ID D7FRQ5_ECTSI Unreviewed; 942 AA.
AC D7FRQ5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Similar to CG1848-PA, isoform A/ leucine rich repeat protein {ECO:0000313|EMBL:CBJ30846.1};
GN Name=LRR-PK {ECO:0000313|EMBL:CBJ30846.1};
GN ORFNames=Esi_0217_0027 {ECO:0000313|EMBL:CBJ30846.1};
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:CBJ30846.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ30846.1, 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; FN648395; CBJ30846.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FRQ5; -.
DR STRING; 2880.D7FRQ5; -.
DR EnsemblProtists; CBJ30846; CBJ30846; Esi_0217_0027.
DR InParanoid; D7FRQ5; -.
DR OrthoDB; 1356102at2759; -.
DR Proteomes; UP000002630; Unplaced LGUn.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_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 PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR23257:SF966; SERINE_THREONINE-PROTEIN KINASE DDB_G0281745-RELATED; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00364; LRR_BAC; 4.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00220; S_TKc; 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 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}.
FT DOMAIN 677..937
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 202..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 705
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 942 AA; 100322 MW; 0E0DA5FC95970CDB CRC64;
MIGLSLLVAQ NAGCACWWAG RALSITMGRS KSLVENELTT LPEGIFGGLS AMEILYLWHN
ELTTLPEGIF QNATALQQLS LYGNQLTTLP EGIFGGLTAL GYLWLTYNNL TTLPEGIFGG
LTGLEYLNLD GNALECLPST TLVEVDDYAS FYEIGLHVDP YGDECGCSIE GVIDNVCGQE
ACTPGDEGYT CAVTLAPAPA PALGTTAPES TPHPTSVPGS SSEGDASTAG VVVGVVAGAL
ALAALGFFLR RRRVAKSTGP DPSAPRYYAG ESLKHGLGEQ HQQRQQDMHS SSPIITGSAG
GNATRGPPPP TQQDSPPPPP PNAHDGADQR DARPLSPNMH DRGTHQRDAR PPAASQQHAA
VVAETTFGED CTPIQSLFPA PPVGALPKSE ENPRRRTRDK NKSGGGTRAA DSGRGRGGDD
AAENGGGCVA AAEQSLLSLT TTNSTADMST EERTAEVAGL RFSAEGKGDS APSAAAPSPA
AAPAGGRRRT SCGIGYGQAV LAAAEELVHN CQIPGVCEAA TAVSILIRLV LDSRDLTSSP
GVKRCRSIVT MLQRAAKVVG TGGDTSTEEG RVLMEEVHGA VSDLVELIKT YENKSKLAQM
LTSTLFKRRQ DELNAVLDRA IWGLHLGLQV QVGHDVAHLV KRSTAEAQDQ AESVAEARRL
RRRRKLDQNE IPEDHVSITN EMLGKGGFGV VYLADYNGHN AAAKKAERKA FLRELEAMIR
LRNPHTVNVY GAITSQPNRL VLVMELLAGG DLRAMLKNSE QPLPEDKCRQ IIHDVCAGMA
FLHSKATVHG DLKSANVLLD GRGRAKIGDF GTSRWAQNTE RSTGLATYTT NPGPSTHISL
AWTAPEVLEA KETSKASDVY SFGMVAWEVL TRQTPWADQT RPRDIFLRVV MREERPAIPA
DAPVDIAEMV RSCWAQEPLD RPTFPVLYNE GNVQPTALST SS
//