ID A0A137NPP0_CONC2 Unreviewed; 624 AA.
AC A0A137NPP0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN ORFNames=CONCODRAFT_80922 {ECO:0000313|EMBL:KXN64698.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN64698.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN64698.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN64698.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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}.
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DR EMBL; KQ965263; KXN64698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137NPP0; -.
DR STRING; 796925.A0A137NPP0; -.
DR EnsemblFungi; KXN64698; KXN64698; CONCODRAFT_80922.
DR OMA; QRRRTIC; -.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000070444; 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; cd13117; POLO_box_2; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 2.
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; IPR033695; POLO_box_2.
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; 2.
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|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361162};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000070444};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 24..279
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 428..496
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 528..606
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 624 AA; 71221 MW; 7F5DEDF24F031377 CRC64;
MAFKNFTAPA LPNKIYDKKK DKSYLVEKKI GEGGFASCYR VIDSSNKAFA CKAVYKPSLK
SEKHREKLKS EIKVHDSLNH PYICSLRTCF QDENYIYIIL ELCENQSLGD MIKRRKRVSE
EEARYFMLQM FSGIGYCHKN QVIHRDIKLG NVFLDSDMNV KIGDFGLAAQ LESEEDRKKT
ICGTPNYIAP EVLYDTKNGH SFKADIWSLG VMLYTLVIGI PPFQTKDANE IYKRIQVANF
SFPSDKKVSD EFKSCVKFIL NPDPEARPSL DQIKAHAFFD AFTPKELPQT AFYSAPDFTY
DIRQHELTRD MLKKQQATTE EAAASEQALQ TPSGNKRKLF HYQITPDKRS NVATAPSAQT
SATKAMRDAI LALPDMTNFS VIETMNFNLK QARSYIQAFN TIKGLERLTK YEPKVPVLIR
KWVDQGAKYG LAYELTDDTQ AVFFKDTTTF TLNPVSPKYH YLYTSSNATT SQPITQDSYS
INEIPEPLAK KAKLFDAYRN YMSSKLTSSI PTVPFAGFET PLYVTKFIKT TDAALFRLSS
NVIQINFKDH YKLVLSEDAC ILNLIHPSGE IITLKTIEVI ASHYKVNELQ PCFDTEDAYY
RLKYAQDMLQ GIIEKSRKKV TTEN
//
