ID A0A118K693_CYNCS Unreviewed; 1178 AA.
AC A0A118K693;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=Ccrd_011368 {ECO:0000313|EMBL:KVI10263.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI10263.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVI10263.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVI10263.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(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:KVI10263.1}.
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DR EMBL; LEKV01001025; KVI10263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A118K693; -.
DR EnsemblPlants; KVI10263; KVI10263; Ccrd_011368.
DR Gramene; KVI10263; KVI10263; Ccrd_011368.
DR OMA; EEWNELE; -.
DR Proteomes; UP000243975; Unassembled WGS sequence.
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:SF957; 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:UP000243975};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 898..1163
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 929
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1178 AA; 129461 MW; F45E1D00FD937709 CRC64;
MEPSKPDNYV QYNSVQSENS DSAPSSQSFL NANTRPASVK PVLNYSIRTG EEFALEFIRD
RVNPRMPFVP YPAGDSNLTT GYMELKGILG ISHTGSESGS DISMLNIVER GSKDHEHNSS
LYEGTSNFGS VSSMPQPSSE FNSTRPVVHG YSSSGASDGS SKIKILCSFG GKILPRPSDG
KLRYVGGETR IIRIRRDIFW QELRQKMIEI YIETYAIKYQ LPGEDLDALV SVSSDEDLQN
MMEECHVLGI GEGSKKLRLF LFSLSDLDDA HFGHANSSGD SEFQFVVAVN GMDMGSRRES
GMDGLMRSSA NNLSELDGQT VERNISRAAT DFVGGNAPLS TDLHVSSSVP ASSPAMLPNS
SNAYGNRNQI HQVLPVHHGE ANLNIQHHAS VSRPTGDKPP AETSVPLNTD GLVDRQGGFT
DGYPSRTMVV QNRQPQKEEK PKGDSSVKQE VKQANIRSPR DEAASGALPS GEGKLPPKPK
MNEERHQDQI QVSPPLNVAS MAKVVASNDN DSCTSSIALA PDNSGSDLID LSYLEPPVPP
PRVYHSERIP RGQGEYNRLT KSDDSLGSQF LVTHLQSDVE SQDFISESVG SLHTEDLPPQ
NELPPISMGK PSHTNSQITY GGNGKSKEAP HESVEDHAVN NDQVQNASNV SDATMISDKK
VKFDKPAETG SHLMHQQKQT TSDFTASGAQ VHAQSSAPSA SRPEQGDILI DLNDRFPRDF
LSDVFTRAMA EDSPGIGVLP QDGAGLSLNI ANHEPKHWSF FQKLARGEFR QKDVSLIDQD
HLAFLSGLQN IEEEASAVYN VAKFKNDVSG SQLDSQNTII EDEEKEITGS ESTSMQPHYN
PSHMKSSEGM QFGDLAENLR MPDSEYEVET RNDGLPSIDL SLGDLDISSL QIIRNEDLEE
LRELGSGTFG TVYHGKWRGT DVAIKRIKKS CFAGRSSEQE RLTIEFWREA DILSKLHHPN
VMAFYGVVQD GPDGTLATVT EFMVDGSLRH VLLRKDRHLD HRKRLIIAMD AAFGMEYLHS
KNIVHFDLKC DNLLVNMKDS SRPICKVGDF GLSKIKRNTL VSGGVRGTLP WMAPELLNGG
SNKVSEKVDV FSFGIVLWEI LTREEPYANM HYGAIIGGIV NNSLRPTIPS DCDPEWRRLM
EQCWSPDPVV RPSFTEITNQ LLVMSAACQS KGHAHKAS
//
