ID B7G3H7_PHATC Unreviewed; 2400 AA.
AC B7G3H7;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=PHATRDRAFT_21660 {ECO:0000313|EMBL:EEC46831.1};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC46831.1, ECO:0000313|Proteomes:UP000000759};
RN [1] {ECO:0000313|EMBL:EEC46831.1, ECO:0000313|Proteomes:UP000000759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC46831.1,
RC ECO:0000313|Proteomes:UP000000759};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
RN [2] {ECO:0000313|Proteomes:UP000000759}
RP GENOME REANNOTATION.
RC STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA Rokhsar D., Bowler C.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC ECO:0000256|RuleBase:RU364109};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
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DR EMBL; CM000615; EEC46831.1; -; Genomic_DNA.
DR RefSeq; XP_002181617.1; XM_002181581.1.
DR STRING; 556484.B7G3H7; -.
DR PaxDb; 2850-Phatr21660; -.
DR GeneID; 7202587; -.
DR KEGG; pti:PHATRDRAFT_21660; -.
DR eggNOG; KOG0891; Eukaryota.
DR InParanoid; B7G3H7; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000000759; Chromosome 13.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
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; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
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; IPR024585; mTOR_dom.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
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; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364109};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364109};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364109};
KW Reference proteome {ECO:0000313|Proteomes:UP000000759};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU364109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT DOMAIN 1272..1830
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2022..2341
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2368..2400
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2400 AA; 267676 MW; 08C7AB34CD1B6CEC CRC64;
MANQRAAAEL ASLLWTLAHE MSVEDFGAVE SEVFTLVFAL VHAPDKESRM AGLAALDGLL
VAPSADEEKK AIKFANALST GLRAANGDYE FFSAVSKALG HMAMRISNVD FVEAEVTRAL
EWLRTGRSDR SLLRLRRLAA SLSLKEFAIH APTTFHSKTS QSTLGQGGSN EFLDTIFQSI
RDPQPIVRVC AADALSQCLR ILVDRRHLSL TGLLCQIHFS TMEGLQEATK KQSWHAASES
EAAKHGSLLV VGTMLAYTRE FLLPRFEEIC RAVLACSKNP KVLIRLEVVR LIPKLAACCS
SVFGRRYLEQ SLVFLIDNVS SPASLRDNVD IRPSVYDAIG DLIMAMSDEN TGRRLEEIFA
VVRKGLHAPT SRSSVGHTLC PALHCASSLV EALKDLALPY LDGVIDDMFQ SGLSIDLIQC
LHSIAQSIPM YKDEIEDRML QEVSLSLAGN RRSSDHTLGS SYPAGAASTT ESSNVHINMN
NDAKTTKLLV LSLQTFASFS NSTAQVTLSG KIIPLMPFVQ DVTARYLLHP SNEVRRAAAL
ACCVLLIPHG SIFASAGSCS GLIIEDVLEA LLRAAVSDSS AVVRLCVVRA LDTRYDPFLC
QTHHLQDLFL VLQDETLATR VAGLQLLGRL ASLNPAPILP VLRRFLNDLV VELQCGVDTG
RGREEATRLL VVFLRVKPLQ RLIHPVLATL VGALPLTGAA PPRLASASLE ALGELAQATG
TALQPWVNDI IPHVLNTMKD QSSASKQRTS LRTLGQIAGS TGYVVRLYLD YPNLLSQATD
ILPATKRAPW TLRREVIRTL GIIGALDPDR YYSVASKARK GGVQYAMVAQ PVSNLSPAKR
MTPSEEDFYP TVSIQALMRI FRDSTLTVHH GMVIQAIMFI FKSLGVRCVP FLGKVLPHMI
LTIRHCPSNL KESLFIQLSN LTLVVKAHLR IFVDDIFDIV EQFWDSRHLS IILKLLSNIA
IGVPDAFRQF VPRFIRRLLT SLDELQVADW STAKQSLLPQ NGRAESEKLS HILKSISKLN
SMLREYLHIL IPALLKLADS LASLSFNGAT TTTISILDGF SVLNCRTLSA LIESQAPAPN
PVALALFTGL SCTPPINSEN GLPSRVVQPL VRIFRETPPR SLAVGLSMVE TLFDEHPVAP
ALRASFSVSN RQKVNQGNLQ RAWDVSQRSS REDWDEWMRR FAIQLLREAP SPALRASANL
AHAYQPLARE LFSAAFACCW KELSHPYRTD LLSALETAFV ADISPEILLA LLNLAEFMEH
DPSGGLPIDI SILADLALKC RAYAKALHYK EREYRNGGSG SCVEALISIN RKLDLQEGAL
GILKASAIDD EDASKQSGWW LAKLGNWTEA LEVYREKLKS DPHDFEAIVG CMRCLDASGE
WRKVLDLAEQ NWTALSQHRC IVRMCAQAAW RLGQWDDLEK YSSQLTCVGF DGAFYSAVLH
VHRQDWSHAA DAIDAARKAM DSRFTALLAE SYSRAYPSMV TAQMLSEMEE IIEYMKTEER
SRIEIDHHPA NRQSIERARE RLISVWKDRL AGCRMDSEAH ASILAVRSLV IGPEDDVDAV
LTLSKLSRQA ERHKFAERVL LDPLHSLKIQ HTFYFAYVKH LWYTGEKHEA TRRLEHLCDV
VDMVSHCERI NETSLRVACW LEYGEWKLST TTSLGSSMSP QFQLDVLTSL KRATQPDDCG
YKAWHGWSLL NFRIALQLND RHHLSSQADA QRPGASFDKS IRNHVVAAVR GFVNAINLGT
IKQSASVQQD LLNLLTCLFK FGSLQDVAVV LNECVSSVAI EAWLGVLPQL LARIHIKDPA
IRSVLHPLLT RLGEKHPQAL MYQLSVLLKS PVVERRTAAE SLMNSLKSHS SDLVEESLMV
SSELIRVAIL WSETWHAGLE NASAFFYVEN NIAAMLDQLH SLHGEFEKEP ETSMERDFAE
AHGGNIRQAY DCIKKYIQLS SNDDENLSPE QKDSRREEAE TFLHKAWDSY YVVFRPINQD
LKSMSLLRLP ECSPALSRAR NLELGVPGSY RVDGSYVRIQ KFVQRVSIIN SKQRPRKVTL
RGSDGKHYVF LLKGHEDLRQ DERVMQLFGL VNALLVRDPQ TKNQDLMIKR YTISPLSHNC
GLVGWVPHCD TMHALIRDYR EAKKVPMNIE NREMMKTAPD YDLLTGMQKV EVFTDALQKT
PGKGDDLAEI FWLKSTNSEE WLERRTKYTR SLAVMSMVGY ILGLGDRHPS NLMIDKLSGR
VLHIDFGDCF EIAMVRDKYP ERVPFRLTRM LVKAMEVSGI EGTYRSTCER TMNLLRSSRD
TLVAMLEAFV HDPLISWRLV NFITGGASAR VATETSIARS RMERSLMGVM GGENGVVHEE
ALNVKALQVI RRVEDKLSGT DFPDCEGEPL DVSDQVQRLI VQATSSENLC QLFIGWCAFW
//
