ID D7FYJ6_ECTSI Unreviewed; 1929 AA.
AC D7FYJ6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=TOR2 {ECO:0000313|EMBL:CBJ32538.1};
GN ORFNames=Esi_0345_0036 {ECO:0000313|EMBL:CBJ32538.1};
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:CBJ32538.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ32538.1, 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).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN648537; CBJ32538.1; -; Genomic_DNA.
DR STRING; 2880.D7FYJ6; -.
DR EnsemblProtists; CBJ32538; CBJ32538; Esi_0345_0036.
DR eggNOG; KOG0891; Eukaryota.
DR InParanoid; D7FYJ6; -.
DR OMA; HEDWITW; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000002630; Chromosome LG24.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 2.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR_cat.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 2.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1929
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003095554"
FT DOMAIN 527..1279
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1524..1840
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1897..1929
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 216..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1806..1900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1812..1827
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1838..1874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1929 AA; 205045 MW; A9AE225CB83B2484 CRC64;
MAVAGGFRTF LFRQVIVLIY AAGPRLPPWA VSRLVQIVHQ DSLEGYLQLL LPVLLRMIER
RDVGLAMRHI TLAVRALFEA MDTTGCTKRG DWTEWMRVVS VELLRQSPSR VLRPCAALAE
AHQPVAQDLF NAAFLTVWDE LFMENWEGDN THSPVIEAIQ SALSSPSLPP EIQTQLLNLA
GFMELQDKSV TSVMESDFGF AAGGVGWGAA WEGVPAAVPP GGGESVAGSE SGAGGPGSVS
GGGGRSCSGS GPNPDTLEAL ISVNHKLGLD MAAAGILRQA EQQAEAGLCE FVVRPSWLEK
LWRPTVMSRP AAGRQGSGDS LLGGAGGGES SAAAAAAAAA VVAAVTAAAV VAGPSPAVSR
SSSAGLIPGV GPAAAAAVKG GAAGGDEHTP AFDPDRMLLG SFNSDEAFAE VGPAGAPASS
AAAAAAVGMG GAGAWSGGFD GGLSTTDVVV EWYQVMLGRL RCLDALGEHR KEDWARVGVG
REPAGGFSTV AAGARGPRAP KMLPPPALAT KAATKAAAAA SATATTATTV AALTTMTVPA
ALLSTTAYPS LASRSTDSMD LGGGAAAAAS LASAEVMGSR AAWALGEWPA LEMFVRGEHM
QERRHVVEEG QGVEACLVLE AVVATQKGRL DEALTLIEEA RQALAPGLAA LLSESYTRSY
KRMLTIMSLA ELEEVVEYKR VVKDARSLGT PPVKGEGMEG SERSRRWSEV AEHRSNLRAK
WTARLQWVPE DVDVWRGILA VRSLVLKPRE DLGTWLKLAS LARKTGRPEL CANTLRLLGA
QPPRPDEPSG PLTYGRSTAS SGGGTGSSRP RSESSSSVGG GDNSNNNNNN NNNNNNASSS
GFAATSASMS SFSSMLSSAA AQQQENLSLS MHSSRLLTSE LTVPSDAAAA ASGGGGGGGG
GGVSTRTAAV ASSPPPHPRV VYHMYKYMWA TGDQERALGR LERFTSTLML RLRRGHSMHG
VTPPAGSKEA AGHGLRSLLV KCLLQACEWR LEMREMKDSD EQADGQGGGS GGSGGGGGGG
LNPDGNVIPE SLVNTLSWLR RAIELDPTSY DAWHAWALMN YQLTEEENAR RKEIDERERE
EKERGGGGED DDAKREQAQS STAAAAPSSS PGSDLPPPTN TTATTTISSS ALSGKFKIGK
KAVRWLPKWP SLSKAQQGAD PPPQYRDYPS QSSLMRDASP IRSGLERSRG SVGDMSGADT
LRLLTLWFAH GGFESVHREM SLGIQACGVD TWLGVVPQLI ARVHAASPRV TKLLRELLVR
IGRKHPQALI YPITVASKNS SRPRQEAAGA VMADMRKQYP VLVEEASLVS RAMIKVAMTW
PEVWHEGLEE ASRMYFGDGN VEGMLRRLQM LHDLLPWETP PASAVYSGGG GGGAGTTGGA
GGGGACGDLS SSSANAAAAA SGGGGGEGTS STSSPGSDDG SASTDGPAAD TVRGVAFLHL
HGRDLAEAWE WVQRYQACRR EADILQAWDI YYHVFRKISR QLTTLKYIEL RHVAPALPQA
NGLQLAVPGT YRAHADVVRI RSFAPTVEVI TWSKQRPRRM TIHGGDGVPY LFLLKGREDL
RQDERVMQLF GLVNALLASE RKTARFNLSI QRFAILPLSN NSGLIGWVPS CDTMHQLIKH
YRESKEMRLN MEYKIMTSLA PDFDKLPPLN KLEVFERALA QTDGQDLARM LWLKSQSAEA
WLDRRTNYSQ SLSVMCMAGY ILGLGDRHMS NIMVDRVSGR VVHIDFGDCF EVAMQRDKFP
EKVPFRLTRM LVNAMEVSRI EGVFRSTCEM VMAVLRDHKD SLMAMLEAFV HDPLISWRLL
AQPRMSASPL TDEDGEDSDD DDEATHDPTA DGSEVGGHTG ASRSSQYSDG GTTVRSVGST
ATGGERAASG STTSRARGRR RRRRDGRGSF GGMGMSKEPD PLAEVDRLIQ LASNNENLCQ
LFVGWCPFW
//
