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Database: UniProt
Entry: A0A445BYR1_ARAHY
LinkDB: A0A445BYR1_ARAHY
Original site: A0A445BYR1_ARAHY 
ID   A0A445BYR1_ARAHY        Unreviewed;      1031 AA.
AC   A0A445BYR1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=Ahy_A08g040287 {ECO:0000313|EMBL:RYR43895.1};
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:RYR43895.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR43895.1, 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:RYR43895.1};
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. Ser/Thr protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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:RYR43895.1}.
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DR   EMBL; SDMP01000008; RYR43895.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445BYR1; -.
DR   STRING; 3818.A0A445BYR1; -.
DR   Proteomes; UP000289738; Chromosome a08.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   GO; GO:0099402; P:plant organ development; IEA:UniProt.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48055; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR   PANTHER; PTHR48055:SF35; PHYTOSULFOKINE RECEPTOR 2; 1.
DR   Pfam; PF00560; LRR_1; 7.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00365; LRR_SD22; 5.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52047; RNI-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   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        675..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          750..1026
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         778
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1031 AA;  112557 MW;  72E1058062466852 CRC64;
     MLACLLWQAI SSSCDPLDSS ALKEFAGNLT KNNFMTSWSN DVSCCKWYGV ICGNVTGGGG
     GAASSRVTKL NLPGIGLNGT IPASLSKLDQ LIFLNLSFNH LGGRLPVEFS NLKLLRILDL
     SHNMLSGPVS AAISGLQSIQ VLNISSNSFD EDMLKLGEFP QLLALNMSNN SFNGRFNSRI
     CSSSKGLQTL DLSANHLVGG LEGLDNCAKS LQQLHLDSNS FTGTLPDSLY SFSALEQFSV
     SANNLSGQLS RELSKLSSLT ALVVSGNRFS GELPNVFQSL LNLEQLVAHA NSFTGPLPSS
     LAFCSKLKVL DLKNNSLSGQ IDLDFTGLSN LSTLDLATNH FNGSLPNSLS NCRELKVLSL
     ARNGLTGRIP ESYANLTMLS FVSISNNSLV DLSGALSVLK QCKNLTTLIF TKNFHGEEIP
     QNVTLGFESL LILAFGNCGL KGQIPPWISN CRKLGVLDLS WNNLNGSIPS WIGHTDSLFY
     LDLSNNSLTG GIPKSLTELR GLMSTNCTRP NLTVSSGIPL FVKRNKSASG LQYNQASSFP
     PSILLSNNML SGSIWPEIGH LKDLHVLDLS RNNISGTIPS TISEMENLEM LDLSYNDLVG
     SIPESFNNLT FLSKFSVAYN RLQGKIPDGV QFYSFPSSSF EGNLGLCGSI DLPCKNVPSL
     KPNSSSGSSR KRANVLGLTI GIGIGLALLL AIILLKMSKR EDKPVDNYDE ELSNRPHRLS
     EALVSSKLVL FHSDCKDLTV ADLLKSTNNF NQANIVGCGG FGLVYKAYLP NGTKAAVKRL
     SGDCGQMERE FQAEVEALSR AQHKNLVSLK GYCKHGNDRL LIYSYLENGS LDYWLHESVD
     GNSTLKWDVR LKIAQGAARG LAYLHKGCEP YIVHRDVKSS NILLDDKFEA HLADFGLSRL
     LQPYDTHVTT DLVGTLGYIP PEYSQTLTAT FRGDVYSFGV VLLELLTGRR PVEVIKGKNC
     RNLVSWVFQM KYENKEQEIF DPAIWHKDHE KQLLEVLAIA CKCLDQDPRM RPSIEVVVSW
     LDSVRFDVPQ Q
//
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