ID A0A022R6W4_ERYGU Unreviewed; 1139 AA.
AC A0A022R6W4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=MIMGU_mgv1a017969mg {ECO:0000313|EMBL:EYU34605.1};
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:EYU34605.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU34605.1, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; KI630674; EYU34605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022R6W4; -.
DR STRING; 4155.A0A022R6W4; -.
DR eggNOG; ENOG502QSHG; Eukaryota.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 6.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48056:SF81; LEUCINE-RICH REPEAT CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00560; LRR_1; 8.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
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:UP000030748};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..42
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 43..1139
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001504897"
FT TRANSMEM 796..818
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 860..1134
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 766..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 888
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1139 AA; 123333 MW; 60F8B6DA1FDE46F4 CRC64;
MGPSSSSSSL LQWRHHHIHK PPLKLLIFLC VLLSAPIGPV WGSDSDKSAL LAFKALLSDP
LGALSSWDSK SPDHCSWVGV SCGSGSRVVA LNITGGGNSL SCARIAQFPL YGFGIRRTCS
LAGGSKVKIL GRISAAVSEL TELKILSMPF NELSGGIPAE IWGMEKLEVL DLEGNSISGS
LPYSFTGLRS LKVLNLGFNE LFGAIPSSLS NCVGLRILNL AGNRFNGSIP GFVGGFQDLN
GLYLSFNLLS GSIPVSIGNN CEKLEHLEIS GNYLTEAIPR SIGNCRALKT LLLYSNMLEE
VIPSELGRLS QLEVLDVSRN NFGGVIPSAI GNCTKLSVLV LSNLWDPLPN ASSLGEKLAF
TADEYNFYEG TIPNEISTLS SLRMVWAPRA TLEGKFPDSW GTCGNLEMLN LAQNYYSGEI
SVGFSNKCKK LRFLDLSSNR LSGAISDEIP VPCMNLFDIS DNFLSGPIPK FSYGSCVPIE
SRNPYDAPSA YISYFRYRTQ IESSLPLSEN GGDDDGNFLV LHNFGSNNLT GPLQAMPIAS
EILGKQTVYA FLAGRNKLTG NFPPSFAEKC DQAKGVVVNV SNNLLTGQVP IDFATSCKSL
MLLDASVNQI SGTLPPSIGN LVSLRVLNLS WNPLQGPIPN SLGLIKDIEC LSLAGNNLNG
SIPESFGQLY NLEVLDLSSN SLSGEIPKGL ASLRKLSVLL LNNNKLSGQL PSELATNAST
LSTFNVSFNN LSGNLPPNND MLKCSSFLGN PFLQCPILSL SSNPVDQNGR IGNQDSSSSS
SSTDRRREEK LNSIEIASIT SAAAIVFVLL ALIFLFFYTR KWKPRSRVTN GASSRREVIT
FTDIGVPLTF DTVVRATSNF NASNCIGNGG FGATFKAEIS PGVLVAIKRL AVGRFQGVQQ
FDAEIRTLGR LRHPNLVTLI GYHASETEMF LIYNYLPSGN LEKFIHERSN RAVDWRVLHR
IALDIARALA YLHEQCVPRV LHRDVKPSNI LLDEEYNAYL SDFGLARLLG TSETHATTGV
AGTFGYVAPE YAMTCRVSDK ADVYSYGVVL LELISDKKAL DPSFSSYGNG FNIVAWGCML
LRAGRAKEFF TAGLWEAGPH DDLVEVLHLA VVCTVESLSH RPTMKQVVRR LKQLQPPSC
//
