ID D7FM46_ECTSI Unreviewed; 866 AA.
AC D7FM46;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative Leucine Rich Repeat Protein Kinase {ECO:0000313|EMBL:CBJ29871.1};
GN Name=LRR-PK {ECO:0000313|EMBL:CBJ29871.1};
GN ORFNames=Esi_0163_0063 {ECO:0000313|EMBL:CBJ29871.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ29871.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ29871.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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DR EMBL; FN648164; CBJ29871.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FM46; -.
DR STRING; 2880.D7FM46; -.
DR EnsemblProtists; CBJ29871; CBJ29871; Esi_0163_0063.
DR InParanoid; D7FM46; -.
DR OrthoDB; 1333437at2759; -.
DR Proteomes; UP000002630; Chromosome LG02.
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 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; IPR046959; PRK1-6/SRF4-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR48007:SF9; LEUCINE RICH REPEAT N-TERMINAL DOMAIN AND SERINE-THREONINE_TYROSINE-PROTEIN KINASE CATALYTIC DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48007; LEUCINE-RICH REPEAT RECEPTOR-LIKE PROTEIN KINASE PXC1; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 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; 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:CBJ29871.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:CBJ29871.1}.
FT DOMAIN 137..400
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 403..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 866 AA; 93677 MW; BBD3D09B04C944B8 CRC64;
MIAVHRGRQT ADHAVLATIK DLVTEAQVFM ERFLDPEWWS KGASRKEDSE MFRELTFRLG
FLMQAPPGFQ EQSQEEDHAD RLQDYSDLQI ILEEKLRVTK DERVARDIMA VLRRVSMRAA
SEGRFAASEI GFDRLQFLGE RSLGNGGFGT VLGASLEGAP VAVKKLNNQN IRAELLDGLR
RDVQDFHAMQ YDFVVRTLGG CTVRPNVCIV QEQAATNLFD LLHRPDLSIP LTLPSPEKAA
MLYDVARGLH FLHVKRMVHG NLKSTNVLVF ENNRLKVSDF GMIALRESQS LGGGDTVGSA
AWTAPEVLDD QNPSVLSDVY SFGILVHEVL TQRVPFAGKN VAKVITAVVA KGHRPGYLEN
EEAQFPPGLT KLVDVCWTQD PAARPTSLNG IVTELGHILN ALGGDPRPQP HTQTAGEAAP
STPIEQNTPG RIPRVSMTEQ ERRIHDLEQE LRALKMQKGG DGGGRGGSGE RKALRALYTA
TQGPGWYEQT GWETNDPNLS KWYGVVCGEG GRVTSLHLRS NNLQGQLPRE LGCLSRLKTL
VLSDNKLEGP VPHEFGDLGR LAELDLSMND LTGAIPGGLS RAVSLERLYL QCNGFTGNLP
RSLQKLNHLK IFMVDWRELS DTHPFRNFRK ASPPPTQAEM DRALCESRTI ARARTLMSAR
AACPPAPTNP NQQQIPPGYP GAAAGLSHSN PGSNPQTPIS SNGGGAPRGG GGGGGGDRFK
VMLRGGSSGS RSDTPSRLGR ATSAVEGPVS GAAYGGGEEW VGGGDGRAPG NSGDGGGQWM
NAHQHQYPGA AAPYHTPTAP YRGEDGIQSK AKAKVEAEAP APARKWKNAF SFAGKHLKDI
VAVDLHPGFT DSSHQGNEQP PPRGNK
//
