ID A0A161YHC4_DAUCS Unreviewed; 1210 AA.
AC A0A161YHC4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=DCAR_020116 {ECO:0000313|EMBL:KZM92519.1};
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:KZM92519.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM92519.1, 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:KZM92519.1};
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:KZM92519.1}.
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DR EMBL; LNRQ01000006; KZM92519.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161YHC4; -.
DR EnsemblPlants; KZM92519; KZM92519; DCAR_020116.
DR Gramene; KZM92519; KZM92519; DCAR_020116.
DR OMA; NWVPSEN; -.
DR Proteomes; UP000077755; Chromosome 6.
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:SF980; 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); 2.
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 937..1207
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 737..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 964
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1210 AA; 135143 MW; 7BCBD6934DB4D712 CRC64;
MMCNKGVECI KQSEAEVVYS MDSPTATMTP GSHRSSNDEN QRVKFLCSFG GSILPRPQDG
KLRYVGGETR IVSAPRDISY EDLMGKMREL FEGAMVLKYQ QPDEDLDALV SVVNDDDVTN
MMEEYDKLVF GSGFTRLRIF LFSGLDQDGS VHFVNGDEMD NERRYVDALN SLNDSPDMRR
LHYSESQVFG SLDDYQLNEQ YLNQISHEGS LHNHRNNEMP IPPLNLRRLN IPQMGSGHQS
ITQRYNDMEA PWSPGYYSPG NQDPRPIMEV PASPSSSRYF MPYGEFPDRT FDRMPEEYNR
QQQNRQPSTH QPQLQENVVW LPPGSVAGDS PGFPGNILQG PGNVHQGFGM FEGNKCEQCR
TTFLRNQAHY DSHLKHGEQH MEMPNMVNGF QQVPCAECPP TRDTLMLNTE AKLHSPFYPR
EQNDPRPLCT DSNERARISL HQPNLRVDEQ RLPTSGTARL SDHYIVDGSG MKFSAGHGNF
PESQHVSSHY AHPEDHSWYM RPGHELGNEV FPDQTGVTGS SHIHIPLDDH GVRYGNPPVV
YGMEKFYQQP HGHVPEHSIW RNHNAPLHYP PKYEVGTVPQ QPDGIPGFYR GTYDSSPNFQ
VGLGNQNLLA DPSLTVGGID GSAVLEYPQD HSFNSIAIQN TLNNHVTSDM INSTRLPNTE
PCADLASTLI DGRLVSQIVS TSDSKLDLEK EGKCANGVLK ETNGTENFED SNMPFVSGLQ
LKDKPDAIAS RGAVNLNRLG PVHKGNGPEK PKGHETHSNF QTEQPPVDQL NFVPELIASV
KRVAIQSAED VKLKVQEGAL SADLNDVMAK EACHNEKEAA VKEEIHNKSE AVAKEEIQNE
SEAVDLNGNL DLGSSGDNVD DTKIEPTKAE AEAFARGLQT IRNDDLEEIR ELGSGTYGSV
YHGKWKGSDV AIKRIKASCF AGRPSERERL TIRNDDLEEI RELGSGTYGS VYHGKWKGSD
VAIKRIKASC FAGRPSERER LIADFWKEAL ILGSLHHPNV VSFYGIVRDG PDGSLATVTE
FMVNGSLKQF LQKKDRTIDR RKRLIIAMDA AFGMEYLHEK NIVHFDLKCE NLLVNMRDPH
RPVCKIGDLG LSKVKQRTLV SGGVRGTLPW MAPELLSGKS NMVTDKIDVY SFGIVMWELL
TGEEPYADIH CASIIGGIVN DSLRPQIPTW CDPEWKALME SCWSSDPAQR PSFAEVAQKL
RNMAAAINVK
//
