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Serine/threonine-protein kinase TOR1 (EC 2.7.11.1) (Dominant rapamycin resistance protein 1) (Phosphatidylinositol kinase homolog TOR1) (Target of rapamycin kinase 1)

 TOR1_YEAST              Reviewed;        2470 AA.
P35169; D6VWN7;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 3.
23-MAY-2018, entry version 184.
RecName: Full=Serine/threonine-protein kinase TOR1;
EC=2.7.11.1;
AltName: Full=Dominant rapamycin resistance protein 1;
AltName: Full=Phosphatidylinositol kinase homolog TOR1;
AltName: Full=Target of rapamycin kinase 1;
Name=TOR1; Synonyms=DRR1; OrderedLocusNames=YJR066W; ORFNames=J1803;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF SER-1972.
STRAIN=RC11-8D;
PubMed=8413204; DOI=10.1128/MCB.13.10.6012;
Cafferkey R., Young P.R., McLaughlin M.M., Bergsma D.J., Koltin Y.,
Sathe G.M., Faucette L., Eng W.-K., Johnson R.K., Livi G.P.;
"Dominant missense mutations in a novel yeast protein related to
mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin
cytotoxicity.";
Mol. Cell. Biol. 13:6012-6023(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=JK9-3D;
PubMed=8186460; DOI=10.1091/mbc.5.1.105;
Helliwell S.B., Wagner P., Kunz J., Deuter-Reinhard M., Henriquez R.,
Hall M.N.;
"TOR1 and TOR2 are structurally and functionally similar but not
identical phosphatidylinositol kinase homologues in yeast.";
Mol. Biol. Cell 5:105-118(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8840504;
DOI=10.1002/(SICI)1097-0061(199607)12:9<869::AID-YEA964>3.0.CO;2-1;
Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
"Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open
reading frames and a gene cluster with a counterpart on chromosome
XI.";
Yeast 12:869-875(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269;
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
X.";
EMBO J. 15:2031-2049(1996).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
FUNCTION, MUTAGENESIS OF SER-1972; ARG-2276 AND ASP-2294, AND
INTERACTION WITH FPR1.
PubMed=7606777; DOI=10.1016/0092-8674(95)90058-6;
Zheng X.-F., Florentino D., Chen J., Crabtree G.R., Schreiber S.L.;
"TOR kinase domains are required for two distinct functions, only one
of which is inhibited by rapamycin.";
Cell 82:121-130(1995).
[7]
FUNCTION.
PubMed=8741837; DOI=10.1091/mbc.7.1.25;
Barbet N.C., Schneider U., Helliwell S.B., Stansfield I., Tuite M.F.,
Hall M.N.;
"TOR controls translation initiation and early G1 progression in
yeast.";
Mol. Biol. Cell 7:25-42(1996).
[8]
FUNCTION.
PubMed=9843498; DOI=10.1093/emboj/17.23.6924;
Schmidt A., Beck T., Koller A., Kunz J., Hall M.N.;
"The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits
turnover of the tryptophan permease.";
EMBO J. 17:6924-6931(1998).
[9]
FUNCTION.
PubMed=9539725; DOI=10.1073/pnas.95.8.4264;
Berset C., Trachsel H., Altmann M.;
"The TOR (target of rapamycin) signal transduction pathway regulates
the stability of translation initiation factor eIF4G in the yeast
Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 95:4264-4269(1998).
[10]
FUNCTION.
PubMed=10329624; DOI=10.1093/emboj/18.10.2782;
Jiang Y., Broach J.R.;
"Tor proteins and protein phosphatase 2A reciprocally regulate Tap42
in controlling cell growth in yeast.";
EMBO J. 18:2782-2792(1999).
[11]
FUNCTION.
PubMed=10198052; DOI=10.1091/mbc.10.4.987;
Powers T., Walter P.;
"Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-
signaling pathway in Saccharomyces cerevisiae.";
Mol. Biol. Cell 10:987-1000(1999).
[12]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-2275.
PubMed=10436010; DOI=10.1091/mbc.10.8.2531;
Alarcon C.M., Heitman J., Cardenas M.E.;
"Protein kinase activity and identification of a toxic effector domain
of the target of rapamycin TOR proteins in yeast.";
Mol. Biol. Cell 10:2531-2546(1999).
[13]
FUNCTION.
PubMed=10604478; DOI=10.1038/45287;
Beck T., Hall M.N.;
"The TOR signalling pathway controls nuclear localization of nutrient-
regulated transcription factors.";
Nature 402:689-692(1999).
