ID I0YPN5_COCSC Unreviewed; 2491 AA.
AC I0YPN5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=COCSUDRAFT_30586 {ECO:0000313|EMBL:EIE20354.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE20354.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE20354.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE20354.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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}.
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:EIE20354.1}.
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DR EMBL; AGSI01000015; EIE20354.1; -; Genomic_DNA.
DR RefSeq; XP_005644898.1; XM_005644841.1.
DR STRING; 574566.I0YPN5; -.
DR GeneID; 17038604; -.
DR KEGG; csl:COCSUDRAFT_30586; -.
DR eggNOG; KOG0891; Eukaryota.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000007264; Unassembled WGS sequence.
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: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; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 5.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic 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 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; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000007264};
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 1304..1910
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2085..2405
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2459..2491
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT COILED 1366..1393
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2491 AA; 275854 MW; 71FF55747B3B8BB8 CRC64;
MGSTGVVAGM LERRREAEHH LQDYVEAEAR DLSGEPFTRF MNQIYKRIYA LISRCASLNE
RLGGVLAIDE LIDVKLLGED AAKTSYFASY LREVFQPSTD PMTMEVAAST LGHLVKSGGA
LTADIVDMHH AQVRRSIEWL GDRGEARRYA AALILRELAE NAPAVFNVHV RAFIDAIWSG
LRDAKLLVRE ASVAALRACL VLVEKRETRY RVQWYYRLFE ETQRGLTRYP NSVDHIHGSL
LALGELLRHT GEFMLARYRE VVEIVLHFRE SKEKLIRRAV ISLIPRLAAF APERFAATYL
STCTDYLINV VKTPNKRGPG FVAIGDMALA LASAGCAARM EPVLPRLAEQ LREAIAAPRS
RRGVNCPEAL QCVGVLAEAL RGAWKPYATA LIEPMILMGL SPTLVLALQE LVAALPELLG
HIQGQLLDLL SLVLARRLYR EGLPQLHLNA LHQAVAHGEL QGAALTRLAL QTLVSFDFGS
ARLLDFVRDD VTPYLDEADV SVRRAAAAAA AAVLHRTASA APGSRAAIHP QAHTLAVEAV
VSRLLMAACA DTSVSVRRTV LQSVQAPSPL DTYLAQADSL RALFVALNDE SGAVRALAVG
VAGRLASLNP AYIMPALRKH LMQLLSDMEL SPDSKQREGS AHLLGRLINA CPRLVLPYVS
PILKALVAKL RLAPHLQLTA AGPSGATTKA TLLARVAGPG LRVHIGEVLP LIIEAIQDTS
GGNKRLVAVS TLGQVVESTG LVMSPYLEYP QLLGVLLRML NEGEGSQHVR REVLKVLGII
GALDPHTHKL NQADLQGEGK LEREGVRPQR QLGPDGVLPG ETLGALSFGF MMREEFAHAG
AMGGDELTGD LLSSTGLVTS SEEYYPTVAI NALMRTLRDP AMSSHHPQVV RSLFYIFQAL
QLQAVPYLPK VMSVLLGVLR NADEALSEFL VQQVTALVAL MKAHMRKWLP DILQLIADFW
SPTSPLLPHL LRLLSELAVA LRDDIRAYLP GLLPKFVALF GEAERGGGYE LVRPALACLE
ALGTALEDHL ALLLPALVRL IHPSVAGTPL EIRRAALHSM RRLLPRMPLA GSSAAVLHPL
LRVLDGSVEE LRRDAADTIC SVAIALGPDF ALFVPTISRA MARHKMVHEK FARLAERVTL
QEPPCMSEAD DWESNNRWID DLVPAADATS SLPALPDAAS ESKLPVNEAG LRRAWESSQR
STKEDWAEWM RHFSVELLKE SPSPALRATH SLAQVQPAMA RDLFPAGFVS CWAELEEGMQ
EALVRSLEAA LASPSIPKDI VTTLLNLAEF MEHDEKSLPL DTRTLGALAE KCHAFAKALH
YKEVEFAQTP ETAVESLISI NNQLRQPEAA IGILAVAQND LHMELKESWY EKLNRWEEAL
EAYERKYQNT AGTPAYVDAA LGRLRRDTFP SCDVGKMILC LGALAEWERL SEACRFEWRQ
LEPHLRPRMA YLGANAAWHM GQWDEMSTYV AALESEEGPE LSTGSFMSAV LNVRHGNYAA
AKSCIERSRE LLGQELAALV GESYERAYQN MVRVQQLTEL EETIDYSLAL TLAQGDEVAA
EARRALTRQM WRERLNGVQR NHEVWQSLLS VRSLVLPMHE DTHTWLKFAS LCRKSGRPKQ
AYRTLRSLLG YDPTAIPAGQ SGYGAGSGAP DLMFGFLKHL WATHSRHDAL HRMEDLEHEV
TVSPLPTAEE AAVAAQSIVV GGRTGPAMAI LFATPAGRMA GGYRASLVAR VHLRLGMWRW
SISEASKEVT EDVIEAVKSN LHIAIQAAPD WAKAWHNWGL FNVNAMDHYS RSDVATANRH
VAPAVAAFFK SVSLSQASGG EGSRGSNLQD ILRLLTLWFT HGAAPDVEKA LEEGFGHVSI
DTWLVVIPQV IARIHDQQVV VRRLICSLLI CIGRHHPQAL MYPLLVASKS QSGNRRSAAT
SIIDNVRQHS ATLVEQAQLV STELIRMAIL WHEMWHEALE EASRQYFGES NVEAMLATLM
PLHEMMAQQG PTTLKEIAFV QAYGRELAEA YEWCQKYRMS RREAELHQAW DLYYHVFKRI
NKQLPSLTVL ELQYVAPALV RAQGLELAVP GTYIAGEPVV TIAAFAPQLH VITSKQRPRK
LTIHGSDGAE YMFLLKGHED LRQDERVMQL FGLVNTMLAH DRTTAERDLS IARYAVIPLS
PNSGLIGWVP NTDTLHALIR EYRDARKIPL NVEHRLMLGM APDYDHLTVI QKVEVFEHAL
DSTSGEDLHK VLWLKSRSSE VWLERRTHYT RSTAVMSMVG YLLGLGDRHP SNLMLDRYSG
KLLHIDFGDC FEASMNREKF PERVPFRLTR MMVKAMEVSG VEGNFRSTCE SVMRVLRSNK
DSVMAMLEAF VYDPLINWRL VKTGEGETDN ALAAMNSEML PSNVTFTGKL EDVGSAEMPS
PPRRETRERE MLTAYGQLGD AVEVINERAV AVMKRMSDKL TGRDFVQTLL QEGLPGSTES
DSIQSQVQRL IVQAYSHENL CQSYIGWCPF W
//
