ID A0A7N2LIC7_QUELO Unreviewed; 807 AA.
AC A0A7N2LIC7;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
OS Quercus lobata (Valley oak).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Fagaceae; Quercus.
OX NCBI_TaxID=97700 {ECO:0000313|EnsemblPlants:QL04p082421:mrna, ECO:0000313|Proteomes:UP000594261};
RN [1] {ECO:0000313|EnsemblPlants:QL04p082421:mrna, ECO:0000313|Proteomes:UP000594261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SW786 {ECO:0000313|EnsemblPlants:QL04p082421:mrna,
RC ECO:0000313|Proteomes:UP000594261};
RX PubMed=27621377; DOI=10.1534/g3.116.030411;
RA Sork V.L., Fitz-Gibbon S.T., Puiu D., Crepeau M., Gugger P.F., Sherman R.,
RA Stevens K., Langley C.H., Pellegrini M., Salzberg S.L.;
RT "First Draft Assembly and Annotation of the Genome of a California Endemic
RT Oak Quercus lobata Nee (Fagaceae).";
RL G3 (Bethesda) 6:3485-3495(2016).
RN [2] {ECO:0000313|EnsemblPlants:QL04p082421:mrna}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JAN-2021) to UniProtKB.
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 ECO:0000256|PIRNR:PIRNR000641};
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 ECO:0000256|PIRNR:PIRNR000641};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR EMBL; LRBV02000004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_030966723.1; XM_031110863.1.
DR AlphaFoldDB; A0A7N2LIC7; -.
DR EnsemblPlants; QL04p082421:mrna; QL04p082421:mrna; QL04p082421.
DR GeneID; 115987333; -.
DR Gramene; QL04p082421:mrna; QL04p082421:mrna; QL04p082421.
DR InParanoid; A0A7N2LIC7; -.
DR OMA; KTWIWIL; -.
DR OrthoDB; 4062651at2759; -.
DR Proteomes; UP000594261; Chromosome 4.
DR GO; GO:0005886; C:plasma 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 CDD; cd01098; PAN_AP_plant; 1.
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; 3.30.200.20:FF:000195; G-type lectin S-receptor-like serine/threonine-protein kinase; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
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 InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR27002:SF926; OS07G0535800 PROTEIN; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000641; SRK; 2.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50948; PAN; 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|PIRNR:PIRNR000641};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Reference proteome {ECO:0000313|Proteomes:UP000594261};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..807
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029498475"
FT TRANSMEM 408..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..168
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 319..396
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 490..765
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 518
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 807 AA; 90809 MW; 2DC4BE5D20E69468 CRC64;
MATTNILLVH LLTLVLLLVF SSLWTPHVAD WVYVTSGNLS SIGDTLKPGD TLNSTSYLVS
QKGAFALGFF RRIDIISNDS YVGISDMADP KSPFNLYVWF GNRGQPFIKD KTGSLTLDNN
GTLKIVRQGE SPIILYSSGT NNTVATLYDN GNFVLKEVNF DGSTKRVLWQ SFDYLMDTLL
PEMKLGINHK TGQTWALTSW LTTDIPDYGA FSLEWDPKGL ELVIKQRGVV HWKSGILRNN
QFENISPDIT SMYDFKVVSN EDEEYFSFSN KNQSVLMSEW IITFLGQFKD LRGPDIGRAD
NCYSYDTSGG CQGWEQPVCR ERGDKFDVAA GYYVTGDSLS GNNYSLGISD CKAICWSNCS
CVAFTYQFAN ETGCRFWTGE TAVQSDHASD FVSIYLLSSS PHKGAKKWIW IGTVIVAALL
VIFFSILCYI QRRRKVVPRG NNVTKDENDL LDLVSLDQSP IVNQIPNDGK KGHDLSVFNY
AYVMTATNNF APQNKLGEGG FGEVYMGELL TGQKIAIKRL SRNSGQGILE FKNELILISK
LQHMNLVKLL GFCLHGEERM LIYEYMPNKS LDSFLFDANK SKLLDWQKRF GIIEGVAQGL
LYLHKYSRLR VIHRDLKASN ILLDENMNPK ISDFGMARIF QQNELEANTK RVVGTYGYMS
PEYAMEGVFS IKSDVYSFGV LMLEILSGRK NNSFFKTEHL FNLVGYAWEL WNEGTALDLM
DPALDDSYMD QMLRCVHVGL LCVEDSAIDR PAMSDVLAML TNDNLSLPSP KKPAFSLARQ
AIEAHIYDKE SECNSINWAS ISNMVPR
//
