ID A0A067C9N1_SAPPC Unreviewed; 519 AA.
AC A0A067C9N1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=AGC protein kinase {ECO:0000313|EMBL:KDO23532.1};
GN ORFNames=SPRG_10726 {ECO:0000313|EMBL:KDO23532.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO23532.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO23532.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO23532.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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; KK583252; KDO23532.1; -; Genomic_DNA.
DR RefSeq; XP_012205684.1; XM_012350294.1.
DR AlphaFoldDB; A0A067C9N1; -.
DR STRING; 695850.A0A067C9N1; -.
DR EnsemblProtists; KDO23532; KDO23532; SPRG_10726.
DR GeneID; 24132821; -.
DR KEGG; spar:SPRG_10726; -.
DR VEuPathDB; FungiDB:SPRG_10726; -.
DR OMA; TMMERRI; -.
DR OrthoDB; 3028764at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
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:KDO23532.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..148
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 174..433
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 434..504
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 519 AA; 59189 MW; B53A1414A3CDD5F2 CRC64;
MTWSVLDVVT ARIPTWNSQL ENQTARGGGQ RFTSFQITVQ GRSASWSLAK RYSQFRDLHL
GLCKRYASVR SLPFPPKRFF SSLSLRVIEQ RRLGLEGYVQ SLLAMRPRPH ELTPFLAPDA
DDNSMNDPAG RTPTSEIGST FTTQHAALDV VTPPIDLYLD TSFDPSRKWS VADFDILKVL
GKGSFGKVYL VRTRDDKNTL YAMKVLKKTE LIQRHQVDHT MTEREVMSAL KHPFIVALRC
SFQTESTLFM VSDYCCGGEI FFHLKKFRAF SESMVRFYAA ELISALGYLH SKNIVYRDLK
PENVLLDADG HLRLTDFGLS KKQVTSTSGA RTFCGTPEYL APEMLLSRKH KSMYGSAIDW
WSLGTLLYEM LTGWPPYFDR DVQKMCENIL IAPLAFPARF GISSAAKSLI RGLLERDPTK
RLQAPALKAH PFFQGLDWKA LEEKRLKPPF KPRLQSPTDL QNFDKEFTKD AVPNLVNEET
SSTSVEDEFY GFSFTYHHQA SPMLTESDML RLRRNHSIV
//
