ID A0A022Q3I2_ERYGU Unreviewed; 483 AA.
AC A0A022Q3I2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
DE Flags: Fragment;
GN ORFNames=MIMGU_mgv1a025779mg {ECO:0000313|EMBL:EYU21055.1};
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:EYU21055.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU21055.1, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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DR EMBL; KI632232; EYU21055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022Q3I2; -.
DR STRING; 4155.A0A022Q3I2; -.
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:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR045874; LRK10-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27009:SF276; RUST RESISTANCE KINASE LR10-LIKE; 1.
DR PANTHER; PTHR27009; RUST RESISTANCE KINASE LR10-RELATED; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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 3: Inferred from homology;
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|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 218..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 276..483
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 483
FT /evidence="ECO:0000313|EMBL:EYU21055.1"
SQ SEQUENCE 483 AA; 54916 MW; DAB7D513D7E533E9 CRC64;
MGGISKLRAG LSPSSQRIRC SKHSPIIRFP FRHQTQQPQH CGYPGFDLNC DHKNNTVLVL
PFSVNVVVKE INYASQTILV YDPENCLPQK LPHLNLSTSS FHFLLDDFDN YKSDSAIFKC
SDDADTSLYR FIPCLIDPIN KYYIVDNDNI YLYTLASCTK IHDISAVIPW SISDKKGFRL
EWSEPTCGHC EAQGKRCSLF NSTRLDSIHC IDKQPTTIHH GFGCFLAVII LVALVYQYIR
FRTGRENQIK IEKFLQDYRA LKPSRFSYSD ITRITHQFRN KLGEGCYGVV YKGKLNNEID
VAVKVLNNSK GNGEEFVNEV STIGRIHHVN IVRLVGFCAD GFRRALVYEF LPNDSLEKII
FQAGSMKISL DWEKLKDIAQ GIARGIEYLH EGCDQQILHF DIKPQNVLLD HNFNPKICDF
GLAKLCSKEQ SAVTMTAARG TMGYIAPEVL SRTFGRVSYK SDVYSFGMLL LEMVGGRKNE
DRN
//