ID W2ZST2_PHYPR Unreviewed; 759 AA.
AC W2ZST2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=F442_04326 {ECO:0000313|EMBL:ETP50392.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP50392.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP50392.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP50392.1,
RC ECO:0000313|Proteomes:UP000018948};
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., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:ETP50392.1}.
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DR EMBL; ANIY01000974; ETP50392.1; -; Genomic_DNA.
DR AlphaFoldDB; W2ZST2; -.
DR EnsemblProtists; ETP50392; ETP50392; F442_04326.
DR Proteomes; UP000018948; 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; 1.
DR InterPro; IPR019530; Intra-flagellar_transport_57.
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; PTHR44899; CAMK FAMILY PROTEIN KINASE; 1.
DR PANTHER; PTHR44899:SF3; SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF10498; IFT57; 1.
DR Pfam; PF00069; Pkinase; 1.
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 3: Inferred from homology;
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:ETP50392.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000018948};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..287
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 287..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 628..708
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 293..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 759 AA; 87068 MW; ECA79E78051B0476 CRC64;
MESLTDEQRA LFSDGGQLDD YEVLKPIGKG KFSVVYKAKR RHDNQAVALK KIAIFDMMNL
KAREKTLKEV RLVQSVGHPN IIQYLDAFVQ NNELYIAFEW AEAGDLKRQI RKANEKGVRF
DERTIWRYFT QLCGAILYLH QNRIMHRDLK PANIFLTLKG VVKVGDLGLG RYLSENTIEA
RSKVGTPLYM SPEVLRGESY DWKSDVWSMG CILYELAMLR SPFKSEGLNL VGLFQKINKG
YYEEIPEVYS DHLRGIVKRM ISLTPSDRPS VQEVWEFCRT RPPSAVLQER MRKHQAVSQS
NNSARPDSET RSTRTRSSRS KSTPESDNPS HPSSSDQQQE TPPQSRPSSQ GDASNTVSEE
SSRRRRAEAK MELLFERLRI LRYEKVLNKR ISPAYFASDI RTLPKVTPQS RFEDMCTLSN
WLISLLGGEV PRNDDQNDEP PIVSAQKILL AAEKAGVFAV AQLSAPTLTS GVGSEVCELL
DALTAAALSS EAYCTTPPEY PREPIDTLES CDELDVTDDD GQQNENVGES TTSLAFENDD
VFSRWVVVKE ENQYTAMIDD RENAMIYTDI DPVAWELERR RMLPKLHAVL QDKLQRRPAE
SSWRVRLDLV KAHAELIVAG QEDMQLDIAQ IQATRQKQTE QLERYEKQLN KRFLRARRLY
DESTTRLAKS QDQMHTAQES VNRATLEMVR LQAARSELAE AVQDAEERLT DNSMLLERKR
HVRRLIGENR ELSLRLQVLH DYWTRKQQHA MQCSHLDPV
//
