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Database: UniProt
Entry: R0HI14_9BRAS
LinkDB: R0HI14_9BRAS
Original site: R0HI14_9BRAS 
ID   R0HI14_9BRAS            Unreviewed;       939 AA.
AC   R0HI14;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=CARUB_v10016642mg {ECO:0000313|EMBL:EOA23453.1};
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:EOA23453.1, 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; KB870809; EOA23453.1; -; Genomic_DNA.
DR   RefSeq; XP_006290555.1; XM_006290493.1.
DR   AlphaFoldDB; R0HI14; -.
DR   Proteomes; UP000029121; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR48055; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR   PANTHER; PTHR48055:SF57; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 3.
DR   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF13855; LRR_8; 4.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS51450; LRR; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527};
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..939
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004352069"
FT   DOMAIN          653..926
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         682
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   939 AA;  101492 MW;  9A50FC7B2AEE7810 CRC64;
     MFKALIFSVW LLSVVLVAPV RSLDPPLNDD VLGLIVFKAD LRDPQQKLAS WNEDDYTPCS
     WTGVKCHPRT NRVTELNLDG FSLSGRIGRG LLQLEFLHKL SLSNNNLTGI INPNLLLSLV
     NLKVVDLSSN ALSGSLSDGF FRQCGSLRVL SLAKNKLTGK IPVSISSCSS LAALNLSSNR
     FSGSMPSGIW SLNTLRSLDL SWNELEGEFP EKIDRLNNLR SLDLSRNRLS GPIPSEIGSC
     MLLKTIDLSD NSLSGTLPDT FQQLSLCYSL NLGKNALEGE VPKWIGEMRS LETLDLSMNK
     FSGQVPESIG NLLALKVLNF SGNGLIGSLP DSTANCINLL ALDFSGNSLT GKLPMWIFQD
     GSRDVSALQN DNSTGGIKKI QVLDLSHNSF SGEIGAGLGD LRDLEGLHLS RNSLTGPIPS
     AIGDLKHLGV LDLSHNQLNG TIPRETGGAV SLEELRLDNN LLEGNIPSSI KTCSSLRSLI
     LSHNKLVGTI PPELAKLTKL EEVDISFNEL TGTLPKQLAN LGYLHTFNMS HNHLFGELPA
     GGIFNGLSPS SVSGNTGICG AVVNNSCPAV SPKPIVLNPN ATFDSYSAIV VGVIAITVLN
     LRVRASTVSR SAVPLTFSGG DDFSRSPTTD SNSGKLVMFS GEPDFSTGTH ALLNKDCELG
     RGGFGAVYRT VIRDGYPVAI KKLTVSSLVK SQEEFEREVK KLGKLRHSNL VKLEGYYWTT
     SLQLLIYEFL SGGSLYKHLH EAPGGSSLLS WNDRFNVILG TAKCLAYLHQ SNIIHYNIKS
     SNVLLDSSGE PKVGDYGLAR LLPMLDRYVL SSKIQSALGY MAPEFACRTV KITEKCDVYG
     FGVLVLEVVT GKKPVEYMED DVVVLCDMVR EALEDGRADE CIDPRLQGKF PVEEAIAVIK
     LGLICTSQVP SSRPHMGEAV NILRMIRCPS GSSDELGSS
//
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