ID A0A022RZ14_ERYGU Unreviewed; 1128 AA.
AC A0A022RZ14;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=MIMGU_mgv1a000477mg {ECO:0000313|EMBL:EYU44215.1};
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:EYU44215.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU44215.1, 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI630214; EYU44215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022RZ14; -.
DR STRING; 4155.A0A022RZ14; -.
DR eggNOG; KOG1187; 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:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 3.
DR InterPro; IPR045272; ANXUR1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
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; PTHR27003; OS07G0166700 PROTEIN; 1.
DR PANTHER; PTHR27003:SF460; RECEPTOR-LIKE PROTEIN KINASE FERONIA; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW 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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {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..1128
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001505413"
FT TRANSMEM 430..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 491..770
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 864..1128
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 775..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1128 AA; 127433 MW; 1199BB0D29E153A8 CRC64;
MYISESSKNF LIFSLFLHIL IIPATYSLDS IAISCGSSGN STALDGRIWI GDSTPKSTFS
PQINGKTSES RTTDKLASLD SVPYKTARAS RHEFTYVFQV NPGQKFIRLH FYRDSSYKGF
ESSKALFTVK AGPYTLLSNF STSLISDVSG EKQILKEYCV NVDESRALTL TFSPAQKERK
SDDFYAFVNA IEVVSMPTGL YFTPEGELGA LVVGQKYRFY IDNTTAFELV RRLNVGGTTI
SPAEDSRMFR RWDEDSTYLM EAGSFPVETL TTVGYRGTST HVAPIKVYDT ARTMQTVTTN
NLTWRIPVDL GFRYLTRLHF SELHPRIAQQ FSIFINNQIA ENDANIIQRG GESGVAVYRD
YIVMMDGDKT EGKRHLSITF QAKIESTYRQ FNGLEVFKLS NPDNNLAGMG PVLELQSSTS
TPQQKKPKSI YSSNMIAALL TVILALLNIA VYHLRIISET NSGTRNIRSS TMEPRCRRFP
IDEIRLATNY FDLRFHIGSG GYGRVYKGSI DGGATVVAIK RLKSESRQGD TEFWTEIKML
SKIRHKHLVS LIGYCNDGQE RVLVYHYMAQ GTLSDHIYKT YRHGKSNPPL SWELRLKASI
GAARGLYYLH SRHRVIHRDV KSSNILLDEN WVAKISDFGL SKMGPTNDSF THISTNVKGT
FGYLDPEYFL TRKLTRKSDV YAFGVVLFEV LSGRPAVEIR LEEEKHSLAG WARYCIREGR
VDQLIDQNLT GQILPACLKV FVGIAGRCLH TQPQGRPAMA DVVMGLELAL ALQQSTDPME
EEENIGRTDS DRNNPSSSTR IRGRDQKNPK LKTKDSSSAT NSTHKWWWDP FGILPRTPSK
PKASPQAVIH HFSIQEIQTA TNDFHNSLVI GFGGADNVYK GCINGGQKLV AIRQSRTRES
RLCMSRELQS QKETQTKSSP SQKHVVSLIG YCETESDMVL VYEYMPNGTL YDHLHEPLKS
PLPWKRRLQI CIGAARGLIY IHSTIKQTVL HRDFKSTNIW LDENFVPKVS EWDYIRGEES
TEKSYVYSFG LVLFELLFDN KESDRWLDED QVSLAQWIKS CMRNNLSGCI DPFLVGRVSP
DSLRIFVETA GRCLLDHGNR RPSMNDIVTQ LEAALEQQEV TEGKVLNS
//