ID A0A225VR21_9STRA Unreviewed; 474 AA.
AC A0A225VR21;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=PHMEG_00020385 {ECO:0000313|EMBL:OWZ07247.1};
OS Phytophthora megakarya.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ07247.1, ECO:0000313|Proteomes:UP000198211};
RN [1] {ECO:0000313|Proteomes:UP000198211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT of cacao black pod achieved similar genome size and gene model numbers by
RT different mechanisms.";
RL Submitted (MAR-2017) 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. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
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:OWZ07247.1}.
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DR EMBL; NBNE01003613; OWZ07247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225VR21; -.
DR STRING; 4795.A0A225VR21; -.
DR EnsemblProtists; OWZ07247; OWZ07247; PHMEG_00020385.
DR OrthoDB; 70094at2759; -.
DR Proteomes; UP000198211; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05145; RIO1_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF1; SERINE_THREONINE-PROTEIN KINASE RIO3; 1.
DR Pfam; PF01163; RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OWZ07247.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198211};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 172..474
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 120..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..451
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 52963 MW; A822BA7B71AAF9CD CRC64;
MASTCPWGLP TEPAKAQPSM QDLMDEALAL SLYEEEVSAL QKEINPEYQS SVFANIQRSK
ERREENRNKE LLNADSVDVV TAASGEGSVA SSVLKRTPGV AAGAAALARA RVTGSLSMED
AAHGAGSGKG FTSLRESQRR QQKSVKKGFG AGRVETETHA TTDGVMDERT TLILQKMINR
GELDEVHGCV QSGKEAHVYF AVGTDEDTMR PVQLAVKIFR TTLNEFGNRH EYVTGDRRFD
LNFQKKDQRR QIKAWTEKEY RNLCRVAKCS IRAPTPIVCK EHVLVMQFVG ADGWPEPTLK
DVHAEMSPKQ QARAYADVLQ ATRALYQRAH LVHGDLSEYN ILFSIRDKRI WLIDFGQAVD
RSHPDTEKFL RRDLHTINRF FQRGDLLEAT ADEVGLISDD KAYEYVVSET PKDVVAEFSV
LSALLEALTD VPEAEEEESD EDEETQEEEE QKEVIQQDKA DASEAVNTQA IPEA
//
