ID A0A175YNZ0_DAUCS Unreviewed; 1052 AA.
AC A0A175YNZ0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=DCAR_027395 {ECO:0000313|EMBL:KZM85183.1};
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:KZM85183.1};
RN [1] {ECO:0000313|EMBL:KZM85183.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM85183.1};
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:KZM85183.1}.
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DR EMBL; LNRQ01000008; KZM85183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175YNZ0; -.
DR EnsemblPlants; KZM85183; KZM85183; DCAR_027395.
DR Gramene; KZM85183; KZM85183; DCAR_027395.
DR OMA; YACENPE; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_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 PANTHER; PTHR45621; OS01G0588500 PROTEIN-RELATED; 1.
DR PANTHER; PTHR45621:SF35; SERINE_THREONINE-PROTEIN KINASE PBL3-RELATED; 1.
DR Pfam; PF00560; LRR_1; 4.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW 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};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 683..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..372
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 772..1034
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 394..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1052 AA; 117217 MW; 5C4B9BBA6EB543B6 CRC64;
MIVSEIQSSI LLIVHHFHCS VFYFFPASES LKTASKTTPS ARSSVTIPSY SWRSSAESLP
TPRSESEILS SPHVKAFSFT ELKNATRNFR PDSLLGEGGF GYVFKGWIDQ HSLSAAKPGS
GMVVAVKKLK PEGFQGHKEW LTEVNYLGQL HHPNLVKLIG YCSDGDNRLL VYEFLPKGSL
ENHLFRRGAQ PLSWATRIKV AIGAARGLSF LHDAEEQVIY RDFKAANILL DAEFNAKLSD
FGLAKAGPTG DKTHVSTQVM GTHGYAAPEY VATGRLTSKS DVYSFGVVML ELLSGRRAVD
KTKPGVEQSL VEWAKPYLGD KRKLFRIMDI KLEGQYPQKA AHSAATLALH CLRSEPKARP
RMSEVLTTLE QIQAPKTASQ NSSAVHQTVT DPLRRSPMNQ HRSPLNLTPS ASPLQHHRKS
PHVKNCTREL AAVGSRMKHR SKGYSCRGFA APEYVATGLW GPLPRDIDLL GSLEVLNISS
NQIYGNIPAS IATIKNLKNL VLADNVLYGR IPNLKGLQNL EELDLSNNHL GPRLPSLSGN
VVSVTLKNNS LKFEIPSALQ SYDRLERLDL SANKLSGPIP SFLFSLQSIQ YLSLSRNHLS
GELAKNVSCN KNLKYVDISN NFLIGKLPVC IQSNSQNRTV ISWWNCLSNS SSKYQHRYSF
CQKEALAVKP PAMNQKKRTT MKLGIVLGII GATVGIVCTI GILVFIIYRR KAAAKARHHK
DNGFIFDQNP ARGSPIVDSR HRPQTMRRMA TFGLPPYQIF TWEEIHDASN NFDYSNLVGE
DSQGQVYNAW LRDGSPVLLK RMNVKHKHSP QIMKQYKESL SKLRHQNLVS VLGHCIANNV
GNPNLTTIYV VQEFSINGSL RDHFKDWRKR EVLKWPQRMG IIIGVAKGIE FLHRGVAPGH
FGNNIKMKNI MDVRSPLNRD VKNSETARES SLYACENPEK DDIYQLGVIL LQVITGKLFN
SRSEIAEMKL QLETNLTDVM PDSSPKMSDL ADPSLRGTFA YGSLKAAVEI TVHCLEDDSS
SRPSIDDVVW HLQYSIQVQE GWNSSGNLDT RV
//
