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Database: UniProt
Entry: A0A445EDQ1_ARAHY
LinkDB: A0A445EDQ1_ARAHY
Original site: A0A445EDQ1_ARAHY 
ID   A0A445EDQ1_ARAHY        Unreviewed;       547 AA.
AC   A0A445EDQ1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Serine/threonine-protein kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Ahy_A02g007920 {ECO:0000313|EMBL:RYR73538.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR73538.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR73538.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR73538.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RYR73538.1}.
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DR   EMBL; SDMP01000002; RYR73538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445EDQ1; -.
DR   STRING; 3818.A0A445EDQ1; -.
DR   OrthoDB; 988261at2759; -.
DR   Proteomes; UP000289738; Chromosome a02.
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; cd21742; MobB_NDR_LATS-like; 1.
DR   CDD; cd05599; STKc_NDR_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:SF429; AGC KINASE; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   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:UP000289738};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          119..418
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          419..491
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          61..88
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   547 AA;  63336 MW;  0689AA97BA8831C2 CRC64;
     MENTRRWFSK FNSKDKMKSS KNKETVGMTK EGSKPPTNEE APSKVTKQKV EAAKQYIENH
     YKKQMQSLQE RKERRNMLEK KLADAEVSEE EQSNLLKYLE KKETEYMRLQ RHKMGTDDFE
     PLTMIGKGAF GEVRVCREKA TGHVYAMKKL KKSEMLRRGQ VEHVKAERNL LAEVDSNCIV
     KLYCSFQDEE NLYLIMEYLP GGDMMTLLMR KDILTEDEAR FYVGETVLAI ESIHKHNYIH
     RDIKPDNLLL DRNGHMKLSD FGLCKPLDCS SLQEKDFSIG VNRSGTLQSD GRPTAPRRTQ
     QEQLQHWQKN RRMLAYSTVG TPDYIAPEVL LKKGYGVECD WWSLGAIMYE MLVGYPPFYS
     DEPMSTCRKI VNWRTHLKFP EEAKLSAEAK DLICRLLCNV EQRLGTKGAD EIKAHPWFKG
     IEWDKLYQMK AAFIPEVNDE LDTQNFEKFE EVDKQTETSS KAGPWRKMLP SKDVNFVGYT
     YKNFEIVKDH ELPGIAELKK KNTKPKRPSI KALFDDESAM AANQQAKGSF LNLLPPQMEV
     PEKSGSQ
//
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