[14]
SUBCELLULAR LOCATION.
PubMed=10973982; DOI=10.1074/jbc.M007296200;
Kunz J., Schneider U., Howald I., Schmidt A., Hall M.N.;
"HEAT repeats mediate plasma membrane localization of Tor2p in
yeast.";
J. Biol. Chem. 275:37011-37020(2000).
[15]
FUNCTION IN AUTOPHAGY.
PubMed=10995454; DOI=10.1083/jcb.150.6.1507;
Kamada Y., Funakoshi T., Shintani T., Nagano K., Ohsumi M., Ohsumi Y.;
"Tor-mediated induction of autophagy via an Apg1 protein kinase
complex.";
J. Cell Biol. 150:1507-1513(2000).
[16]
FUNCTION.
PubMed=11741537; DOI=10.1016/S1097-2765(01)00386-0;
Jacinto E., Guo B., Arndt K.T., Schmelzle T., Hall M.N.;
"TIP41 interacts with TAP42 and negatively regulates the TOR signaling
pathway.";
Mol. Cell 8:1017-1026(2001).
[17]
SUBUNIT.
PubMed=12408816; DOI=10.1016/S1097-2765(02)00636-6;
Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L.,
Bonenfant D., Oppliger W., Jenoe P., Hall M.N.;
"Two TOR complexes, only one of which is rapamycin sensitive, have
distinct roles in cell growth control.";
Mol. Cell 10:457-468(2002).
[18]
SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH KOG1 AND LST8.
PubMed=12631735; DOI=10.1091/mbc.E02-09-0609;
Wedaman K.P., Reinke A., Anderson S., Yates J.R. III, McCaffery J.M.,
Powers T.;
"Tor kinases are in distinct membrane-associated protein complexes in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 14:1204-1220(2003).
[19]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[20]
FUNCTION.
PubMed=15620355; DOI=10.1016/j.cell.2004.11.047;
Martin D.E., Soulard A., Hall M.N.;
"TOR regulates ribosomal protein gene expression via PKA and the
forkhead transcription factor FHL1.";
Cell 119:969-979(2004).
[21]
FUNCTION.
PubMed=17560372; DOI=10.1016/j.molcel.2007.04.020;
Urban J., Soulard A., Huber A., Lippman S., Mukhopadhyay D.,
Deloche O., Wanke V., Anrather D., Ammerer G., Riezman H.,
Broach J.R., De Virgilio C., Hall M.N., Loewith R.;
"Sch9 is a major target of TORC1 in Saccharomyces cerevisiae.";
Mol. Cell 26:663-674(2007).
[22]
FUNCTION.
PubMed=25767889; DOI=10.1371/journal.pone.0120250;
Gonzalez A., Shimobayashi M., Eisenberg T., Merle D.A., Pendl T.,
Hall M.N., Moustafa T.;
"TORC1 promotes phosphorylation of ribosomal protein S6 via the AGC
kinase Ypk3 in Saccharomyces cerevisiae.";
PLoS ONE 10:E0120250-E0120250(2015).
[23]
STRUCTURE BY NMR OF 2438-2470.
PubMed=15772072; DOI=10.1074/jbc.M501116200;
Dames S.A., Mulet J.M., Rathgeb-Szabo K., Hall M.N., Grzesiek S.;
"The solution structure of the FATC domain of the protein kinase
target of rapamycin suggests a role for redox-dependent structural and
cellular stability.";
J. Biol. Chem. 280:20558-20564(2005).
-!- FUNCTION: Phosphatidylinositol 3-kinase homolog, component of
TORC1, which regulates multiple cellular processes to control cell
growth in response to environmental signals. Nutrient limitation
and environmental stress signals cause inactivation of TORC1.
Active TORC1 positively controls ribosome biogenesis via control
of rRNA, ribosomal protein and tRNA gene expression, and rRNA
processing. TORC1 positively controls protein biosynthesis by
regulation of mRNA stability, translation initiation factor
activity, and high-affinity amino acid permeases that serve to
provide amino acids for use by the translation machinery. TORC1
also promotes growth by sequestering a number of nutrient and
general stress-responsive transcription factors in the cytoplasm.
TORC1 negatively controls macroautophagy, a process to recycle
surplus cytoplasmic mass under nutrient starvation conditions.
