM83656.1};
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 -!- 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:KZM83656.1}.
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DR EMBL; LNRQ01000008; KZM83656.1; -; Genomic_DNA.
DR RefSeq; XP_017220434.1; XM_017364945.1.
DR AlphaFoldDB; A0A175YIW1; -.
DR EnsemblPlants; KZM83656; KZM83656; DCAR_028922.
DR GeneID; 108197357; -.
DR Gramene; KZM83656; KZM83656; DCAR_028922.
DR KEGG; dcr:108197357; -.
DR OMA; ESMATCY; -.
DR OrthoDB; 384316at2759; -.
DR Proteomes; UP000077755; Chromosome 8.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR48056:SF50; BRASSINOSTEROID LRR RECEPTOR KINASE; 1.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00560; LRR_1; 11.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..970
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008044611"
FT TRANSMEM 608..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 687..959
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 716
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 970 AA; 105757 MW; 9F73D5CFB9982378 CRC64;
MLLSLVLVVF LIPLHVHSVS SSAAFSDDLL GLIVFKADLS DPLSKLTSWN EDDASPCNWF
GIKCHPYTNR VTELHLDNLS LSGHIGRGLL GLEFLHKLSL SNNNFTGPIT PILSQFDNLQ
VIDLSHNAFS GFIPQQLFVQ CRSLRVIALA NNHLTGPIPD TFSSCSTLKG VNFSSNRLSG
QLPSGIWSLN ALRSLDLSDN LLEGVIPRGI QSLYDLRALS LRKNNFIGQL PDDIGGCLLL
KSLDFSNNHL SGELPWSMQK LSLCNSLYLG GNSLSGEFPD WISNMRSLET LDLSVNSFYG
QLAYSIGELQ FLKQLNLSRN QFTGSLPESL KNCISLKTVD VSWNLLAGNL PPWIFELGLE
TISLSGNRLN GSVEYPLSML MSASYQSIQV IDLSSNALFG EIPSGVGNLS RLQFLNMSRN
FLFGTIPGTF GELKAARVLD LSHNWLNGSI PSGIGGAAAL LELWLENNFL TGEIPLEIGN
CSSLTTLILS QNNLTGPVPV VIANLTELQT VDFSFNQLSG SLPKELKNLS YLHIFNISHN
NLQGELPVGG FFDTIPLSSL AGNPSLCGYV MNNSCNATHP KPIVLNPDSS SGSSNHGSLS
PSFHHKKIVL SISALVAIGA AILIALGVLT VAILNLHARS AMPGANTSLN SYGGDEFSPA
HTSESNYGKL VMFAGDSEFV DGAHGLLNKD CEIGHGGFGI VYETALRDGR SVAIKKLNAS
GLMKSQDDFE REVKKLGKIR HQNLVALEGY YWTQSLQLLI NEYVCNGSLY THLHGGQSEN
CLSWKQRFNI IHGTAKGLEH LHRSNVIHYN LKPSNILIDS CFEAKVGDFG LASLLPLLDR
YNLSSKIQSA LGYMAPEFAC QTVKITEKCD IYGFGILILE VVTGNRPVEY MEDDVVVLCD
MVREALDEGR SEDCVDRKLM GNFPVEEAIP VIKLGLICAS QVPSNRPDME EVIRILDLIR
CPSESQGETE
//
