ID R0IGT2_9BRAS Unreviewed; 870 AA.
AC R0IGT2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CARUB_v10011886mg {ECO:0000313|EMBL:EOA37565.1};
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:EOA37565.1, 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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB870805; EOA37565.1; -; Genomic_DNA.
DR RefSeq; XP_006304667.1; XM_006304605.1.
DR AlphaFoldDB; R0IGT2; -.
DR GeneID; 17898607; -.
DR KEGG; crb:17898607; -.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR OrthoDB; 658246at2759; -.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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; IPR024788; Malectin-like_Carb-bd_dom.
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; PTHR45631:SF151; MALECTIN-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45631; OS07G0107800 PROTEIN-RELATED; 1.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF12819; Malectin_like; 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 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: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: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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..870
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004343104"
FT TRANSMEM 508..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 564..833
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 849..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 591
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 870 AA; 97763 MW; 4B1842A7DF9A461C CRC64;
METRNKLLLL ACATFSIISF VKSQNQQGFI SLDCGLPSNE SPYNEPLTNL TYISDVNFIR
GGKTGNIKIS AETDLVGKPF KVLRYFPDGT RNCYSLSVKQ GTKYLIRTMF LYGNYDGLNT
SPRFDLYLGP NIWKSVDVLI SGIGDGVVEE IIHITKSDIL EICLVKTGTS TPMISAIELR
PLRYDTYTTR TGSLMNIAHL YFLNSDKIIR YPKDVYDRVW TPYLQQEWTH INTTLNVSGS
PDGYDAPRDV ITTAAIPTNV SEPFSFTWNL EASDDETYIY LYFAEIQRLQ PNETREFEIA
ANGKVYISYS PMNFEEDTLF NPAPLKCEGG VCLLKLSKTP KSNLPPLLNA IELFSVIQFP
QSETNRDDVN AIKNIQSTYQ LSRISWQGDP CVPKQFSWNG LSCNVIDIST PPRIIALDLS
SSGLTGVIPP SIQNLSLLRE LDLSNNNLTG EVPEFLAKMK SLLVINFRGN NLRGFVPQAL
LEREKDGLKL YVDENNKPRG SSEPRSRLVA IVAASISSAA VVIIVLVLIF IFRRRRSSTR
KVMRPSLEMK NRRFTYSEVK EMTSNFKVVL GKGGFGIVYH GFLNNEQVAV KVLSQSSTQG
YKEFKTEVEL LLRVHHVNLV SLVGYCDEGN DLALIYEFME YGNLREHLSG KRGGSVLNWS
GRLKITIESA LGIEYLHIGC KPPMVHRDVK STNILLGRQF EAKLADFGLS RSFLVGSQTH
VSTNVAGTLG YLDPEYYKKN WLTEKSDVYS FGIVLLEIIT GQHVIEQSRD KSYIVEWAIS
MISNGDIESI MDPNLHQDYD TGSSWKALEL AMSCINPCST ERPNMTRVAH ELNECLEIYE
NLRKRRSQGS NSTKSLVDSI TSISDTPSAR
//
