ID A0A2P5EIG0_TREOI Unreviewed; 648 AA.
AC A0A2P5EIG0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cysteine rich receptor like kinase {ECO:0000313|EMBL:PON85326.1};
GN Name=TorCRK21 {ECO:0000313|EMBL:PON85326.1};
GN ORFNames=TorRG33x02_188530 {ECO:0000313|EMBL:PON85326.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON85326.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:PON85326.1}.
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DR EMBL; JXTC01000149; PON85326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5EIG0; -.
DR STRING; 63057.A0A2P5EIG0; -.
DR InParanoid; A0A2P5EIG0; -.
DR OrthoDB; 1126834at2759; -.
DR Proteomes; UP000237000; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PTHR27002:SF123; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 10 ISOFORM X1; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51473; GNK2; 2.
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, ECO:0000313|EMBL:PON85326.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:PON85326.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 253..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..117
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 125..232
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 333..620
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 626..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 648 AA; 72714 MW; 86A67575DFCABAFE CRC64;
MISVSVFTKA DPLYTDCSSG RNYTPNGQFQ NNLKLLLNDL SSNTTRNDTS LGGFYNTSVG
DNPNTVYGQS LCRGDVNSSV CRNCIRKASL TLLENCTSQD AMIWFELCQV RYSFQILVPI
QIYTGMFPVS NKRQKLVQNP VLFNRVLMYL MIEISKEAAF NASKLKFATG QIRFSDKETI
YGLLQCTWDI PEGDCQSCFE FSFSELTECC SFRQGGIVVS RSCNVRFELD QFYNDSSTSL
LTYTFPKGTK WKIWEVVMVT SAAILLVAII AGSCNVYYRQ KKRTQRDDRS ENALLQELAS
PTAVSITQEG NLVTSEELPF FDLPTIRAAT DNFADSNQLG QGGFGTVYMG VLPDGKEVAV
KRLSKKSWQG VEEFKNEVKL IAKLQHRNLV RLVGCGIEGE EKLLIYEFMP NRSLDFFIFD
SERRSQLDWQ TYYNVIGGIA RGLLYLHEDS RLKIIHRDLK PSNVLLDHEM VAKISDFGMA
RIFCENQNTN NTKRVVGTYG YMAPEYAMEG IFSIKSDVFS FGVILLEIIS GKKNSGFYLT
KHAQTLLAYA WRLWKNGKEV EFVDPLLIES GSVEEVLRCM HIGLLCVQED PEDRPTMSAV
VVLLQGSESA PLPEPGQPAI AVGRVVANDE TTTDPSVNGL TTSTISPR
//
