ID F0WH74_9STRA Unreviewed; 1086 AA.
AC F0WH74;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Protein kinase putative {ECO:0000313|EMBL:CCA20589.1};
GN Name=AlNc14C98G5941 {ECO:0000313|EMBL:CCA20589.1};
GN ORFNames=ALNC14_067320 {ECO:0000313|EMBL:CCA20589.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA20589.1};
RN [1] {ECO:0000313|EMBL:CCA20589.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA20589.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; FR824143; CCA20589.1; -; Genomic_DNA.
DR AlphaFoldDB; F0WH74; -.
DR EnsemblProtists; CCA20589; CCA20589; ALNC14_067320.
DR HOGENOM; CLU_009612_0_0_1; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06093; PX_domain; 1.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR PANTHER; PTHR24351:SF247; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCA20589.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 380..500
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 584..849
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 850..907
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 31..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1086 AA; 125734 MW; 041EC7AABBE8D93F CRC64;
MRSTSIILFL RSSHYLVLRR ARCHFTVEST EIGQKSDRDA SGNASLHTIP GTMKENHRLE
VASRANRSQN DHKKLWNTYQ ECTNSLSRTQ LHDQSISRTV LQGKNRHGCK KEVGRPMPGS
NSSSTTHNRK LYRPKTIQGD TRHTSEKTMQ GYNDLDSFAS DRDSHCFIDD RLRTHSTVSR
SKRPATSIIA RAKARPDTDR EGRIYHNSAD TDYWYRTSNP HAPSHTPHFT SEQERKSDSI
STQLLREKKK EMLDRNNRLS EHVHMADQYQ RNSIGLESDA SSSSSFQIDG FYRDFHPGMP
REHHDVARKS REDLNDTIEQ VVIPRWIVCN ASQIDSAEKE KSSYVTSSQI EKEEDEDISD
ISLNQPVSSV TRTSNRAGLF RKPLRKWAII ASKHESKQFT VFQLVVYYQS KRVSTLEKRF
SQFRVLHKLM CRENPAILQL KFPHRHFFSS MSLHVITQRK ECLELYINSL LSIAPRSRNL
HHFFSTDIVT GSFVDNNEEK SNFIFDPDQM RNENSSIHHQ SKPHRKQQGT QHSSPGSSSF
ELDRQSRLSR KSSQRNTCGS LKSFASFRYG SESEVEQLVT ISDFEILQVL GKGSFGKVYM
VRKHLTQEIF AMKVLRKAEL VKRNQVRHTM TERQVLTLIS HPFIVSMRYA FQTSSKLIMI
SDYCCGGEIF FHLKKFRSFS EAMVRFYAAE LIAALSHLHG HNILYRDLKP ENILLDQDGH
IQLTDFGLSK MKCSVFHGAK TFCGTPEYLA PEMLHSRKNK TQYGTAIDWW SLGTLIYEML
TGWPPFFDQN CDVMCTKILK APLRFPAQFG LSPVVRNLIA GLLHRDPAKR LGCRASHGGV
QELKLHPFFS NINWELLELR SVKPPFKPRI RSPTDTQNFD KMFTRETLDQ LTLRLSFCIA
GRMMRKPKAK SKKDSKHIES AKELVETVEQ LCNVYIDYKL DGKWNELLNV FEAPENTENW
NDIARICASQ HEVDSLSFWH LERLAMGELE TGRNAWTNEF ISFQKESEKS KILMQTILDK
GEEAERKRKH HEEAMKVQRE VVLQELQAAK DYQRRLYGKD DNHDREEMKP VSVKQRLLDA
IESAQK
//