TORC1 controls many of these processes via TIP41-TAP42-mediated
inhibition of the type 2A-related phosphatases PP2A and SIT4
(PubMed:10198052, PubMed:10329624, PubMed:10604478,
PubMed:10995454, PubMed:11741537, PubMed:15620355, PubMed:7606777,
PubMed:8741837, PubMed:9539725, PubMed:9843498). In nutrient rich
conditions, responsible for the phosphorylation of AGC S6 kinase
(S6K) YPK3, activating YPK3 kinase activity and promoting
phosphorylation of ribosomal protein S6 (PubMed:25767889).
Phosphorylates kinase SCH9 at 6 amino acids in the C-terminus,
activating SCH9 kinase activity to properly regulate ribosome
biogenesis, translation initiation, and entry into stationary
phase (PubMed:17560372). {ECO:0000269|PubMed:10198052,
ECO:0000269|PubMed:10329624, ECO:0000269|PubMed:10604478,
ECO:0000269|PubMed:10995454, ECO:0000269|PubMed:11741537,
ECO:0000269|PubMed:15620355, ECO:0000269|PubMed:17560372,
ECO:0000269|PubMed:25767889, ECO:0000269|PubMed:7606777,
ECO:0000269|PubMed:8741837, ECO:0000269|PubMed:9539725,
ECO:0000269|PubMed:9843498}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10436010}.
-!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of
at least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2
(TORC1-B). TORC1 binds to and is inhibited by FKBP-rapamycin.
{ECO:0000269|PubMed:12408816, ECO:0000269|PubMed:12631735,
ECO:0000269|PubMed:7606777}.
-!- INTERACTION:
P53233:FMP48; NbExp=3; IntAct=EBI-19374, EBI-9664;
P20081:FPR1; NbExp=4; IntAct=EBI-19374, EBI-6961;
P38873:KOG1; NbExp=7; IntAct=EBI-19374, EBI-24864;
P38691:KSP1; NbExp=2; IntAct=EBI-19374, EBI-9937;
P41318:LST8; NbExp=5; IntAct=EBI-19374, EBI-28598;
P34072:MKS1; NbExp=3; IntAct=EBI-19374, EBI-10978;
P36003:NNK1; NbExp=3; IntAct=EBI-19374, EBI-9796;
P22211:NPR1; NbExp=2; IntAct=EBI-19374, EBI-12207;
Q03656:SKY1; NbExp=2; IntAct=EBI-19374, EBI-9800;
Q08921:TCO89; NbExp=4; IntAct=EBI-19374, EBI-37395;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10973982,
ECO:0000269|PubMed:12631735}; Peripheral membrane protein
{ECO:0000269|PubMed:10973982, ECO:0000269|PubMed:12631735};
Cytoplasmic side {ECO:0000269|PubMed:10973982,
ECO:0000269|PubMed:12631735}. Vacuole membrane
{ECO:0000269|PubMed:12631735}; Peripheral membrane protein
{ECO:0000269|PubMed:12631735}; Cytoplasmic side
{ECO:0000269|PubMed:12631735}. Note=Also localizes to membranous
structures both proximal to, yet distinct from, the plasma
membrane as well as within the cell interior, probably endosomal
or Golgi membranes. {ECO:0000269|PubMed:10973982}.
-!- MISCELLANEOUS: It may act on another substrate or phosphorylate a
different position in the phosphatidylinositol ring.
-!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 is the initiator.
{ECO:0000305}.
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EMBL; L19540; AAB66881.1; -; Genomic_DNA.
EMBL; X74857; CAA52849.1; -; Genomic_DNA.
EMBL; Z49566; CAA89594.1; -; Genomic_DNA.
EMBL; L47993; AAB39292.1; -; Genomic_DNA.
EMBL; BK006943; DAA08853.1; -; Genomic_DNA.
PIR; S57085; S57085.
RefSeq; NP_012600.1; NM_001181724.1.
PDB; 1W1N; NMR; -; A=2438-2470.
PDB; 2KIO; NMR; -; A=2438-2470.
PDB; 2KIT; NMR; -; A=2438-2470.
PDBsum; 1W1N; -.
PDBsum; 2KIO; -.
PDBsum; 2KIT; -.
ProteinModelPortal; P35169; -.
SMR; P35169; -.
BioGrid; 33823; 438.
DIP; DIP-917N; -.
IntAct; P35169; 37.
MINT; P35169; -.
STRING; 4932.YJR066W; -.
iPTMnet; P35169; -.
