ID A0A319F3W5_9EURO Unreviewed; 2392 AA.
AC A0A319F3W5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=BO71DRAFT_479308 {ECO:0000313|EMBL:PYH99622.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH99622.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH99622.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH99622.1,
RC ECO:0000313|Proteomes:UP000247810};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon genotoxic stresses such as ionizing radiation (IR),
CC ultraviolet light (UV), or DNA replication stalling, thereby acting as
CC a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of
CC DNA damage, involved in the regulation of DNA damage response
CC mechanism. Required for the control of telomere length and genome
CC stability. {ECO:0000256|ARBA:ARBA00025079}.
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 -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
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DR EMBL; KZ825800; PYH99622.1; -; Genomic_DNA.
DR STRING; 1448320.A0A319F3W5; -.
DR Proteomes; UP000247810; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
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:0019219; P:regulation of nucleobase-containing compound metabolic process; 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 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; 3.
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; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364109};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
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:UP000247810};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU364109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT DOMAIN 1242..1825
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1999..2315
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2360..2392
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2392 AA; 270577 MW; C7ACB0E2DC410095 CRC64;
MAQAGPITDV TQRLFTELKS KNEETRVRAA YELYDNVLAI SRDWPPEKFL EFFNAVSQRI
AQLVVTGNDA HEKIGGLLAL DRLIDFDGVD AAQKTTRFAS YLRNALRSND NAVLVYAAMA
LGRLAKPGGA LTAELVESEI QSALESLQSE RQEGRRFAAV LVIRELAKGS PTLLYGFVPQ
IFELIWVALR DPKVLIRETA AQAVSECFEI IAARDMQVRQ LWFARIYEEA LLGLKSSSNV
DWIHGSLLVL KELLLKGAMF MNEHYRNACE IVLRLKDHRD PKIRTQIVLT IPILASYAPV
DFTETYLHRF MIYLQAQLKR DKERNSAFIA IGKIANAVGV AIAQYLDGII VYIREGLAMK
ARNRAAIQEA PMFECISMLS LAVGQALSKY MEALLDPIFA CGLSESLTQA LVDMAHYIPP
IKPTIQEKLL DMLSLILYGT PFRPLGCPES RLPPMPSFAR DFAPQEPHTD TEIALALHTL
GSFDFSGHIL NEFVRDVAIN YVESENPEIR KASALTCCQL FVHDPIINQT SSHSIQVVSE
VIDKLLTVGV GDPDPDIRRT VLWSLDRKFD RHLARPENIR CLFLAVNDEV FPVREAAICI
IGRLSSVNPA YVFPPLRKLL VNLLTSLGFA STARQKEESA QLISLFVSNA TKLIRSYVDP
MVNTLLPKAT DANPGVASTT LRAIGELANV GGGEMKTYLP QLMPIILDAL QDLSSHAKRE
AALRTLGQLA SNSGYVIDPY LEYSHLLAVL INIIKTEQTG SLRKETIKLL GILGALDPYK
YQQIGEAAPD IHHINEVQTV SDVALIMQGL TPSNEEYYPT VVINTLMQNI LRENSLVQYH
SAVIDAIVTI FKTLGLKCVP FLGQIIPGFI SVIRGSPPSR LESYFNQMAI LVNIVRQHIR
GFLPEIIEVV RDFWDASYQV QATILSLVEA ISKSLEGEFK KYLAGLIPPM LDTLEKDNTP
RRQPSEKILH TFLIFGTSGE EYMHLIVPSI VRLFDRAQNP QSIRKSAIDT LTKLSRQVNV
SDFASLMVHS LSRVVASNDR LLRQAAMDCI CALIFQLGQD FNHYIHLLNK VLKYHQITHV
NYQILITKLQ KGDPLPQDLN PDENFATLAD DTNYAEIGQK KMVVNQQHLK NAWDASQKST
REDWQEWIRR FSVELLKESP SPALRACASL AGIYQPLARD LFNAAFVSCW TELYDQYQEE
LVRSIEKALT SPNIPPEILQ VLLNLAEFME HDDKALPIDI RTLGKYAAKC HAFAKALHYK
ELEFEQDQNS GAVEALITIN NQLQQSDAAI GILRKAQAYR DVELKETWFE KLQRWEEALA
AYKRREKIDP DSFGVTMGKM RCLHALGEWK VLSDLAQEKW NQASLDHRRA IAPLAAAAAW
GRGQWELMDS YLGVMKEQSP DRSFFGAILA IHRNQFDDAT MYIEKARNGL DTELSALLGE
SYNRAYNVVV RVQMLAELEE IITYKQNIGD PEKQDSMRQT WNKRLLGCQQ NVEVWQRMLK
VRALVTSPRE NLDMWIKFAN LCRKSNRMGL AERSLASLET VVSDTNGTRA IAPPEVTYAR
LKFNWATGHQ REALQMLKEF TSNLTEDLTR FNALMLSQPD HNGVNGVNGL NGVNGIADSN
HTDVMGLRER IGDVAKFRRL LAKSYLRQGE WETTLQRGDW RPDNVHEVLT AYAAATKYNR
DSYKAWHSWA LANFEVVTAI ASQVSRDGTT PLPIVNGHIV TEHVIPAIRG FLRSISLSST
SSLQDTLRFL TLWFTHGGDQ EVSNVVTEGF TAVNIDTWLA VTPQLIARIN QPNHRVRSTV
HRLLAEVGKT HPQALVYPLT VAMKSNVARR SQSASNIMDS MRQHSARLVE QADLVSHELI
RVAVLWHELW HEGLEEASRL YFGDHNVEGM FATLAPLHEM LDKGAETLRE VSFAQAFGRD
LAEAKHYCML YRETEEIGDL NQAWDLYYTV FRKISRQLPQ LSTLDLKYVS PKLKDYVDLD
LAVPGTYQSG RPIIRIISFD PILHVLQTKK RPRRMTLKGS DGNSYMYLLK GHEDIRQDER
VMQLFGLVNT LLDSDGESFK RHLSVQRFPA IPLSQSSGLL GWFSNSDTLH ALIKEYRESR
RILLNIEHRI MLQMAPDYDN LTLMQKVEVF GYAMDNTTGK DLYRVLWLKS KSSEAWLERR
TNYTRSLGVM SMVGYILGLG DRHPSNLLLD RITGKVVHID FGDCFEVAMH REKYPERVPF
RLTRMLTFAM EVSNIEGSYR ITCEAVMRVL RENKDSLMAV LEAFIHDPLI NWRLGVRESP
ERMPFSAERR QSVISNANLE HGVHPSNFSR HRRPSILEGG ILDAQEGIPN EAREAQNARA
LQVLARVKEK LTGRDFKPSE ELNVSDQVDK LLAQATSVEN ICQHWIGWCS FW
//
