ID A0A0W8BWQ5_PHYNI Unreviewed; 939 AA.
AC A0A0W8BWQ5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine/threonine-protein kinase drkA {ECO:0000313|EMBL:KUF76267.1};
GN ORFNames=AM587_10006838 {ECO:0000313|EMBL:KUF76267.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF76267.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF76267.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF76267.1}.
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DR EMBL; LNFO01005840; KUF76267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8BWQ5; -.
DR STRING; 4790.A0A0W8BWQ5; -.
DR EnsemblProtists; KUF76267; KUF76267; AM587_10006838.
DR OMA; SIIVWEV; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:KUF76267.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:KUF76267.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 134..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 358..637
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 677..933
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 705
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 939 AA; 104191 MW; 05BFCA1A0FF676F4 CRC64;
MTDTPTRVSM AKVIPRDASG KVTDMVRSSG RSGTNQLSKN ESPLYTLPSP KTPNGVSSAP
VSPQKGTRLH IMGASMHDLK LNHIFRPRAS RHGETPSRQE DIGISFVSLE FSNAEMEQRF
TLARCVKYQT RLKFGAGFTA FFIPLLVIMQ VSFKANSEDG GKWTQLPLVM VFPGVVTLMG
ILVILFQHFF MTHMRWLTLV CLIGQISALL DTTAAGTMVS ERNIWVQFIF SLGITSSTGL
TFLKSTTVLV CSSIFFLILA WVRFASKTST EQLSAPGTVS AAIILYSILL CFLSWNWEYE
ERRDFVLTER LAQENVMVQM TMEMTGWFSG GAADQSPDNR SDAGGILSAN CHIDPKDVLV
KEELGEGTFG CVYAATWKET RVAVKKITLQ GDTKSIVTSF GSEASVMAQL RHPNVVMFMG
VMVHPEFVGL VMELCPKGSV YSVIHNNDVK IDWSLLLRMM VDSSRGMHFL HSSKPPILHR
DLKSVNLLID ADWRCKVSDF GLSKLKAFRE DRNDASMNAN TNTGNTPNVS RVFIGSSVWI
APEVFKGEEH TEKTDVYSFG VIIFEALSSS VPYNSISVDA VPFVVQAGKR PIDFHALELP
EGDAMQDLYT LMTRCWSAEI YARPSFSVII STLQSILTKH CGDEKWEDHI IYPDRKIVSA
SNAPADDDGL SIREEDLVID SAIGRGVFGV VYKGSYFGTP VAIKKLHVSG VPKNTLVEFE
KECSIMKGLH HPNIVLFMGS CSKPPTLLLV TELLANGSFF DIYHKMPRPE PARQLRLAYS
IAFDMAKGLA YLHNHNPIVI HRDLKSQNIL LDDRMRTKIA DFGLSKFRDV GKTMSICGSP
LWVAPEVLRG EKYGTPCDVY SFSIIVWEAL AWGEPYPDLG SSDIMNGVAG GNLRPTVPDG
TPTALARLLE ECWTKKQDQR PTFNELVPRL EAMGKDFGV
//
