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
//