ID A0A9J6AEN0_SOLCO Unreviewed; 839 AA.
AC A0A9J6AEN0;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
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=H5410_007958 {ECO:0000313|EMBL:KAG5622740.1};
OS Solanum commersonii (Commerson's wild potato) (Commerson's nightshade).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4109 {ECO:0000313|EMBL:KAG5622740.1, ECO:0000313|Proteomes:UP000824120};
RN [1] {ECO:0000313|EMBL:KAG5622740.1, ECO:0000313|Proteomes:UP000824120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZ3.2 {ECO:0000313|EMBL:KAG5622740.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG5622740.1};
RA Cho K.;
RT "De no assembly of potato wild relative species, Solanum commersonii.";
RL Submitted (SEP-2020) 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: 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:KAG5622740.1}.
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DR EMBL; JACXVP010000002; KAG5622740.1; -; Genomic_DNA.
DR OrthoDB; 1934880at2759; -.
DR Proteomes; UP000824120; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP 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; 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; 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; IPR021820; S-locus_recpt_kinase_C.
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:SF1082; OS06G0693000 PROTEIN; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF11883; DUF3403; 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; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 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 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:UP000824120};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..839
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039899393"
FT TRANSMEM 447..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..148
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 351..424
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 522..810
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 800..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 95328 MW; 1392BCB96774E66D CRC64;
MKLSLSCKKI LLWCAFLVLF FHITNASSDS ISINEFLQDS ETLVSNNKTF KLGFFSPENS
ANRYVGVMFN MKSQSVIWVA NRDQPLQDSS GRVTISEDGN LVILNGQGKS VWSSNISPAV
RNSTAQLLDT GNLVLKDNSS ERVLWESFSD LSDSYLQHMK LGTDKSTNTT NLLKSWRSPV
DPSDGSFSAG IQTETIPQIF IWKNGLPHWR SGPWDKQVFI GVPNMTSFYF SGFELVNDNM
GTTYFYYSYA YLGDDIMYLV LNSTGFLQQK DLYGRKNEWE VTWVTPSNEC DFYRKCGPFG
SCDSESSPIC SCLQGFKPKN QEEWVKGNWT NGCIRKTVLE KKRNNSNVEQ GKQDWFLKLQ
SMKVPDSAIW VPSAKEDCES DCLRNFSCIA YSYYTGIGCM HWEGSLIDSQ KFSKGGADLF
IRLAYAEQGS ISLHLEQKKS NKVAIRIIVP IICSIVIAIL GYISCKLLAK HRGRKRKREL
LSKKLFPSYY KLSLARDDIY RVKFEDLTIY NFDMLANATD NFHLSSKLGQ GGFGPVYKGK
LPKGQEIAVK RLSQSSGQGQ EEFMNEVVVI SKLQHRNLVR LLGCCIERGE KMLVYEYMPK
RSLDAYLFGA HSEEEYFLDW SKRVIIIEGI GRGLLYLHRD SRLRIIHRDL KASNILLDEY
LNPKISDFGM ARIIAGNQDQ ANTIRVVGTY GYMAPEYAMS GRFSEKSDVY SFGVLLLEII
SGRRNTSFYQ DDVALSLLAW AWKLWNENKI VELVDPKIIE LQLKKEIHRC VHVGLLCVQE
YAEDRPNVST VLSMLSREID DLPSPKQPAF TTRPTPSKKG SSRIQVSVND VSITIMEAR
//
