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Database: UniProt
Entry: A0A0K9PDD3_ZOSMR
LinkDB: A0A0K9PDD3_ZOSMR
Original site: A0A0K9PDD3_ZOSMR 
ID   A0A0K9PDD3_ZOSMR        Unreviewed;       625 AA.
AC   A0A0K9PDD3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Receptor-like protein kinase 1-like {ECO:0000313|EMBL:KMZ67068.1};
GN   ORFNames=ZOSMA_27G01210 {ECO:0000313|EMBL:KMZ67068.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ67068.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
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:KMZ67068.1}.
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DR   EMBL; LFYR01000932; KMZ67068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9PDD3; -.
DR   OMA; KSRCIGY; -.
DR   OrthoDB; 1215196at2759; -.
DR   Proteomes; UP000036987; 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; IPR025875; Leu-rich_rpt_4.
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   PANTHER; PTHR48010; OS05G0588300 PROTEIN; 1.
DR   PANTHER; PTHR48010:SF59; OS07G0681100 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF12799; LRR_4; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 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:KMZ67068.1};
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:KMZ67068.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:KMZ67068.1};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..625
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005527488"
FT   TRANSMEM        256..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          339..613
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          226..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..240
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         377
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   625 AA;  69369 MW;  F128E6A5C8C4B04F CRC64;
     MVHHQFRFSL LVFILVTVNA ANDLNTDKEA LVSFANLVPH QRALNWDDDN PICSYWIGVM
     CDSGGTRVIA LHLPAIGLLG SIPPNTLGKL DYLQLLSLRY NLLSGDVPLD VSTLASLKYV
     FLQNNNFSGK LPVFLSYHIR ILDLSFNSFT GEISPMINYL FQLRTLDLSN NNLTGEIPDL
     NNLQRLKYFN LSYNSLRGFI PTSLQKISNS SFLGNLGLCG SPLPKCPPSP PLPPPPSLAT
     STKTPHTRSK KKLSTIVIIT IVISGSAILL LVAIIFLLIY LRSKSKEDCQ GLSKGKEAVV
     GPGSSGINNS SSGPHGAEMN KLTFFEGSSF SFNLEDLLRA SAEILGKGSY GTTYKAVLED
     GMTAVVVKRL REVVVGKKDF EQQMEILGRL HRHPNVVPLR AYYYSKDEKL LVYDYLPLGN
     LTSILHGNKT DDRTPLVWES RVRIALGVAR GLWHIHSQGG GKFFHGNLKS NNVLLNRDFD
     GSCISDFGIV PLMNIPTTPR NLVGYRAPEV ILSKKFTKKS DVYSFGVILL ELLTGKAPQQ
     SPGRDDISDL PRWVRSVVKE EWTAEVFDKE LLAMRQNIQD DMLQMLQIAM LCVDRHPDRR
     PTIDQIIGML GDLQTSDSDN RPSSD
//
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