ID A0A0B1P4P2_UNCNE Unreviewed; 949 AA.
AC A0A0B1P4P2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN ORFNames=EV44_g6216 {ECO:0000313|EMBL:KHJ33238.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ33238.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ33238.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(2014).
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=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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:KHJ33238.1}.
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DR EMBL; JNVN01001550; KHJ33238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1P4P2; -.
DR STRING; 52586.A0A0B1P4P2; -.
DR HOGENOM; CLU_000288_46_0_1; -.
DR OMA; SPWIDFY; -.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000030854; 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 CDD; cd13118; POLO_box_1; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50078; POLO_BOX; 2.
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};
KW Kinase {ECO:0000256|RuleBase:RU361162, ECO:0000313|EMBL:KHJ33238.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000030854};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 61..323
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 605..624
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 777..799
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 445..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 949 AA; 108607 MW; F73297655794F3DD CRC64;
MEALSPRDVN ANIRNNHNVK QIVKSSTVPV KITHEEKDHP PPPPSEVIEP KGINQKCGVT
YKTGQLLGRG GFAVCYEGQN TATYQKYALK IVKSHMPQKK MEQKFQTELQ IHSKMNQANI
VEFHKAFSYQ KCTYIVLELC PNGSLMDMVK KRKYVTEPEV RFWTVQMAGA IKYMHGKGII
HRDLKMGNIF LDKNMNVKVG DFGLAALLMS GKDLQACRRT TLCGTPNYIA PEILSKDKGG
HDHAVDIWSL GIIIFAMLTG KPPFQSATAD EIYRRARERD YYWPKFNTSE NIISEETKDL
VSELLQAPQE RPEPDKIVQH AFFTCGWTPK AEEMTTSLRE KHPNEFQFSS IDREDKMASS
LQNLKNICIQ CEVGPWTLPR KYTSTYREVE EEEKLGLTPA VPLVEGVVYR PFHIWLQEQM
VNFKNNGEST VNILKLLKEV VSPLPRKNSK NGNSLRSSNR IGTTQRVKSQ KLNSQAQIGE
EKKNNAAFNI SKKKSTYKLN KSEPEAKQDV NDQLAVNMFN KLDINDIKRD HRRECEANSI
SREPFSIFHK KDGVKVVPDS KPDFILSRLR RLQDELERSL GSRSFATDSH IPKETPVIVV
KWVDYTNKYG LGYILSNGSV GTIFKAIPAF PQDPKKGLSP PSCVLVRDSE KHLLNQNNPN
WIDYGQLVPV TGHKIEFYEN RGDQGFFKAE VDAVNFKSIP GLNGEMFKLG IGRDEYDSRK
KERIAIWRKF GNYMTQYGRD TDYPYDRNSD AYPEAESSAA NFVNFYQRWG DVGCWGFDDG
HLQFNFPDHT KIILSADGKW CDFYHLSLEA AQDLHEKGVL SPQALDERQH LSYPLQTILN
FTARTIRTRS NRLPEIDPMI LDIPQANDFR RKIEFIVLCI KEWTTNGGMG ISDLSVKGRL
RWNGARQRID TKAPYKQVWV CVGGRATEER KVMWFDPRVP DLISPDIEL
//
