ID A0A1J6KBC0_NICAT Unreviewed; 653 AA.
AC A0A1J6KBC0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cysteine-rich receptor-like protein kinase 2 {ECO:0000313|EMBL:OIT22256.1};
GN Name=CRK2_0 {ECO:0000313|EMBL:OIT22256.1};
GN ORFNames=A4A49_31526 {ECO:0000313|EMBL:OIT22256.1};
OS Nicotiana attenuata (Coyote tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=49451 {ECO:0000313|EMBL:OIT22256.1, ECO:0000313|Proteomes:UP000187609};
RN [1] {ECO:0000313|EMBL:OIT22256.1, ECO:0000313|Proteomes:UP000187609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC TISSUE=Leaves {ECO:0000313|EMBL:OIT22256.1};
RA Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA Timmermann B., Baldwin I.T.;
RT "The genome of Nicotiana attenuata.";
RL Submitted (NOV-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:OIT22256.1}.
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DR EMBL; MJEQ01003795; OIT22256.1; -; Genomic_DNA.
DR RefSeq; XP_019237675.1; XM_019382130.1.
DR RefSeq; XP_019237676.1; XM_019382131.1.
DR AlphaFoldDB; A0A1J6KBC0; -.
DR EnsemblPlants; OIT22256; OIT22256; A4A49_31526.
DR GeneID; 109217847; -.
DR Gramene; OIT22256; OIT22256; A4A49_31526.
DR KEGG; nau:109217847; -.
DR OMA; IYDPNIM; -.
DR OrthoDB; 1039691at2759; -.
DR Proteomes; UP000187609; 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:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47973:SF40; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 2; 1.
DR PANTHER; PTHR47973; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 3; 1.
DR Pfam; PF00069; Pkinase; 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:OIT22256.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:OIT22256.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187609};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..653
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012882288"
FT TRANSMEM 258..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..132
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 137..242
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 324..626
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 604..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 653 AA; 72497 MW; 6551D8E797F3ECDA CRC64;
MERTTPSILC SLFFIALILL LPELSVGEPR SQTVQIICGK QIEQNTTIFV PNFVATMETI
SQQMRTRGYG VAVNGTGPNT NYGLAQCYGD LSLLDCVLCY AEARTVLPQC FPYNGGRIYL
DGCFMRAENY TFYDQYLGPE DRHVCGNRTT KGSLFQQTAR RAVQQAVANA PSNNGYARAE
VPVPGPSNET AYVLADCWKT LSANACTACL QSASASMLGC LPWSEGRALY TGCFMRYSDT
NFLNAISTSG GSSSGGKVVV IVIVVVSSVI VLAVGAVIGI YIWKNKQIQK KRKGAKDAEK
LVKILHDSSL NFKYSTLDKA TGSFDEANKL GQGGFGTVYK GVLQDGREIA VKRLFFNNKH
RAADFYNEVN IISSVEHKNL VRLLGCSCSG PESLLVYEFL PNQSLDRFIF DSNKGKALNW
EKRFEIIIGT AEGLVYLHEN TKNRIIHRDI KASNILLDSR LRAKIADFGL ARSFQEDKSH
ISTVIAGTLG YMAPEYLAHG QLTEKVDVYS FGVLLLEIVT GRQNNRSKNA EYTDSLVSIA
WEHFQRGTTE ELFDPNLMLH NYHTINVKNE VLRVLHVGLL CTQEIATLRP YMSKALQMLV
KKEEELPPPT NPPFIDEKTM ELHDPREKYS NDPLREGDSA SVATLSNSGF YPR
//
