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
//