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Database: UniProt
Entry: F0WPQ9_9STRA
LinkDB: F0WPQ9_9STRA
Original site: F0WPQ9_9STRA 
ID   F0WPQ9_9STRA            Unreviewed;       449 AA.
AC   F0WPQ9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   08-NOV-2023, entry version 44.
DE   SubName: Full=Protein kinase putative {ECO:0000313|EMBL:CCA23310.1};
GN   Name=AlNc14C189G8401 {ECO:0000313|EMBL:CCA23310.1};
GN   Synonyms=AlNc14C235G9372 {ECO:0000313|EMBL:CCA24354.1};
GN   ORFNames=ALNC14_094530 {ECO:0000313|EMBL:CCA23310.1}, ALNC14_104980
GN   {ECO:0000313|EMBL:CCA24354.1};
OS   Albugo laibachii Nc14.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA23310.1};
RN   [1] {ECO:0000313|EMBL:CCA23310.1}
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:CCA23310.1}
RP   NUCLEOTIDE SEQUENCE.
RA   MacLean D.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   EMBL; FR824234; CCA23310.1; -; Genomic_DNA.
DR   EMBL; FR824280; CCA24354.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0WPQ9; -.
DR   EnsemblProtists; CCA23310; CCA23310; ALNC14_094530.
DR   EnsemblProtists; CCA24354; CCA24354; ALNC14_104980.
DR   HOGENOM; CLU_038648_0_0_1; -.
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; 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; 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; PTHR44329:SF146; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE; 1.
DR   PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00220; S_TKc; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CCA23310.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304}; Transferase {ECO:0000313|EMBL:CCA23310.1}.
FT   DOMAIN          178..441
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   449 AA;  51483 MW;  65457689884E25B6 CRC64;
     MKYDALNQFA FRRRSRIAQN DNKPSITMET FFGTVGSPIK MSKLEPAKYD EPMHSPVHSN
     RTYQRNSLPD IYSTDLLKKG ENLALGEENA DDIPTIRNPQ RQQEAKRSPK FIGKPAKPLE
     QLKLDGAKMA QIPRFISPWF HEGDKEGRIK PKIKEPRPQL VHAHSPLAHS ENIPVSDLEL
     GRVIGQGAFG KVHEGRWRGR AVAIKVLICQ DLRHDIMKEL ESEVRIMSVL RHPNICRLLG
     ACMDPQHRAL VVELSQRGSL WSVLRNSRRS LTLDMRTRFL YDTAKGMSYL HHFERPILHR
     DLKSPNLLVD ANYTIKLSDF GLARVKAHVQ TMTGNCGTVQ WMAPEVLGHQ KYTEKADVFS
     FAIVIWEVMT GRCPYDGMSQ IHVALGVLNR NLRPSIPRDC PPFFARLMKS CWNRQPELRP
     SFPHIVSAFR SYQSKLMHQD VRLHLKNTA
//
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