ID A0A2H3TID1_FUSOX Unreviewed; 440 AA.
AC A0A2H3TID1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=FRV6_07033 {ECO:0000313|EMBL:SCO82820.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO82820.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) 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};
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DR EMBL; FMJY01000004; SCO82820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3TID1; -.
DR VEuPathDB; FungiDB:FOC1_g10009309; -.
DR VEuPathDB; FungiDB:FOC4_g10010892; -.
DR VEuPathDB; FungiDB:FOIG_15631; -.
DR VEuPathDB; FungiDB:FOMG_04492; -.
DR VEuPathDB; FungiDB:FOXG_02505; -.
DR VEuPathDB; FungiDB:FOZG_04670; -.
DR VEuPathDB; FungiDB:HZS61_010381; -.
DR OrthoDB; 1615316at2759; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR47634; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47634:SF9; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SCO82820.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 52..431
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 440 AA; 50211 MW; 1F1CBDBB0DCE1D2C CRC64;
MAEISDSPPP TPTAPFKRRL KNFTSPGENP AKYRPGGYHP VNLGDIFNDG QYKAIRKLGE
GCFSIVWLAH DLRNSRYVAL KILVSDQADQ SQEVEILHHL AKIAPSEAPQ RTTQILAEFE
HKGPNGTHKC LVFEPMGPSV NQMILEFAYR EDKFPSEIKY PPQMAKRILR DSLKGLAFLH
KNGISHADFQ PGNMLFSLNN IDFCDEAALC QEETPDEEYR IERLDGKKDK WAPEYLLTAE
PLASHTSIDE NLEVKLADMG GAYFLNDPPE EPVVPRALRA PELVLKGEFD KAQDIWSFGC
LVFELIAGRH LFYVCGPFKD ETEPDDEHLL EIQDRLGPLP DELYSHWKTS SRYYTKDRKL
YNWALGGVEE GEEPNMPKPS MLSTMEEAFD KESSDMTKEE AQEVKKLIRW ILQYDPAKRP
SAEEILRHPW FAEDSSEKAE
//