ID A0A103XNM9_CYNCS Unreviewed; 618 AA.
AC A0A103XNM9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Pleckstrin homology-like domain-containing protein {ECO:0000313|EMBL:KVH94116.1};
GN ORFNames=Ccrd_003852 {ECO:0000313|EMBL:KVH94116.1};
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:KVH94116.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH94116.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH94116.1};
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:KVH94116.1}.
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DR EMBL; LEKV01004570; KVH94116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103XNM9; -.
DR STRING; 59895.A0A103XNM9; -.
DR EnsemblPlants; KVH94116; KVH94116; Ccrd_003852.
DR Gramene; KVH94116; KVH94116; Ccrd_003852.
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:0006913; P:nucleocytoplasmic transport; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13179; RanBD_RanBP1; 1.
DR CDD; cd06606; STKc_MAPKKK; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045256; RanBP1_RanBD.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48011; CCR4-NOT TRANSCRIPTIONAL COMPLEX SUBUNIT CAF120-RELATED; 1.
DR PANTHER; PTHR48011:SF70; SERINE_THREONINE_DUAL SPECIFICITY PROTEIN KINASE, CATALYTIC DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50729; PH domain-like; 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.
DR PROSITE; PS50196; RANBD1; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 431..566
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT REGION 344..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 618 AA; 68288 MW; 0272A750A948DD2A CRC64;
MTTYTSQSNW LRRNCIGRGS FGVVNLAVHP YHGALFAVKS VENNSRPFVG CLENEIRILK
SLSSPYVVGY LGDDVTSEFS SSSSSSVVYR NLHIEYMSGG TVADVAKLLD GDGSGGVNLR
GYTRCITAAL SYIHARNIVH CDVKGKNVLI GDIPGTAKLA DFGSAIELGV SVTGTRGSPL
WMAPEVIRGE YQGPESDVWS LGCTVIEMFT GKPAWQDRGA DTLRQIGYSD ELPEFPTQAP
EDLHDFLDKC LRREPRERWS CDQLLHHPFL SSCPSTSPPH MTTKLSPRCV FDWSFSSSSK
ESTLEIYQLD TQNSHAKQRI GKLASNSVAN WESEGWEVVR HVTSESGETT SEHDDSINEE
ASVSGSGRAN WEYTNYNASY DDDLESTTNN AQDTRGFGRY RDRYRSTMAS TDPEHNEEET
AAAEDEDTGA QVAPIVKLEE VAVTTGEENE DAILDLKAKL YRFDKDGKQW KERGAGSVKL
LKHKETGKVR LVMRQSKTLK ICANHLVIPT TSIQEHAGND KSCVWHAADF SDGELKDELF
CIRFGSVENC KKFKETVQEV AESQHEGKEE DKKEASSTAG LLEKLSVDDK KEGGKELVKE
SSKTEDSEKK EEAPIAAA
//
