ID A0A6A3BD72_HIBSY Unreviewed; 832 AA.
AC A0A6A3BD72;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, 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};
GN ORFNames=F3Y22_tig00110187pilonHSYRG00284
GN {ECO:0000313|EMBL:KAE8714936.1};
OS Hibiscus syriacus (Rose of Sharon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX NCBI_TaxID=106335 {ECO:0000313|EMBL:KAE8714936.1, ECO:0000313|Proteomes:UP000436088};
RN [1] {ECO:0000313|EMBL:KAE8714936.1, ECO:0000313|Proteomes:UP000436088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Baekdansim {ECO:0000313|Proteomes:UP000436088};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAE8714936.1};
RA Kim Y.-M.;
RT "Draft genome information of white flower Hibiscus syriacus.";
RL Submitted (SEP-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 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}.
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:KAE8714936.1}.
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DR EMBL; VEPZ02000867; KAE8714936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A3BD72; -.
DR Proteomes; UP000436088; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd01098; PAN_AP_plant; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR FunFam; 2.90.10.10:FF:000005; G-type lectin S-receptor-like serine/threonine-protein kinase; 1.
DR FunFam; 3.30.200.20:FF:000330; G-type lectin S-receptor-like serine/threonine-protein kinase At4g03230; 1.
DR FunFam; 1.10.510.10:FF:000467; Liguleless narrow1; 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; 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 InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR27002:SF1095; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE RKS1; 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 Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
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; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50948; PAN; 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 EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW Lectin {ECO:0000256|ARBA:ARBA00022734, ECO:0000313|EMBL:KAE8714936.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KAE8714936.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000436088};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..832
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025431712"
FT TRANSMEM 442..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..148
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 284..321
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 341..424
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 524..801
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 832 AA; 93376 MW; ADAC661E70CFFED8 CRC64;
MNTVKWLLRI LLIFLLSHFS FSADTITQHH FIKDNNNEVI VSGGKIFALG FFSPGSSRNR
YVGIWYYQIP GKTVVWVANR DNPVKDTSGI LRIDGRGNLV LFQGNQTLPV WSTNISIAGA
RNSYAQILDS GNLVLIHNDT RKAVLWQSFG YPTNTWLSFM KIGFNLRTGL NQAYTSWKSP
DDPGVGNYSF RMNPGVSPQM VFYKGSVPLW RSGTWTGQRW SGIPQMTNNF IFNDSFVNTD
DEVSFSSDAK NASIITRWVT NETGVVQRII WNNKARRWIF LPIPKEQCDF YGHCGPNGYC
NPYLGDFECT CFPGFEPKSH EAWIVRDRTG GCVRKRDVSM CGNGEGFVKF PHVKVPDTSA
HALVDMSIGL KQCEEKCLRN CSCMAYASAN SETNGGVGCL TWHGDLMDAR AYTETGQDLF
IRVDKNDLAR YTKKGLIQKK GVLAAIIISS AIVFLILVAF LRCLVRRKRR EARTRTNKNI
FSFTTRTSLY FEDSLGEKET DESGRNGDLP FFSLRTIAVA TNNFSSDNKL GQGGFGPVYK
GVLLNGKEIA VKRLSKHSGQ GVQEFKNEIL LIAKLQHRNL VRMLGCCIEG EEKMLIYELL
PNKSLDSIIF DESKSSLLDW KKRFEIICGI ARGMLYLHQD SRLRVIHRDL KAGNVLLDAS
MNPKISDFGM ARIFGGNQTE GDTKRVVGTY GYMSPEYAME GHFSMKSDVY SFGVLLLEII
TGKKISSYFP DSPSLSLVGH VWELWKEDRA TEVVDSTLGD SYSTDEILNC IQIGLLCVQE
HATHRPTMST VVSMLSNEET LPSPEQPGFL EKKSLEVANS VNVVSITMIQ AR
//
