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Database: UniProt
Entry: A0A2K3L0E7_TRIPR
LinkDB: A0A2K3L0E7_TRIPR
Original site: A0A2K3L0E7_TRIPR 
ID   A0A2K3L0E7_TRIPR        Unreviewed;       610 AA.
AC   A0A2K3L0E7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Putative inactive receptor kinase {ECO:0000313|EMBL:PNX72021.1};
DE   Flags: Fragment;
GN   ORFNames=L195_g027909 {ECO:0000313|EMBL:PNX72021.1};
OS   Trifolium pratense (Red clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=57577 {ECO:0000313|EMBL:PNX72021.1, ECO:0000313|Proteomes:UP000236291};
RN   [1] {ECO:0000313|EMBL:PNX72021.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNX72021.1};
RX   PubMed=24500806; DOI=10.3732/ajb.1300340;
RA   Istvanek J., Jaros M., Krenek A., Repkova J.;
RT   "Genome assembly and annotation for red clover (Trifolium pratense;
RT   Fabaceae).";
RL   Am. J. Bot. 101:327-337(2014).
RN   [2] {ECO:0000313|EMBL:PNX72021.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNX72021.1};
RX   PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA   Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT   "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT   (Trifolium pratense) Breeding.";
RL   Front. Plant Sci. 8:367-367(2017).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNX72021.1}.
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DR   EMBL; ASHM01024097; PNX72021.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3L0E7; -.
DR   STRING; 57577.A0A2K3L0E7; -.
DR   Proteomes; UP000236291; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; 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; PTHR48010; OS05G0588300 PROTEIN; 1.
DR   PANTHER; PTHR48010:SF59; OS07G0681100 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 4.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-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:0000313|EMBL:PNX72021.1};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000313|EMBL:PNX72021.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236291};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:PNX72021.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        232..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          315..610
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          266..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PNX72021.1"
SQ   SEQUENCE   610 AA;  66718 MW;  F43AF6A671A62010 CRC64;
     VTSDLNSDKQ ALLDFVSSVP HRRNLKWDLA TSICTSWIGI TCNPNQTRVV SVRLPGVGLV
     GTIPANTLGK IDSLKTISLR SNLLSGSLPP DITSLPSLQY LFLQHNNLSG ELPTSLSSQL
     NALVLSYNSF KGRIPKTLLN LTQLTRLSLE NNSLSGPIPD FHVNLKYLNL SYNHLNGSIP
     SSLHNFSSSS FEGNSLLCGL PLKPCSGVPP SPAPPALAPV KHSSKNKLSK GAIIAIAVGG
     AVLLFFVALV IVLCCLKKKD NGTSREVKAK GPIGGGGRNE KPKEEFGSGV QESEKNKLVF
     FEGCSYNFDL EDLLRASAEV LGKGSYGTAY KAILEELTTV VVKRLKEVVV GKREFEQQME
     IIGSIGSHPN VVPLRAYYYS KDEKLLVCDY YPNGNLSILL HGTRTGGRTT LDWNTRVKIT
     LGIARGIAHL HSVGGPKFAH GNVKSSNVLL NQDNDGCISD FGLTPLMNVP ATPSRAAGYR
     APEVIETRKH THKSDVYSFG VLLLEMLTGK APQQSPVRDD MVDLPRWVQS VVREEWTAEV
     FDVELMRYQN IEEEMVQMLQ IGMACVAKVP DMRPNMEEVV RMIEEIRQSD SDNRPSSDDN
     KSKDLTVQTP
//
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