ID A0A165WW34_DAUCS Unreviewed; 1399 AA.
AC A0A165WW34;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=DCAR_014924 {ECO:0000313|EMBL:KZM97714.1};
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:KZM97714.1};
RN [1] {ECO:0000313|EMBL:KZM97714.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM97714.1};
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:KZM97714.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNRQ01000004; KZM97714.1; -; Genomic_DNA.
DR STRING; 79200.A0A165WW34; -.
DR EnsemblPlants; KZM97714; KZM97714; DCAR_014924.
DR Gramene; KZM97714; KZM97714; DCAR_014924.
DR OMA; SYNTYQV; -.
DR Proteomes; UP000077755; Chromosome 4.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06410; PB1_UP2; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000270; PB1_dom.
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 PANTHER; PTHR23257:SF797; KINASE SUPERFAMILY WITH OCTICOSAPEPTIDE_PHOX_BEM1P DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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 1110..1376
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 121..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1399 AA; 152581 MW; C2EF67E5834807E7 CRC64;
MAFDQNSIPI NLRPLNTART LVDDSRIAPP VTTTSGRNIE GFYAANPSRD HPHPGSPSAV
PLYYPATVSD SGYVGLGYPG VGGGWVQRMP HPPAAVIGAP VVTSPAVVAS PAVVPTAGYG
NSPKLGNRLG GTNFDQASDD SRDDSVSGKK VKFLCSFGGK IMPRPNDGAL RYVGGETKII
SVRRNLSFNE LVQKMTDSYG QNVVIKYQLP DEDLDALVSV SSPDDMENML DEYERLVERS
PDGSAKLRVF LFSPTEGDSP ATVQTGISKD NGQRYIEAVN GIVDGTTDGI TRRESMASAT
STQNSDLSGT EAVDSTGHGQ VDVVGNLSTG GVSPKTNFIA TQEVAPRLVY VDPNPPMHIE
AATAPIGVQM VSSHPPVLST QPISVVQPPQ QLGFPPRAPY FQAYADPQQE VLNRTEYVQY
PSQMGFPAQL YGTVRPVFTQ QQYHNNVANI NPHQQYIPAV HMSMTPSSYA NLRPTAVQPI
VQPQQVQVEL FPEENKYGQR VMQLPGDQSY NAYHAQVSQS PIMPGGFGWH QAPQTEQVPF
SDGLVPQQQA ALAEKLPRFE ECFMCQKALP HAHSDTVAQG QRDSPTTTSD FIPGYHSLQT
DIKIRSQPIS TAAPTGPMAE SIVEHQFTGA PQTSLGHLDH EGRKPAHMGV ALPQYVDDKT
SLQRENNHNH LQTSLPQSVV GGSQSPDSGL TGTAPQLYQV NISQQPVLLM EHKAKQDVVY
NTSVSVASAR DASSQASDHL VHESPKENSG KVPDFVSKEG TLESSPVYDQ LRQIDSRLEN
LGVRPSEVVI DNEQLIPPAD SSKDDIVDSR AHQISNTEPY IDNAFSNPQM VLDGNYYKQN
EMQYCPSDEV PNLHNEVPSC YEVAQPPLLG NPDFPFERLR MNNLATNHAS YGHSVSFAGN
ESVQVTGAPP SGESKDNSSQ FIPDTVGHVE AIPIDGKSQY HIPPANRIGD VQDNSNSLFS
SQDPWNLRHE THFPPPRPNK ILTRKEAHNR DPFGENRFGN IGEAPSGNNL GFTSELLSDD
GVQTGSAEEH IKQELQAVAE GVAASVLHTS IPSVSVSEAN QDSLVHNNDV EFLHANKVEE
TKSKLPEKAN LGFPVSDGIG RLQIIKNSDL EELRELGSGT FGTVYHGKWR GSDVAIKRIN
DRCFSGKPSE QERMRDDFWN EAIKLADLHH PNVVAFYGVV LDGPGGSVAT VTEYMVNGSL
RTALLKNEKN LDKRKRLLIA MDAAFGMEYL HGKNIVHFDL KSDNLLVNLR DPHRPICKVG
DLGLSKVKCQ TLISGGVRGT LPWMAPELLN GSSSLVSEKV DVFSFGIVLW ELLTGEEPYK
DLHYGAIIGG IVSNSLRPHV PDFCDQEWKS LMERCWSADP SERPNFTEVA NQLRTMAAKV
PQKVQAQQQP SSTQPQVKS
//
