ID A0A428SG87_9HYPO Unreviewed; 664 AA.
AC A0A428SG87;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CEP52_015115 {ECO:0000313|EMBL:RSL88757.1};
OS Fusarium oligoseptatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSL88757.1, ECO:0000313|Proteomes:UP000287144};
RN [1] {ECO:0000313|EMBL:RSL88757.1, ECO:0000313|Proteomes:UP000287144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62579 {ECO:0000313|EMBL:RSL88757.1,
RC ECO:0000313|Proteomes:UP000287144};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-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. STE Ser/Thr
CC protein kinase family. COT1 subfamily. {ECO:0000256|ARBA:ARBA00038271}.
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:RSL88757.1}.
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DR EMBL; NKCK01000255; RSL88757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428SG87; -.
DR STRING; 1325735.A0A428SG87; -.
DR Proteomes; UP000287144; Unassembled WGS sequence.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21776; MobB_Sid2p-like; 1.
DR CDD; cd05600; STKc_Sid2p_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF417; CELL CYCLE PROTEIN KINASE DBF2-RELATED; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000287144};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 264..567
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 568..647
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 664 AA; 75658 MW; 0B1ED820B5651319 CRC64;
MASFMANFFP GGKDRNAGDS NLPRPATPKS DNFINPPSTP QGSPSKKTNP PGANDLPAAF
DHAMTLTPSL EPPLRLGRPQ SVVTPLSLSP GKSSNAQPLD ESSANVDDSV IHKSRSGSPL
KKQGQENTPP ASRLAGTDSP HQHNHAALSR QQHYEHRDHR DRPTTPGTKR FNTARGLTAE
EREILQKPNV KRMVNVTQLY FLDYYFDLLT YVGARQNRLA AFKTEYPPPP ETDEETHSKM
WTKYAGRERA NLRKRRVRLR HGDFQILTQV GQGGYGQVFL AQKKDTREVC ALKVMSKKLL
FKLDEVRHVL TERDILTTAQ SEWLVRLLYS FQDEKSIYLA MEYVPGGDFR TLLNNTGVLS
NRHARFYIAE MFCAVDALHQ LGYIHRDLKP ENFLVDSTGH VKLTDFGLAA GVLAPSRIES
MRIKLEKASE TAVPFGKPMD QRTVAERRES YRTMRENDVN YAKSIVGSPD YMAPEVLRGE
EYDFTVDYWS LGCMLFEALT GFPPFAGATP DETWRNLKHW KEVLKRPVWE DPNYFLSNRT
WNFITTCINS RTRRFSNIKD ICAHHYFAEV DWETLRQTRA PFVPELDSET DAGYFDDFTN
EADMAKYKEV HEKQQALETM AEREDQMSKS LFVGFTFRHR KPAGEDGSSP RKRIPTDDTF
GTML
//
