ID A0A5J5AJJ0_9ASTE Unreviewed; 1018 AA.
AC A0A5J5AJJ0;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=F0562_005163 {ECO:0000313|EMBL:KAA8530454.1};
OS Nyssa sinensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Cornales; Nyssaceae; Nyssa.
OX NCBI_TaxID=561372 {ECO:0000313|EMBL:KAA8530454.1, ECO:0000313|Proteomes:UP000325577};
RN [1] {ECO:0000313|EMBL:KAA8530454.1, ECO:0000313|Proteomes:UP000325577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J267 {ECO:0000313|EMBL:KAA8530454.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAA8530454.1};
RA Yang X., Kang M., Yang Y., Xiong H., Wang M., Zhang Z., Wang Z., Wu H.,
RA Ma T., Liu J., Xi Z.;
RT "A chromosome-level genome assembly of the Chinese tupelo Nyssa sinensis.";
RL Submitted (SEP-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}.
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DR EMBL; CM018043; KAA8530454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5AJJ0; -.
DR OrthoDB; 1720310at2759; -.
DR Proteomes; UP000325577; Linkage Group LG2.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0010038; P:response to metal ion; IEA:UniProtKB-ARBA.
DR CDD; cd14066; STKc_IRAK; 1.
DR FunFam; 2.60.120.430:FF:000003; FERONIA receptor-like kinase; 1.
DR FunFam; 2.60.120.430:FF:000007; FERONIA receptor-like kinase; 1.
DR FunFam; 1.10.510.10:FF:000252; Receptor-like protein kinase FERONIA; 1.
DR FunFam; 3.30.200.20:FF:000645; Receptor-like protein kinase FERONIA; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 2.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045272; ANXUR1/2-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_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; PTHR34590; OS03G0124300 PROTEIN-RELATED; 1.
DR PANTHER; PTHR34590:SF15; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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:UP000325577};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1018
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023933851"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 668..944
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 217..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 697
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1018 AA; 113039 MW; D37F80F62E5760BD CRC64;
MGMVGKKTFF LAFLVMTVSA TATSLSRAAV SSQRTELKSW CKGAIDECLE EEVEYLMDSD
INARLLQQGG KDPFTNFTTS KSKTIGAYCD RGKYASCIPD ENKKVRRAYY ICSFRKDFSP
LYSSCFLYVK TRSSRQLFTS LPPLSPAMKS TVNTNILVIL APLYLCFLLT SLLIIIPIPC
NSQPLYTPRE NIALACGFSG NTTTLDHREW VGDIDSKQST LEQQPNTSTT SSPQRPAVTT
SCPYVNARLS RFDFTYVFQV TPGQKFIRLH FYHSIYQSTD FDPSKALFSV KANGFTLLRN
FSASLAAASI GSDIIVKEYS INVEEDQSLI NVTFSPSSTP SDAYAFVNGI EIVSMPTNLY
YSPSSDSGFT FIGQPQSPFR LENKTSLEKV YRFNVGGQFI SPELDTGMFR SWSPDDDYCS
EVGALPVNTK IRLSFTKIPN YTAPADVYKT ARSMGNNKTV NEGYNLTWNF PVDPGFTYMI
RLHFCEFQIQ VTKPSDREFS IFIANQTAEP SADVIRWSGG NGVPIFRDYA VMVNQGREKK
QNLSVALHPN SESRTRRSDA ILNGIEVFKL SDAAGNLAGL NPDPVVTPPP SSPQPAKSKG
KRNTTLVAAV VGGVLSGVVA LSVLGFLIFL RRVKDTGGGS KVTNSAYLPS DICRHFSLAE
IKTATNNFDR IFIIGRGGFG DVYKGYIDGG AIQVAIKRLN PDSQQGAHEF KTEIEMLSQL
RYLHLVSLIG YCNEAKEMIL VYDYMSHGTL RDHLYDTENT PLSWKQRLQI LIGAARGLHY
LHAGAKQRII HRDVKTTNIL LDEKWVAKVS DFGLSKINPT DMSNAHVTTL VKGSVGYLDP
EYYRRQQLTE KSDVYSFGVV LFEVLCARHP LDKTVLDKDE VNLPRWARQC YKKGTLDQII
DPYLKGKIVP ESLKKFGEIA VNCVDDEGIK RPSMNEVLWS LEFALELQES AEEGIEFDIE
VKEKDFDRQD KKVDESSGQV SSSGLTMTDN GGTSFTISGS ESLSSGAVFS EIKCPGAP
//
