ID A0A444XJC0_ARAHY Unreviewed; 412 AA.
AC A0A444XJC0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=Ahy_B09g096244 {ECO:0000313|EMBL:RYQ89774.1};
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:RYQ89774.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ89774.1, 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:RYQ89774.1};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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:RYQ89774.1}.
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DR EMBL; SDMP01000019; RYQ89774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444XJC0; -.
DR Proteomes; UP000289738; Chromosome b09.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd14066; STKc_IRAK; 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; PTHR47984; OS01G0323000 PROTEIN; 1.
DR PANTHER; PTHR47984:SF14; OS01G0323000 PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..412
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 114..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 412 AA; 45597 MW; 456BD42729A8F78D CRC64;
MGSDLKVELS KKTPIFGIKV WEVIGIAVGL FIIVILCVLS FCLSSRKKSK KDRDNKVPVS
QIPTVSKEIK EVRVEQVPAN GFVPRDGILL TIHDKSSDRE SDKVMVHLGV GKMKHGDSGS
HSDSFHHLEK DGYGSQSGEE GSSGTFKAAY NPSSSYPITA PSPLSGLPEF SHLGWGHWFT
LRDLELATNR FSKENVLGEG GYGVVYRGQL INGTSVAVKR ILNNIGQAEK EFRVEVEAIG
HVRHKNLVRL LGYCIEGTHR ILVYEYVNNG NLEQWLHGAM RHHGYLTWEA RIKILLGTAK
ALAYLHEAIE PKVVHRDIKS SNILIDDDFN AKVSDFGLAK LLGAGKSHVT TRVMGTFGYV
APEYANTGLL NEKSDVYSFG VVLLEAITGR DPVDYGRPPQ EVSKFSIYHH HL
//
