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Database: UniProt
Entry: A0A218XBE5_PUNGR
LinkDB: A0A218XBE5_PUNGR
Original site: A0A218XBE5_PUNGR 
ID   A0A218XBE5_PUNGR        Unreviewed;      1076 AA.
AC   A0A218XBE5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Probable inactive receptor kinase At5g10020 {ECO:0000313|RefSeq:XP_031396960.1};
GN   Name=LOC116207955 {ECO:0000313|RefSeq:XP_031396960.1};
GN   ORFNames=CDL15_Pgr001837 {ECO:0000313|EMBL:OWM82263.1};
OS   Punica granatum (Pomegranate).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Punica.
OX   NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM82263.1, ECO:0000313|Proteomes:UP000197138};
RN   [1] {ECO:0000313|Proteomes:UP000197138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX   PubMed=28654223; DOI=10.1111/tpj.13625;
RA   Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA   Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT   "The pomegranate (Punica granatum L.) genome and the genomics of
RT   punicalagin biosynthesis.";
RL   Plant J. 91:1108-1128(2017).
RN   [2] {ECO:0000313|EMBL:OWM82263.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Fresh leaf {ECO:0000313|EMBL:OWM82263.1};
RA   Xu C.;
RT   "The pomegranate genome and the genomics of punicalagin biosynthesis.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:XP_031396960.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_031396960.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; MTKT01002011; OWM82263.1; -; Genomic_DNA.
DR   RefSeq; XP_031396960.1; XM_031541100.1.
DR   OrthoDB; 5474002at2759; -.
DR   Proteomes; UP000197138; Unassembled WGS sequence.
DR   Proteomes; UP000515151; Chromosome 5.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR025875; Leu-rich_rpt_4.
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   PANTHER; PTHR48003; OS07G0626500 PROTEIN; 1.
DR   PANTHER; PTHR48003:SF5; OS07G0626500 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 9.
DR   Pfam; PF12799; LRR_4; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
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; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|RefSeq:XP_031396960.1};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000313|RefSeq:XP_031396960.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|RefSeq:XP_031396960.1};
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..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1076
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041122520"
FT   TRANSMEM        634..655
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          796..1076
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          678..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1076 AA;  117707 MW;  85BD6A97FD340DF5 CRC64;
     MCVAFLRFIL GFRVLAFPVK CISRVSYFIP SLSICTSQMT LPHFLTLLLL LLACSSGSDS
     ESDSASLLEF KKGIKLDPLG KVTSSWTLHS DDSSCASSWT GVSCSPDGRV SSLSLDGLDL
     SGDLKFTTLI PLSMLINLTL SGNNFTGRIA PSFGSLGSLQ RLDLSHNSFY GPIPARINDM
     YSLNYLNLSS NGFSGGFPDG IRNLQQLKFF DLHSNDLWGD VGQLLSELRN VEFVDLSNNK
     FFGSVSIGEK NVSSIANTLQ VLNLSRNKLN GEFFDADSIK RFRNLRVLDL GDNLITGQLP
     SFDSLPNLQV VRLGNNLLSG SIPEELLDSL IPLEELDLSG NGFTGSIPDI NSSTMSSLNL
     SSNHLSGSLP SSIGRCLRLD LSRNMITGNI STVKDWETPL EYLDLSSNSL SGSCPDMASH
     YRSLITLRLS NNSLIGALPS LPIFWKLSTV DLSLNKLEGE IPPEFFMSAL NYLNLSRNQF
     NGSIQLQRSN VNELSVVPSI RPMEYLDLSD NKLSGPLSAE IGELVSLRGL NLARNSLSGQ
     LPSELSNLTF LEHLDLSGNN FSGTIPKNLS QNLSVFNVSD NNLSGDVPED LFLKFPSSFL
     GNPLLKLPSG HKLPKVDGNF ENKQRHSSKN SARVAIIVAS VGAAVMIIFV VIAYHRSQTK
     DFHGRSAFSS SPRPSSLFKF HSSGQPPPTS LSFSNDHLLT SNSRSLSGQQ PELPAEIVEH
     SSVPSNPPNL MDAYPATTSG RKSSSPDSPT VSSSPRFIDV CEQPVMLDVY SPDRLAGELF
     FLDPSSMVFT AEELSRAPAE VLGRSSHGTL YKATLDNGHM LTVKWLRVGL VKNKKEFAKE
     VKKIGSMKHP GIVPFRAYYW GPREQERLLL ADYIHGDSLA LHLYETTPRR HSPLSFRQRL
     KLAIDVARSL SYLHDKGLPH GNLKPTNILL TGTDYDAHLT DYGLHRLMTP SGIAEQILNL
     GALGYRAPEL ENAPKPSPSL KADVYAFGVI LMELLTRRSA GDIISGQSGA VDLTDWVRLC
     DQEGRGMDCI DRDIAAGEEH SRAMDELLAV SLRCILSVNE RPNIRQVFDD LCSISV
//
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