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Database: UniProt
Entry: A0A022PYD8_ERYGU
LinkDB: A0A022PYD8_ERYGU
Original site: A0A022PYD8_ERYGU 
ID   A0A022PYD8_ERYGU        Unreviewed;      1359 AA.
AC   A0A022PYD8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=MIMGU_mgv1a000252mg {ECO:0000313|EMBL:EYU20831.1};
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:EYU20831.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU20831.1, 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; KI632259; EYU20831.1; -; Genomic_DNA.
DR   STRING; 4155.A0A022PYD8; -.
DR   eggNOG; KOG1187; Eukaryota.
DR   eggNOG; KOG4658; 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; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045272; ANXUR1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032675; LRR_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; PTHR27003; OS07G0166700 PROTEIN; 1.
DR   PANTHER; PTHR27003:SF467; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
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|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1359
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001506820"
FT   DOMAIN          520..798
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          454..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         549
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1359 AA;  153939 MW;  906112EDB3452DB6 CRC64;
     MANLYPVLIA LSFSCFLIKS AAVRSNATRG ISVNCGSTGT SAARSGRVWI GDVWPEYPYL
     LQVKGASTIS AVVGNSISAD PIPYKRARIS RSQFVYAFLV MPGQNIIRLH FNPSKYRGFQ
     GLKDLFTVEA GPFTLLSNFS PSLTADALGV GFFAKEFLLN IPEYERLNII FSPGISESLD
     TYAFVNGIEI FSVPPPSSVS YFQDGDYSTA LEILEVEQIS VPYAGDSGYA HPFPFSISQN
     AKYNTWKIPV DVGFKYLVRV HFLEKGLKFA LAGVGNGIPP YRDYTVVVRG NTDKGKRDIL
     IPLQSYDELI DVMFKDIANE IVADFNVQLV RGSDGNNIPS YSDSMVMMKE KGEHIFIRLQ
     SYDSLIDAPA LVSGVEIFKA INSYNSAWSP SGESFFLASI RTTSTIFILV FTIYFLRVIF
     VLKSWKTWKA IITEKKINFF EKMKRWKSSS RIGRLQETSE TDSSEEINDS EASSNFQQQL
     QETWEAIISY KEKKPKSSSG AERLCRRFSL DEIRLATNNF SDALLIGRGG YGNVYKGHID
     EEQCTVAVKR LKKSSSKQGE SEFWTEIETL FELRHVNIVS LIGYCNEHGE RILVYEYIPC
     GTLADHLYRL ARKSNSCSTL TWKQRLDICI GAGRGLDYLH MGCGVIHRDV KASNILLDEN
     FVAKVSDFGL SRLENRSKSQ SYVSTLVKGT VGYFDPSYFL TGQLTRKSDT YGFGVVLLEV
     LCGRPAIDTM AAEDEKILSR WAQDKINKGE VEEIISESLR EEISPNSLKT FLKVVERCLH
     DEPKKRPTMS EVVSQLELAV EQQEAKQVSA LNQIARVSND NHHPDEYVVD PDEYVVDDPL
     FIRTKEDEEQ NKIYSHEGNL KECVLFCSVF PSGYEFTKDM LVWQWVAKSL INLSEDEIEE
     VYIQCFDKLL NLDFIVPSGY CHFADEVKYK VGHNMTMFLQ NQLLEPKFQN NLEGKQRRMV
     KVENLSLAFK EIDHINFRIL KQCTRLQTLI IHRCYGSKEL PSSVENLEEV RYLDMSETPI
     KWLPESILCL GHLQTLKLDG CLSLVGLPKC TSNLINLRHL VLDIVRQLQS MPTGIGKLSK
     LRTLGAFLVG EEDGTRIGEL KNMNSLRGSL RLLNLENVPT KEEAAEAYLC KKHGLKKIEL
     QWSDLQDEKN PNEEEILNSI QPPFSIQELK ILFYSGGVFP SWISNPSFSE LVNITLYRCR
     YCDTLPSIGE LPSLKLLNII ENNEVKEINS FFCRKESNEH HVAFPKLEKL SFDSMSELEQ
     WTGLKEGDFP CLSYLIIQYC PELIGISFLS HLSSLSHLEI SYCPKITCLP EGGLPLTLES
     LMIKDCPELK ERCCNKQCED WSKVARVPAF YIDNEKVSV
//
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