ID R0FE21_9BRAS Unreviewed; 669 AA.
AC R0FE21;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EOA20116.1};
GN ORFNames=CARUB_v10000395mg {ECO:0000313|EMBL:EOA20116.1};
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:EOA20116.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; KB870810; EOA20116.1; -; Genomic_DNA.
DR RefSeq; XP_006287218.1; XM_006287156.1.
DR AlphaFoldDB; R0FE21; -.
DR GeneID; 17881087; -.
DR KEGG; crb:17881087; -.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR OrthoDB; 687002at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
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; PTHR27002:SF1047; BNAC09G23880D PROTEIN; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51473; GNK2; 2.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {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|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..669
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004350131"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..127
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 133..245
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 345..622
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 254..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 669 AA; 73815 MW; 075877C2C5A53049 CRC64;
MSRNHIVSIL CFITLVFSLG YVSAQKCGEN LFFKPNSTYD TNRRLVLSTL ASNVSSRDGY
YNVSAGEGAG RIYVLGLCIP GTDPKVCSDC IKPASEGLLQ NCPNQTDSWD WRADKTLCFV
RYSNRSFFDE IDLEPTTAEL LTLDVTGDVA EYNRTWEGFM NRMISAASSS TPGSLAGRHY
AANITPLPGF RRIYVLMQCT PGISSVDCDA CLQANVRTYQ GCCGGKQGGS IRRPVCFFRF
DPYPYLGAFD SITSSSPPPQ SSKDPQESQP AASPPPPDGK KISTGVIVAI VFSVVIFVAL
LVLGLIALKR RQSYKALNLE TNDDITSPHS LQFDFKTLEA ATDKFSVNNK VGQGGFGEVY
KGTLPNGTEV AVKRLSKNSG QGSQEFKNEV VLVAKLQHRN LVRLLGFCLE GDEQILVYEF
VPNKSLDYFL FDPTKQPLLD WSRRYHIIGG IARGILYLHQ DSRLKIIHRD LKASNILLDD
DMNPKIADFG MARIFGIEQT GANTSKIAGT FGYMAPEYVM HGQFSMKSDV YSFGVLVLEI
ISGKMNSSFH QTDGSAGNLV THAWRLWRKG SPLELLDPAF AGNYQSDEVT RCIHIALLCV
QEKPETRPMM STLILMLTSS TITLQVPRAP AFFLQSSRDQ DSEAECSSSY GKTILSSIDD
TSMTDLEPR
//
