ID A0A022QIF2_ERYGU Unreviewed; 651 AA.
AC A0A022QIF2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=MIMGU_mgv1a002644mg {ECO:0000313|EMBL:EYU28432.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU28432.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU28432.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; KI631414; EYU28432.1; -; Genomic_DNA.
DR RefSeq; XP_012848059.1; XM_012992605.1.
DR AlphaFoldDB; A0A022QIF2; -.
DR STRING; 4155.A0A022QIF2; -.
DR GeneID; 105968017; -.
DR KEGG; egt:105968017; -.
DR eggNOG; ENOG502QRU4; Eukaryota.
DR OMA; MRSENYT; -.
DR OrthoDB; 1039691at2759; -.
DR PhylomeDB; A0A022QIF2; -.
DR Proteomes; UP000030748; 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; 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:SF2; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW 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..651
FT /note="Cysteine-rich receptor-like protein kinase 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001507271"
FT TRANSMEM 255..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..131
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 136..241
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 321..614
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 603..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 651 AA; 71918 MW; E7299D0AF87C8D33 CRC64;
MKIIMINTAL LMAVILMVLP DPTWSDPRSK TVKLICGEQS EHNATLYVPN FVATMENISA
QIRNSGFGLS VTGPGNIDTN YGLAQCYGDL SPLDCVLCYA EARTVLPQCF PANGGRIFLD
GCFMRAENYS FFHEYSGPND VAVCGNETRT GPAFRESVRR ALNDAVLTAP EKNGYGRAEV
AVSGDGNGSA YVLADCWRTL NASACRSCLK KASSSVMKCL PLSNGRALNA GCFLRYSNTN
FLNPIPQNRN SKERIIVIVM ACVSAAAVLI IGAVIGVYTW KQRIIQRKRK GSDDTKKYAK
TLNDSSLNFK YSTLEKATAS FDEANKLGRG GFGTVYKGVL PDGREIAVKR LFFNNKHRAS
DFYNEVKIIS SVEHKNLVRL LGCSCSGPES LLVYEFLPNT SLDRFIFDSS KGKGLNWEKR
FEIIIGTAEG LVYLHENGNA RIIHRDIKAS NILLDSRLRA KIADFGLARS FQEDKSHIST
AIAGTLGYMA PEYLAHGQLT EKADVYSFGV LLLEIVTGRQ NNRSNTSVYA ESLVTITWKR
FQQRTVEEIF DSNLVTSHNY NYNIETRNDI LRVVHVGLLC TQEIASLRPS MSKALEMLVK
KDEDLPAPTS PPFVDDNTME LNGTNEHPSP PLDYGNSDSA ASMSQSIFFP R
//
