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Database: UniProt
Entry: A0A022R0W1_ERYGU
LinkDB: A0A022R0W1_ERYGU
Original site: A0A022R0W1_ERYGU 
ID   A0A022R0W1_ERYGU        Unreviewed;       952 AA.
AC   A0A022R0W1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=MIMGU_mgv1a025286mg {ECO:0000313|EMBL:EYU33238.1};
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:EYU33238.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU33238.1, 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; KI630784; EYU33238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022R0W1; -.
DR   STRING; 4155.A0A022R0W1; -.
DR   eggNOG; ENOG502QQH6; Eukaryota.
DR   OMA; KCKCAYP; -.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45974:SF266; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE HPCA1; 1.
DR   PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR   Pfam; PF00560; LRR_1; 3.
DR   Pfam; PF00069; Pkinase; 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   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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..952
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001504672"
FT   TRANSMEM        556..579
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          628..901
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          906..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..920
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         656
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   952 AA;  103944 MW;  D902B24023607565 CRC64;
     MIWRVLLSLL VAFIQVLAIA ALTNTNDFTS LKALKDTWGN YPPNWIGSDP CGDVWDGITC
     KNDRVVSITL ASIDLSGQLS SDIAGLTELQ TLDLSYNKRM TGPLPPQIGN VNKLSSLILV
     GCGFFGPIPG SIGSLQQLRY LSLNSNNFIG SIPPSIGNLT NLYWLDLADN KLTGTIPVSD
     GTSPGLDMLV NTKHFHFGKN QLSGVIPPQL FHSNLTLIHL LLENNQLTGR IPSTIGLVDK
     LEVVRLDRNL LSGPVPPNLN NLVSVQELYL SNNALTGSLP NLTGMNLLNY VDMSNNSFDA
     TDIPPWFSSL MSLTSLIMEN TGIQGPIPVS LFSLFQLQTV TLKNNRINGT LNIGSTYSNQ
     LQIIDLQNNF IEAFTQRAGF SVQIILVGNP ICNEGGTESY CSLPQPSSNS YSTPPQNCVP
     STCSSETVSS PTCKCAYPYS GTLVFRAPSF SNFRNATIFA SLESKLMVTF RSNSLPVDSV
     SLSNPTRNTD NYLSLDLQVF PSGLDFFNRT AITGIGFTLS NQTFKPPPEF GPFVFEGRSY
     PHFQVMGSNK SSNTGVIIGA AVGGTVLFLL LVLAGVYAIR QRRRADTADR MNDPFALWDT
     NTTSGSVPQL KGVKAFKFEE LKRITNNFSE TNGIGSGGYG RVYRGTLANG QLVAIKRAVQ
     GSMQGGLEFK TEIELLSRVH HKNVVSLVGF CFDHGEQMLV YEFIANGTLS DSISGKTGIR
     LDWMRRLRIA HGAAKGLQYL HDEADPPIIH RDIKSNNILL DERLTAKVAD FGLSKLMGDS
     ERGHVTTQVK GTMGYLDPEY YMTQQLTEKS DVYSFGILLL ELLTARLPIE NGKHIVREVR
     SVMDTSKNMY NLQGILDPAV ASGMSAKSVE MFVDLALRCV QELGSNRPSM SEVVKEIENT
     MEIAGINPNA ESAPTSSTYE DANKDGKHPY SNENMFAYSG AYPADSKGFE PK
//
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