ID A0A2H3TZC5_FUSOX Unreviewed; 511 AA.
AC A0A2H3TZC5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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_11426 {ECO:0000313|EMBL:SCO87299.1};
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:SCO87299.1, 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; FMJY01000006; SCO87299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3TZC5; -.
DR VEuPathDB; FungiDB:FOC1_g10002526; -.
DR VEuPathDB; FungiDB:FOC4_g10001034; -.
DR VEuPathDB; FungiDB:FOIG_12612; -.
DR VEuPathDB; FungiDB:FOMG_15465; -.
DR VEuPathDB; FungiDB:FOXG_22101; -.
DR VEuPathDB; FungiDB:FOZG_08239; -.
DR VEuPathDB; FungiDB:HZS61_015801; -.
DR OrthoDB; 912242at2759; -.
DR Proteomes; UP000219369; 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; cd14136; STKc_SRPK; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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 SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 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:SCO87299.1};
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 59..478
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 511 AA; 56901 MW; 14A566E6C95CD076 CRC64;
MTSFLKSRSH QLSAMAHSPS SSSVDDAAEN TADEEDSEDY CKGGYHPVQV GEKFKDGKYT
VVRKLGWGHF STVWLSRDNT NGKHVALKVV RSAAHYTETA IDEIKLLNKI VQAKPDHPGR
KHVVSLLDSF EHKGPHGTHV CMVFEVLGEN LLGLIKRWNH RGIPMPLVKQ ITKQVLLGLD
YLHRECGIIH TDLKPENVLI EIGDVEQIVK RVVKPESAEK ENNRNGRRRR RTLITGSQPL
PSPLNTSFNQ SNLFPSPNTH SSLAGVLNEA GKSSNEASPK PSDDAQKQRE KSADLLSREV
SGISLDKSNS PSASTGEKRK AEDAHAFDVI SVKIADLGNA CWVNHHFTND IQTRQYRSPE
VILGSKWGAS TDVWSMAAMS GTKYGKDDDH IAQIIELLGP FPKSLCLSGK WSQEIFNRKG
ELRNIHRLRH WALPDVLREK YHFKEDEAKR IADFLTPMLE LVPEKRANAG GMAGHVWLED
TPGMKGLKIE GLEVGGRGEG IDGWATEVRK R
//
