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Database: UniProt
Entry: A0A444YEW6_ARAHY
LinkDB: A0A444YEW6_ARAHY
Original site: A0A444YEW6_ARAHY 
ID   A0A444YEW6_ARAHY        Unreviewed;      1033 AA.
AC   A0A444YEW6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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_B07g088592 {ECO:0000313|EMBL:RYR00473.1};
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:RYR00473.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR00473.1, 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:RYR00473.1};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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:RYR00473.1}.
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DR   EMBL; SDMP01000017; RYR00473.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A444YEW6; -.
DR   Proteomes; UP000289738; Chromosome b07.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 2.60.120.430; Galactose-binding lectin; 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; IPR032675; LRR_dom_sf.
DR   InterPro; IPR021720; Malectin_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; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR   PANTHER; PTHR48006:SF68; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 4.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF11721; Malectin; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 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}; 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..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..1033
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019006300"
FT   TRANSMEM        624..646
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          685..961
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         713
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1033 AA;  114056 MW;  F2CEB9241B04DF7D CRC64;
     MENNLDHCCC SKLLLFLLLG STSLVFLSHL ASAATPKLNI EEVKALKEIG KKLGKKDWDF
     GVDPCSGEGN WNMSDKKSFQ SFVACDCFSF NQSSCHLVSI YLKAENLSGT LSPEFSKLHY
     LKILDLSRNL ITGSIPQQWA SMNLVELSLM GNKLSGPFPK VLTNITTLKN ISIEGNYFTG
     PIPNEIGKLI NLEKIILSSN GFTGTLPASL SKLTKLNDLR LSDNSFSGRI PDFISNWTSI
     EKLHMQGCSL EGPIPSSISA LTRLSDLRIS DLKGTKGSSF PPLSNMKSMK TLILRKCLIK
     GNIPDYIGRM EKLKMLDLSF NGLSGKIPES FSNLDKLDYM YLTGNMLSGT IASWILRTSK
     NVDISSNNFN WDSSSPVECQ RGGTLNLVEG YSSSADTQSR IPTCLKRNFP CPASVTKYSH
     SMNINCGGPE ANVSGRVYEV DREGRGASML YYPTQGWALS STGNFMDNDI DSDPFIVTNA
     SRLVNVSALN SELYTTARVS PLALTYYGLC LINGNYTVEL HFAEIMFIND RSFYSLGRRI
     FDVYIQGKLV LKEFDIQKAA GGTGKPIVKT FNATVTEHTL KIHFYWAGKG TTGIPTRGVY
     GPLVSAISVE PNFPVPSENG HKSYIILLAA CIVAAVGVLV LILLGVMRRK GYIGGSNAVY
     KELRGIDLQT GLFTLKQIKA ATKNFDVANK IGEGGFGSVY KGLLLDGTVI AVKQLSSKSK
     QGNREFVNEI GMISGLQHPN LVKLYGCCAE GNQLILIYEY MENNCLSRIL FGKDLDRKVK
     LDWPTRKKIC LGIARALAYL HEESRIKIIH RDIKTSNVLL DKDFNAKVSD FGLAKLNEDD
     KSHVSTRIAG TIGYMAPEYA MRGYLTDKAD VYSFGVVALE IVSGKSNTNY RPNEEFVYLL
     DWAYVLQERG NLLELVDPDL GSEYSTKEAM VMLNVALLCT NASPTLRPTM SQAVSMLEGW
     TDIQDILSDP GYSAYSSNSR YKSMRNHFWQ NPSRSQSMST YSTMYADANS SHSLIETEGS
     YHLVKVNSDM SDN
//
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