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Database: UniProt
Entry: A0A445BPL2_ARAHY
LinkDB: A0A445BPL2_ARAHY
Original site: A0A445BPL2_ARAHY 
ID   A0A445BPL2_ARAHY        Unreviewed;       901 AA.
AC   A0A445BPL2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=Ahy_A09g046375 {ECO:0000313|EMBL:RYR40624.1};
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:RYR40624.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR40624.1, 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:RYR40624.1};
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:RYR40624.1}.
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DR   EMBL; SDMP01000009; RYR40624.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445BPL2; -.
DR   STRING; 3818.A0A445BPL2; -.
DR   Proteomes; UP000289738; Chromosome a09.
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   Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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; IPR032675; LRR_dom_sf.
DR   InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45631:SF207; LEUCINE-RICH REPEAT PROTEIN KINASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR45631; OS07G0107800 PROTEIN-RELATED; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51450; LRR; 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}; 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   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..901
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019261737"
FT   TRANSMEM        523..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          589..854
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         616
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   901 AA;  100262 MW;  5578B47BD2FEE360 CRC64;
     MMIINSLHYL FVLLGALSFL APVLGQDPSS GFISIDCGLP ENIRYIDKNT GINYISDVKF
     IDSGVSKSVS PQDKNTHQPQ FNYLRSFPNG VRNCYKINVT SGADYLIRAS FLYGNYDGLN
     KLPQFELHLG PNVWETVKFT NSSISVNYEI IHSPPQNHIH LCLANTDNGT PFISVIELRP
     LPNDTYSISI KSVGSLARLV RLDLGSITNL CIRYKDDLYD RLWEPYSDSE WTQLSTSLNT
     DELNNSVAST PPVIVMSTAA TPINSNASLD FTWDADTVTD SFHICMHFNE IQKLKANEAR
     LFNITLNGKL FYGPFAPIYR KTDTLCTTSP FDGFTTYQLS ILRTEFSTLP PIINGIEIYS
     VRNLSHLETE KDDADAITNI KVAYRVTRNW LGDPCCPEAF KWDGLDCNSI DGDGTPRITS
     LNLSTSGLTG HIIPDFLKLT MLKTLDLSNN NLTGDVPYFL AQLQSLQKLN LENNNLSGSI
     PNELLQKQRD GILSLSVGQN PNLCASTSCN PQTNDKRKKK SNAVIIVVAL MAGMLLLLVI
     AAVIIFRQRK PNDAAKNIIL GKPGNSINGS QLGSKQRQYS FNEVVKMTSS FDRVLGRGGF
     GTVYYGSIED TQLAVKMLSL SSVQGYQQFV AEASVNLLMR VHHRNLTSLI GYCNEETNIG
     LIYEYMKNGN LDEHLSGENN RKKSLNWKDR LQIALDAAQG LEYLHNGCKP PIIHRDIKCT
     NILLDENFHA KLADFGLSKC FAADGDTHVW TIAAGTPGYL DPEYTISNIL TEKSDVYSFG
     VVLLRIITGQ PVIIRMEDTT HHISQRVNSM VAEGDITKIV DSRLQGDFDN NSAWRTVEIA
     MASVSSISVE RPYMSDIVKE LKECLAVELT QKHNSCDFQN EDLIGQVSLN LISTDINPIV
     R
//
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