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Database: UniProt
Entry: A0A059CZH6_EUCGR
LinkDB: A0A059CZH6_EUCGR
Original site: A0A059CZH6_EUCGR 
ID   A0A059CZH6_EUCGR        Unreviewed;       640 AA.
AC   A0A059CZH6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Cysteine-rich receptor-like protein kinase 42 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EUGRSUZ_B00290 {ECO:0000313|EMBL:KCW83355.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW83355.1};
RN   [1] {ECO:0000313|EMBL:KCW83355.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW83355.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   EMBL; KK198754; KCW83355.1; -; Genomic_DNA.
DR   RefSeq; XP_010027537.1; XM_010029235.2.
DR   AlphaFoldDB; A0A059CZH6; -.
DR   EnsemblPlants; KCW83355; KCW83355; EUGRSUZ_B00290.
DR   GeneID; 104418023; -.
DR   Gramene; KCW83355; KCW83355; EUGRSUZ_B00290.
DR   KEGG; egr:104418023; -.
DR   eggNOG; ENOG502QRU4; Eukaryota.
DR   InParanoid; A0A059CZH6; -.
DR   OMA; TQCANIF; -.
DR   OrthoDB; 1039691at2759; -.
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; IBA:GO_Central.
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; PTHR47973:SF12; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 1; 1.
DR   PANTHER; PTHR47973; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 3; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Repeat {ECO:0000256|ARBA:ARBA00022737};
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|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..640
FT                   /note="Cysteine-rich receptor-like protein kinase 42"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001574925"
FT   TRANSMEM        255..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..127
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          135..243
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          319..603
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          599..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         347
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   640 AA;  70207 MW;  C3E12D95C978D70A CRC64;
     MRPSILNLTC VFLVLFSSSF LPSLGDPRIS EAGILCLKSN VTSVSNFLDV MQKVLAKVAE
     DRWANDSITS PLPEIYALAQ CHGDLSRDDC ILCFAHSRTL LSRCTILDTK GRLYLDGCFI
     RSDYYNFLNE TVDPQHDLVK CANQSSVSAD QQARQQFVDK VDRVLTNVSA VAPGNKGFAV
     FGEARRGGVA GVYALAQCWN TLDEKGCREC LANAMIRARN CTPGDEGRAM NAGCFMRYST
     QRFYTVPTDG DSLKLGIIIA IALSVAAATS LLIVSAYVGY RKLSKKREVQ KKLFGVPAIV
     RKSNLNFNYE SLEKATDFFD ESRKLGQGGS GSVYEGILPD GRVVAVKRLV FNTRQWVDDF
     FNEVNLISGI QHKNLVRLLG CSIEGPESLL VYEYVPNRSL DQILFVKNAT HVLSWQERVN
     IISGTAEGLA FLHGPCGVKI IHRDIKSSNV LLDEDLTAKI ADFGLARCLD PEKSHLSTGI
     AGTLGYMAPE YLVKGQLTEK ADVYAFGVLV LEILSGRKNS IFGQASGSVL QSVWKRYKSN
     RLAECIDPAL KGKFPISEAL NVIQIALLCT QASPDLRPSM SEVVEMLNDQ ECIVPMPMQP
     PFLNNNPIPD DSSRSSNTNT GITNQLTNSE ISSGSTISLQ
//
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