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Database: UniProt
Entry: A0A022RZ14_ERYGU
LinkDB: A0A022RZ14_ERYGU
Original site: A0A022RZ14_ERYGU 
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).
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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
//
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