ID V9F7T3_PHYPR Unreviewed; 1022 AA.
AC V9F7T3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=TKL protein kinase {ECO:0000313|EMBL:ETI46818.1};
GN ORFNames=F443_08856 {ECO:0000313|EMBL:ETI46818.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI46818.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI46818.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI46818.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) 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:ETI46818.1}.
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DR EMBL; ANIZ01001506; ETI46818.1; -; Genomic_DNA.
DR AlphaFoldDB; V9F7T3; -.
DR EnsemblProtists; ETI46818; ETI46818; F443_08856.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_011442_0_0_1; -.
DR OrthoDB; 75958at2759; -.
DR Proteomes; UP000018721; 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; cd00637; 7tm_classA_rhodopsin-like; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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:SF975; DUAL SPECIFICITY PROTEIN KINASE SPLA-RELATED; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ETI46818.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 284..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 572..591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 409..668
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT DOMAIN 692..978
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 730
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1022 AA; 113994 MW; 19B3CA2725E58ED0 CRC64;
MASVAAPDKR RKKPRPPPPL LPLESRTSDF PTGSSESSVV PELPATFDMS ANSNASTASE
MTSTSSTSAS SSSRGIKWWK RVTGMRPKRR RTASREDRRS LDQELYVRSI LESYASSMSS
KDRYSTSNPQ FSVDENSSNS SKKSSERVSR RRREERDKTD TQDVTTITTT TTATDSDRRE
DRDSDSPAYM AHFTPNGDTA QAEHRVDMDN HSQPHLTAGV PGLSSGSSPG PYDDVLDDGP
FAPSSVSDDE DRNRRRLRRR MKIEAMRARL LEKNQHRARA RKKMCIFIAC IGVTLTAFVV
AAVLIARVGV EIQSNSLESS TNTTTTNSSS SDNDSGSGSV FVVSSGSIAS EADFSLTNSG
ASALDGLSSS SADSDDDLAW SDSDDDYSSI YSNTYTYIHC ILMVLSLWMS LVVVIMHVTF
RSFRTYSHPF VLELSCVQCG YWITSLLRVM LETSTLSDMT YLFFCMFECF FNFAQISFTC
AIAFNMYRSV VSYADVLMDS QSAKRRYRRY TMNVLLLSVV AAVTLALVGY RSGDTYDYYD
EDESESGSSS ATEEEILDEE TFSPCLYPTC RLILYVYYPL LAFAFNFIFY VRFKRTIGES
YPTSATGRLN KVARSYLIVF FVCWGSLIIL TALKVADSSN VPTIASFVMQ SIFDILGVCT
AAITFTNFHR CRKAFDFGLS LKAIDPNSIE FDDPVNIVGE GTFAIVLKAR WRQGGYIDGS
VSRSIEVAVK TFKHAQMECL EHVKEEAYLS SKLVHPCVMM TYGCYTSGIN LYIVYEYLGG
GTLQDLIDAN RTTPFTYERG LRYAHMIAVG MRFLHGLPVP IVHRDLKPLN CIFDSEQEML
KVADFGESRL LRTRDVVAPR PNFFPSADVT VQMTTNIGSA CWAAPEVLKD EATSEYSVKI
DVYSFGVICW QLYTCAVPYA DIPGSVLAVA EAVLSGVRPP IPRNCPRLFT KIMKRCWHDN
PLRRPSFEDI VQLLEIELTE VRRRQLARAH GRGNDSVIAP PTLDSSNFDD TGRAQGMEGS
YK
//
