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Database: UniProt
Entry: R0HN03_9BRAS
LinkDB: R0HN03_9BRAS
Original site: R0HN03_9BRAS 
ID   R0HN03_9BRAS            Unreviewed;       783 AA.
AC   R0HN03;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=CARUB_v10022675mg {ECO:0000313|EMBL:EOA26615.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA26615.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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DR   EMBL; KB870808; EOA26615.1; -; Genomic_DNA.
DR   RefSeq; XP_006293717.1; XM_006293655.1.
DR   AlphaFoldDB; R0HN03; -.
DR   STRING; 81985.R0HN03; -.
DR   GeneID; 17890537; -.
DR   KEGG; crb:17890537; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   OrthoDB; 560089at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd13999; STKc_MAP3K-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_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; PTHR23257:SF821; ATP BINDING PROTEIN; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF14381; EDR1; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          527..782
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          36..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         554
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   783 AA;  87864 MW;  183B00A8E7E72871 CRC64;
     MEERRDESSS PTQLGSSTAA TAAACWPSEL AERVKSLSLE SQGEGSSKDS PTSVEQDCSP
     GQRASQHLWD TGMLYEPIPN GFYSVVPDKR VKELYNRLPT PSELHALGEE GVRIEVILVD
     FQKDKKLAML KQLITTLVSG SNPALMIKKI AGTVSDFYKR PTLESPSKLA LEENAFLFEN
     HGAQLLGQIK RGCCRARAIL FKVLADTVGL ESRLVVGLPN DGTVDCMDSN KHMSVIVVLN
     SVELLVDLIR FPGQLVPRSA KAIFMSHISP AGESDSAEND SCDSPLEPNS PLYERRDPES
     TEKDENLQFH RKLEGYPNAF GPSLRNLMLR PAIERKLSNT SHSEPNVATV FWKRSRRKVI
     AEQRTASSSP EHPSMRSRGR SILSAGRNSC RDYAGDASPS SSSTSEIRKS RRRSFRITPE
     IGDDIASAVR EMYEKSKQNR LLHGREDENS SGIDNNVSGL QLDDELNSKK TMSLPSSPHA
     YRCQTFGRRG PSEFAVKDTW NKVVESSTLQ NQPLLPYQEW DIDFAELTVG TRVGIGFFGE
     VFRGIWNGTD VAIKLFLEQD LTAENMEDFC NEISILSRVR HPNVVLFLGA CTKPPRLSMI
     TEYMELGSLY YLIHMSGQKK KLSWHRRLRM LRDICRGLMC IHRMKIVHRD LKSANCLVDK
     HWTVKICDFG LSRIMTDENM KDTSSAGTPE WMAPELICNK PFTEKCDIFS LGVIMWELST
     LRKPWEGVPP EKVVFAVAHE GSRLEIPEGP LSKLIADCWA EPEERPNCEE ILRGLLDCEY
     TLC
//
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