ID A0A444XXE0_ARAHY Unreviewed; 1478 AA.
AC A0A444XXE0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 29.
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_B08g089357 {ECO:0000313|EMBL:RYQ94449.1};
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:RYQ94449.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ94449.1, 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:RYQ94449.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:RYQ94449.1}.
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DR EMBL; SDMP01000018; RYQ94449.1; -; Genomic_DNA.
DR STRING; 3818.A0A444XXE0; -.
DR Proteomes; UP000289738; Chromosome B08.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 2.
DR CDD; cd01098; PAN_AP_plant; 2.
DR CDD; cd14066; STKc_IRAK; 1.
DR FunFam; 1.10.510.10:FF:000060; G-type lectin S-receptor-like serine/threonine-protein kinase; 1.
DR FunFam; 2.90.10.10:FF:000001; G-type lectin S-receptor-like serine/threonine-protein kinase; 2.
DR FunFam; 3.30.200.20:FF:000145; receptor-like serine/threonine-protein kinase SD1-8; 2.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 2.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR32444:SF234; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 2.
DR Pfam; PF08276; PAN_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00954; S_locus_glycop; 2.
DR SMART; SM00108; B_lectin; 2.
DR SMART; SM00473; PAN_AP; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS50927; BULB_LECTIN; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50948; PAN; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022527};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 459..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1245..1266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..166
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 306..343
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 362..445
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 520..798
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 827..952
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 1092..1129
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1148..1231
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 1302..1478
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 1478 AA; 166244 MW; BC7AFDD616F63B5F CRC64;
MHDADVHLIL AYVEFMIITT THKLQYEVML AYMLSSSSLA IELDSIHVSQ SLSDGMTLVS
QGGKFELGFF SPGNSSHKRY LGIWYKKIPI QTVVWVANRA NPINDFSGIL TMNSTGNLLL
TKNGTETTFW STISRKQAKN PVLELLESGN LVLRNEEESN PKAYLWQSFD YPSDTFLPTM
KLGRDLRNGF NRRITSWKSP NDPSPGDLSI GLVLNDYPVY YMMNGTKKLF RAGPWNGLYF
SGEPNLSHTY IFEVSFVTNK DEIYFSFNTK VDSITGRGVI SQTSQSLAHY LWDDNLKNWK
FSGSWPGDVC DKYDLCGAYA YCSVAESKHV CQCFKGFSPK SPEEWNSNNS SQGCIRDKPL
SCNVTTSDVF VKYTGLKVPD TQHTKVDENI TLDECRNLCL KNCSCMAYTN SDIRGGGRGC
AMWFGNLIDI KMIQSGGQDL YIRMPAFESG FQQRHKKKVI IASTIAAFCA TLLLCVYVIY
RIRRNNIEKS KIEEYMEGHV NDTDLPLFDL LTITTATHKF SLNNKIGQGG FGPVYKGKLA
DGLEIAVKRL SHSSTQGMTE FITEVKLIAK LQHRNLVKLL GCCIQGEEIL LVYEYVVNGS
LDTFIFDQTK GKLLDWPQRL GIIFGITRGL LYLHQDSRLR IIHRDLKASN VLLDDKLNPK
ISDFGTARTF GGDQTEGNTN RVVGTYGYMA PEYAIDGLYS IKSDVFSFGI LMMEIICGTK
NRALCHANQT LNLIGYAWRL WKEEKALELI DSSIKESCVI SEVLRCIHLS LLCVQQYPED
RPTMASVLLM LASEMDLVDP KEPGFFPKRV SIEANSQPHQ CEVSTNDDLT ITSLDGRDGM
TLVSQGGKFE LGFFSPGNSS HKRYLGIWYK KIPIQTVVWV ANRVNPINGS LGTLTINSTG
NLLLTENGTE TTVWSTSTIS QKQAKNPVLK LLDSGNLVLR NEGESNPKAY LWQSFDYPTD
TFLPTMKLGR DLRKGLDWRI TCWKSPNDPS PGDFSLGLVV RDYPVYYMMN GTQKVYRSGP
WNGLYFSGFP DLSFTYVFED SFVTNKDEIS YSYNTKVDSI IGRGVISQTS QSLTSYLWDD
NLQNWKVSAS TPGDVCDKYD LCGAYAYCSV AESQHLCQCF KGFSPKSPEE WNSNNSSQGC
IRDDPLSCNV TSTDVFVKYT GLKVPDTQHT KLHENINLDE CRNLCLKNCS CMAYANSDIR
GGGSGCAMWF GDLIDIKLFQ NGGQDLYIRM PAFESGLQHR HKQKVIIAST IVAFCATLLL
CVYVIYRVRR NNIEKSNIEE YVNDTDLPLF DLLTITTATH KFSLNNKIGQ GGFGPVYKGK
LADGLEIAVK RLSHSSTQGM TEFITEVKLI AKLQHRNLVK LLGCCIQGEE ILLVYEYVAW
RLWKEDKALE LIDSSIKESC VISEVMRCIH VSLLCVQQYP EDRPTMASVL LMLASEMDLD
EPKEPGFFPK WVSMEANSQP HQCELSYDEL TVTSLDGR
//