MaxQB; P35169; -.
PaxDb; P35169; -.
PRIDE; P35169; -.
EnsemblFungi; YJR066W; YJR066W; YJR066W.
GeneID; 853529; -.
KEGG; sce:YJR066W; -.
EuPathDB; FungiDB:YJR066W; -.
SGD; S000003827; TOR1.
GeneTree; ENSGT00910000144231; -.
HOGENOM; HOG000163215; -.
InParanoid; P35169; -.
KO; K07203; -.
OMA; VCSLCIC; -.
OrthoDB; EOG092C00HJ; -.
BioCyc; YEAST:G3O-31699-MONOMER; -.
BRENDA; 2.7.1.137; 984.
Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
EvolutionaryTrace; P35169; -.
PRO; PR:P35169; -.
Proteomes; UP000002311; Chromosome X.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0010008; C:endosome membrane; IDA:SGD.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:SGD.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0000139; C:Golgi membrane; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0031931; C:TORC1 complex; IPI:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IMP:SGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
GO; GO:0034605; P:cellular response to heat; IGI:SGD.
GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
GO; GO:0001300; P:chronological cell aging; IGI:SGD.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IMP:SGD.
GO; GO:0010507; P:negative regulation of autophagy; IGI:SGD.
GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IMP:SGD.
GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IMP:SGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:SGD.
GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
GO; GO:0001558; P:regulation of cell growth; IMP:SGD.
GO; GO:1905356; P:regulation of snRNA pseudouridine synthesis; IGI:SGD.
GO; GO:0090153; P:regulation of sphingolipid biosynthetic process; IMP:SGD.
GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
GO; GO:0031929; P:TOR signaling; IMP:SGD.
GO; GO:0006413; P:translational initiation; IMP:SGD.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 1.20.120.150; -; 1.
Gene3D; 1.25.10.10; -; 3.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR024585; DUF3385_TOR.
InterPro; IPR003152; FATC_dom.
InterPro; IPR009076; FRB_dom.
InterPro; IPR036738; FRB_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR003151; PIK-rel_kinase_FAT.
InterPro; IPR014009; PIK_FAT.
InterPro; IPR026683; TOR.
PANTHER; PTHR11139:SF9; PTHR11139:SF9; 1.
Pfam; PF11865; DUF3385; 1.
Pfam; PF02259; FAT; 1.
Pfam; PF02260; FATC; 1.
Pfam; PF08771; FRB_dom; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
SMART; SM01346; DUF3385; 1.
SMART; SM01343; FATC; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF47212; SSF47212; 1.
SUPFAM; SSF48371; SSF48371; 6.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51189; FAT; 1.
PROSITE; PS51190; FATC; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Cell membrane;
Complete proteome; Kinase; Membrane; Nucleotide-binding;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase; Vacuole.
CHAIN 1 2470 Serine/threonine-protein kinase TOR1.
/FTId=PRO_0000088813.
REPEAT 114 151 HEAT 1.
REPEAT 249 286 HEAT 2.
REPEAT 627 663 HEAT 3.
REPEAT 664 701 HEAT 4.
REPEAT 747 784 HEAT 5.
REPEAT 788 826 HEAT 6.
REPEAT 832 870 HEAT 7.
REPEAT 908 946 HEAT 8.
REPEAT 950 987 HEAT 9.
REPEAT 1069 1107 HEAT 10.
REPEAT 1109 1147 HEAT 11.
DOMAIN 1331 1919 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
DOMAIN 2125 2437 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 2438 2470 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
REGION 1775 2157 Interaction with FKBP-rapamycin.
COMPBIAS 441 447 Arg/Lys-rich (basic).
MUTAGEN 1972 1972 S->A: No effect.
{ECO:0000269|PubMed:7606777,
ECO:0000269|PubMed:8413204}.
MUTAGEN 1972 1972 S->E,I: Confers resistance to rapamycin.
Abolishes interaction with FKBP-
rapamycin. {ECO:0000269|PubMed:7606777,
ECO:0000269|PubMed:8413204}.
MUTAGEN 1972 1972 S->N: In DRR1-27; confers resistance to
rapamycin. {ECO:0000269|PubMed:7606777,
ECO:0000269|PubMed:8413204}.
MUTAGEN 1972 1972 S->R: In DRR1-1; confers resistance to
rapamycin. Abolishes interaction with
FKBP-rapamycin.
