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Database: UniProt
Entry: F0VYV0_9STRA
LinkDB: F0VYV0_9STRA
Original site: F0VYV0_9STRA 
ID   F0VYV0_9STRA            Unreviewed;       506 AA.
AC   F0VYV0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Protein kinase putative {ECO:0000313|EMBL:CCA13965.1};
GN   Name=AlNc14C1G101 {ECO:0000313|EMBL:CCA13965.1};
GN   ORFNames=ALNC14_001080 {ECO:0000313|EMBL:CCA13965.1};
OS   Albugo laibachii Nc14.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA13965.1};
RN   [1] {ECO:0000313|EMBL:CCA13965.1}
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:CCA13965.1}
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; FR824046; CCA13965.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0VYV0; -.
DR   EnsemblProtists; CCA13965; CCA13965; ALNC14_001080.
DR   HOGENOM; CLU_000288_63_48_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; 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; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 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:CCA13965.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..122
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          168..424
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          425..503
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          124..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   506 AA;  57774 MW;  FF562C80572F7EE1 CRC64;
     MEFAKSIRFV GIIGHDNVSH NGSKTTVYYL QVEYESAMWV VKHRYQDFKE LHERLSSDGF
     RCPALPPKKF LGSFNPEFID KRQQELAFWL HLLSQTDPSN SGDHPRTNEH YKDFMLLNRE
     PMQEAHHKNG GQGDPSTLSN TDSTTSNPSS STDSEALYDT PKTCLDDFEL LKVIGKGSYG
     KVTLVRKKNS NRLFAMKSLH KSNVKRRNQV EHTKTERRVL GRAKHPFIVH LHYAFQTTQK
     LYFVLDYCPG GELFYHLSRM EKFGEAMAKF YAAEITLALQ HLHELGVVYR DLKPENILFD
     KQGHVMLADF GLAKEGITNG AEGTNSMCGT PEYLPPEILD RTGHGTAVDW WALGMVLYEM
     LTGLPPWYTR NRQKLFDRVR NAPLTFPDEV GEQARSLISG FLTRNPNERL GSRTAEDVKQ
     HLFFSDINWQ DLYDRNIRPP FNPCANVANM EEPKNFESEF TKMQIQSVEN SAIGSMRASD
     ASRPSMTFTE FTYNTPNDLA MGSAGK
//
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