ID V9FCS6_PHYPR Unreviewed; 831 AA.
AC V9FCS6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=F443_07750 {ECO:0000313|EMBL:ETI48202.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI48202.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI48202.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI48202.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:ETI48202.1}.
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DR EMBL; ANIZ01001351; ETI48202.1; -; Genomic_DNA.
DR AlphaFoldDB; V9FCS6; -.
DR EnsemblProtists; ETI48202; ETI48202; F443_07750.
DR eggNOG; KOG1290; Eukaryota.
DR HOGENOM; CLU_000288_81_9_1; -.
DR OrthoDB; 912242at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
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 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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47634; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47634:SF9; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00069; Pkinase; 2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ETI48202.1};
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}.
FT DOMAIN 134..814
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..199
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 64..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 831 AA; 93676 MW; 853D0F316A89D2D8 CRC64;
MDAPAARSAI SSSSAKKGPP AAKKTRNRKK KGRGAVPAPP VAAASVATPS SSPEALEEAE
SGSFRSAEGS TSTARRSFSP LSGSSSQRYS SEEEEEENYE EDEYSSESEE EGESSYKPGG
YHRVLVGEMY NSRFEVLEKL GWGHFSTVWK CLDRQTGAMV AMKVQKSARH YTEAAKDEIE
LLECTVHAAR TEYESVEQQE AIKVIRLVDS FEHKGPNGVH VCMVFEMMGD NLLTLIKYYN
YRGVPMQLVQ RLTRDMMEGL AFLHDKCQII HTDLKPENVL LSHHIPQLPK IRKAQWEAFR
TMRQKARNGG TTIAPTCGAD GTPMSKEEKK RLKNRLKKKR QKQKKQGGAV DREASVDDMV
ANGKMDSTAR PTLTSNSVNK LSNNLSQLSI SSSTENESAD DAFVSNFTGQ GANTDTCMSS
DSTRTWYYQV GQLGDEEDKD WIHLPPEFAA RVMLLLPEGR VAGSKRKERE FTLSVSTNSA
VGTEDEVVET SFVLRYLDHV DDDVISSIEE KMLKLREDSS PRKSTSTKAK YRLWRLEFDA
RYTHAVLDYL ERRVDGLRFL NVATSSGIAL PGFFLPKPPS NEDIKSAAKK MENSKNDDAL
VDVVIQGINL LPLAASEDTK SLEVNPLQLR LGRWARRFNK LANSEMFNLM KLDAKICDLG
NACWTTKHFT NDIQTRQYRC PEVILGKRYD TSADIWSMAC FVFELLTGDL LFDPKSGRNF
NRDEDHLAQM IELLGRMPKS FTGSQRGLRE FFNRKGDLKR IRNLKFWSLQ QVLIEKYHFS
RHDAESLASF MGPMLRYDPS KRATAEECLA HPWLAHVDDI EELTDDKKDG E
//