{ECO:0000269|PubMed:7606777,
ECO:0000269|PubMed:8413204}.
MUTAGEN 2275 2275 D->A: Abolishes protein kinase activity.
{ECO:0000269|PubMed:10436010}.
MUTAGEN 2276 2276 R->P: Abolishes rapamycin-resistance of
mutants E-1972; I-1972 and R-1972.
{ECO:0000269|PubMed:7606777}.
MUTAGEN 2294 2294 D->E: Abolishes rapamycin-resistance of
mutants E-1972; I-1972 and R-1972.
{ECO:0000269|PubMed:7606777}.
CONFLICT 58 58 D -> G (in Ref. 1; AAB66881).
{ECO:0000305}.
CONFLICT 115 115 V -> I (in Ref. 1; AAB66881).
{ECO:0000305}.
CONFLICT 133 133 S -> N (in Ref. 1; AAB66881).
{ECO:0000305}.
CONFLICT 231 231 A -> R (in Ref. 2; CAA52849).
{ECO:0000305}.
CONFLICT 396 396 N -> K (in Ref. 1; AAB66881 and 2;
CAA52849). {ECO:0000305}.
CONFLICT 547 547 N -> S (in Ref. 1; AAB66881 and 2;
CAA52849). {ECO:0000305}.
CONFLICT 675 675 T -> I (in Ref. 2; CAA52849).
{ECO:0000305}.
CONFLICT 1292 1292 G -> E (in Ref. 2; CAA52849).
{ECO:0000305}.
CONFLICT 1436 1436 G -> A (in Ref. 2; CAA52849).
{ECO:0000305}.
CONFLICT 1468 1468 A -> R (in Ref. 1; AAB66881 and 2;
CAA52849). {ECO:0000305}.
CONFLICT 1469 1471 WGL -> GGS (in Ref. 2; CAA52849).
{ECO:0000305}.
CONFLICT 1478 1479 EQ -> DE (in Ref. 2; CAA52849).
{ECO:0000305}.
CONFLICT 1590 1590 V -> I (in Ref. 2; CAA52849).
{ECO:0000305}.
CONFLICT 1632 1642 NDPSLPNTFKA -> TILVYQIRSKP (in Ref. 2;
CAA52849). {ECO:0000305}.
CONFLICT 1640 1640 F -> V (in Ref. 1; AAB66881).
{ECO:0000305}.
CONFLICT 1844 1844 L -> S (in Ref. 2; CAA52849).
{ECO:0000305}.
CONFLICT 2202 2202 H -> Q (in Ref. 1; AAB66881).
{ECO:0000305}.
CONFLICT 2414 2414 K -> R (in Ref. 1; AAB66881 and 2;
CAA52849). {ECO:0000305}.
HELIX 2444 2460 {ECO:0000244|PDB:1W1N}.
SEQUENCE 2470 AA; 281140 MW; ACB1781B9963BB1E CRC64;
MEPHEEQIWK SKLLKAANND MDMDRNVPLA PNLNVNMNMK MNASRNGDEF GLTSSRFDGV
VIGSNGDVNF KPILEKIFRE LTSDYKEERK LASISLFDLL VSLEHELSIE EFQAVSNDIN
NKILELVHTK KTSTRVGAVL SIDTLISFYA YTERLPNETS RLAGYLRGLI PSNDVEVMRL
AAKTLGKLAV PGGTYTSDFV EFEIKSCLEW LTASTEKNSF SSSKPDHAKH AALLIITALA
ENCPYLLYQY LNSILDNIWR ALRDPHLVIR IDASITLAKC LSTLRNRDPQ LTSQWVQRLA
TSCEYGFQVN TLECIHASLL VYKEILFLKD PFLNQVFDQM CLNCIAYENH KAKMIREKIY
QIVPLLASFN PQLFAGKYLH QIMDNYLEIL TNAPANKIPH LKDDKPQILI SIGDIAYEVG
PDIAPYVKQI LDYIEHDLQT KFKFRKKFEN EIFYCIGRLA VPLGPVLGKL LNRNILDLMF
KCPLSDYMQE TFQILTERIP SLGPKINDEL LNLVCSTLSG TPFIQPGSPM EIPSFSRERA
REWRNKNILQ KTGESNDDNN DIKIIIQAFR MLKNIKSRFS LVEFVRIVAL SYIEHTDPRV
RKLAALTSCE IYVKDNICKQ TSLHSLNTVS EVLSKLLAIT IADPLQDIRL EVLKNLNPCF
DPQLAQPDNL RLLFTALHDE SFNIQSVAME LVGRLSSVNP AYVIPSIRKI LLELLTKLKF
STSSREKEET ASLLCTLIRS SKDVAKPYIE PLLNVLLPKF QDTSSTVAST ALRTIGELSV
VGGEDMKIYL KDLFPLIIKT FQDQSNSFKR EAALKALGQL AASSGYVIDP LLDYPELLGI
LVNILKTENS QNIRRQTVTL IGILGAIDPY RQKEREVTST TDISTEQNAP PIDIALLMQG
MSPSNDEYYT TVVIHCLLKI LKDPSLSSYH TAVIQAIMHI FQTLGLKCVS FLDQIIPTIL
DVMRTCSQSL LEFYFQQLCS LIIIVRQHIR PHVDSIFQAI KDFSSVAKLQ ITLVSVIEAI
SKALEGEFKR LVPLTLTLFL VILENDKSSD KVLSRRVLRL LESFGPNLEG YSHLITPKIV
QMAEFTSGNL QRSAIITIGK LAKDVDLFEM SSRIVHSLLR VLSSTTSDEL SKVIMNTLSL
LLIQMGTSFA IFIPVINEVL MKKHIQHTIY DDLTNRILNN DVLPTKILEA NTTDYKPAEQ
MEAADAGVAK LPINQSVLKS AWNSSQQRTK EDWQEWSKRL SIQLLKESPS HALRACSNLA
SMYYPLAKEL FNTAFACVWT ELYSQYQEDL IGSLCIALSS PLNPPEIHQT LLNLVEFMEH
DDKALPIPTQ SLGEYAERCH AYAKALHYKE IKFIKEPENS TIESLISINN QLNQTDAAIG
ILKHAQQHHS LQLKETWFEK LERWEDALHA YNEREKAGDT SVSVTLGKMR SLHALGEWEQ
LSQLAARKWK VSKLQTKKLI APLAAGAAWG LGEWDMLEQY ISVMKPKSPD KEFFDAILYL
HKNDYDNASK HILNARDLLV TEISALINES YNRAYSVIVR TQIITEFEEI IKYKQLPPNS
EKKLHYQNLW TKRLLGCQKN VDLWQRVLRV RSLVIKPKQD LQIWIKFANL CRKSGRMRLA
NKALNMLLEG GNDPSLPNTF KAPPPVVYAQ LKYIWATGAY KEALNHLIGF TSRLAHDLGL
DPNNMIAQSV KLSSASTAPY VEEYTKLLAR CFLKQGEWRI ATQPNWRNTN PDAILGSYLL
ATHFDKNWYK AWHNWALANF EVISMVQEET KLNGGKNDDD DDTAVNNDNV RIDGSILGSG
SLTINGNRYP LELIQRHVVP AIKGFFHSIS LLETSCLQDT LRLLTLLFNF GGIKEVSQAM
YEGFNLMKIE NWLEVLPQLI SRIHQPDPTV SNSLLSLLSD LGKAHPQALV YPLTVAIKSE
SVSRQKAALS IIEKIRIHSP VLVNQAELVS HELIRVAVLW HELWYEGLED ASRQFFVEHN
IEKMFSTLEP LHKHLGNEPQ TLSEVSFQKS FGRDLNDAYE WLNNYKKSKD INNLNQAWDI
YYNVFRKITR QIPQLQTLDL QHVSPQLLAT HDLELAVPGT YFPGKPTIRI AKFEPLFSVI
SSKQRPRKFS IKGSDGKDYK YVLKGHEDIR QDSLVMQLFG LVNTLLKNDS ECFKRHLDIQ
QYPAIPLSPK SGLLGWVPNS DTFHVLIREH RDAKKIPLNI EHWVMLQMAP DYENLTLLQK
IEVFTYALDN TKGQDLYKIL WLKSRSSETW LERRTTYTRS LAVMSMTGYI LGLGDRHPSN
LMLDRITGKV IHIDFGDCFE AAILREKYPE KVPFRLTRML TYAMEVSGIE GSFRITCENV
MRVLRDNKES LMAILEAFAL DPLIHWGFDL PPQKLTEQTG IPLPLINPSE LLRKGAITVE
EAANMEAEQQ NETKNARAML VLRRITDKLT GNDIKRFNEL DVPEQVDKLI QQATSIERLC
QHYIGWCPFW


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