ID A0A1S8B406_9PEZI Unreviewed; 2406 AA.
AC A0A1S8B406;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=BK809_0006220 {ECO:0000313|EMBL:OMP81911.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP81911.1, ECO:0000313|Proteomes:UP000190776};
RN [1] {ECO:0000313|EMBL:OMP81911.1, ECO:0000313|Proteomes:UP000190776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F98.1 {ECO:0000313|EMBL:OMP81911.1,
RC ECO:0000313|Proteomes:UP000190776};
RA Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT in grapevine trunk diseases.";
RL Submitted (JAN-2017) 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}.
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:OMP81911.1}.
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DR EMBL; MSZU01000114; OMP81911.1; -; Genomic_DNA.
DR STRING; 420778.A0A1S8B406; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000190776; 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: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; 3.
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; PF13513; HEAT_EZ; 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 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:UP000190776};
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..1842
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2016..2333
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2374..2406
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2318..2348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2406 AA; 271898 MW; D987C9F45370A897 CRC64;
MAQASPETVD RLFNELKSRN TDVRENAAKA LRQSLEAAHR ELPPGQFANY YDRVCNRINA
LVVQGNETNE RLGGIQALDQ LIDFKGDDAG QKTTRFASYL RAISQGNDNA AIDAASHALG
RLAKPGGTLT AELVEAEVKS ALEWLQMDRQ ENRRFAAVSN LRELAKNSPT LMYQWVPQIF
EVIWYALRDP KVRIRQAAAE AISSCLEIIS ARDQQMRNHF FGKVYEQVLT GFTVNTVESI
HGAILAMKEL LRRGAMFMHG SRYIEACNNV LRYKDHRDPL IRQEVIVTIP LLAAYSPNDF
SQHYLHTCML HLQGLLREEN KDRSAAFIVV GKIAGAVGSH FGKYIDGTLT VIKNTLIRKT
RYRAQEEPAI FECLSMLSIA VEQALSKHVD SLLDPMFSCG LSDPLTQCLV DMAHYVPSSR
AAIQERLLDL LSQVLCGRSF ISMGSPQHHA SSPPQIWTRD HKPPEIIRQK EAEIALALKT
LGEFNFSGHV LNEFVRDVAI KYVEADNREI RKAAALTACQ LFIGDPIVTQ TSQHAIQVVG
DVIEKLLTCG VADVDPDIRH TVLRALDYRF DRHLGKAENV RSLFLALNDE VFEIRRAAIS
IIGRLTSVNP AYVFPSLRKV LVQLLTEIEY SNSARDKEES ARLISNLVGA SPKLIKPYVD
PMITVLLPKA RDSNSEVASS TLKAIGDLAT VGGDDMKQYI PELMDIIIEN LQDLSSESKR
MAALIALSQL ASNAGYVIEP YKEHSELLTI LINIVRTEPA NTLRKETVKL MGVLGALDPD
EYQKIVEKSP EHNLQAEAQA VTDVSLIMSG ITPSNEEFYP TVVINTLMGL LKDTSLAQYH
SAVVDAVMNI YATMGLKCVP FLPQVVPGFL GVIRGAPAGR VEGYFNQLSQ LVRVVRQHIR
PFLPSILETV KEFWSGGIQL QATILSLIEA IARSLEGEFK IYLANVLPLM LGVLDQDTSV
KRLPSERVLH AFLIFGSSAE EYMHLIIPVI VRMFDKPGQP HGLRKSAIET IGRLSRQVNI
SEFAAMIIHP LSRVLAGSDI ALKQTALDTL SALIFQLGPD YIHFIPTINK ILVTHKVPHS
NYALIVSKLQ RGEPLPQDLS PDERYGDDDE DLNATEISTK KLAVNQQHLK NAWDATQKTT
REDWIEWMRR FSVELLRESP QQALRACTPL ASVYNPIAKS LFNSAFVSCW TELYDQYQEE
LVRSIEIALA SPNIPPEILQ ILLNLAEFME HDDKALPIDV RTLGMYAARC HAYAKALHYK
ELEFNAEQNA RAVEALISIN NQLQQTDAAF GILRKAQNYQ DVELKETWFE KLEKWEEALK
SYQRREKDEP DSFEITMGKM KCLHALGEWD VLSTLAQDKW IHAPQEYRRS IAPLAAAAAW
GLGQWELMDQ YLSVMKSSSP DWSYYGAILA IHRNQFEEAQ KHITKTRDGL DTQLSAVFGE
SYQRAYLPLV RVQMLAELEE IITYKQNSSN PEKQASMRST WMKRLLGCQP NPEIWQRMLK
VRALVISPRD NMQMWIKFTN LCRKNQRVGL AEKSLRSLLG GTHEDIFGYV RNHAHEIPHP
ISYAVFKFMW SSDRNEEALD LLKDFTARVA DDLQIRSKDA MGQNGNMPNG INGHHGVNGV
HGFTGLVNGM HGLNMNGSAM VNGNSQPPGT NHFDLAETQK LLAKCYLKQG EWQTHLHNGD
WTHEHVHEVL SAYAAATRYN QNWYKAWHAW ALANFEVVNA MSPQADRSTP DLPASAVHEH
IVPAIHGFFK SISLSSASSL QDTLRLLTLW FAHGGHPEVN TAVTEGVGTV SIDTWLEVIP
QLLARINQPN VRVRQSIHNL LSDVGRAHPQ ALVFPLTVSM KSDVTRRLRS ATALMDAMRQ
HSPKLVDQAD SVSHELIRIA VLWHEQWHEG LEEASRLYFG DRNIEGMFAT LAPLHAMLDK
GPETLREISF IQSFGRELQE ARDWCQTFRN SGEEGDLNQA WDLYYQVFRK IARQLPSLMT
LELQYVSPKL KAVHDLDLAV PGTYQSGKPI IRIQSFDPVS TVIQSKQRPR RLMIKGSDGV
NYMFVLKGHE DIRQDERVMQ LFGLVNTLLD HDAECRKRHL NIQRYPAIPL STQSGLLGWV
PNSDTLHVLI REYRESRKIL LNIEHRIMLQ MAPDYDCLTL MQKVEVFGYA LDNTTGQDLY
RVLWLKSKSS EAWLDRRTNY TRSLAVMSMT GYILGLGDRH PSNLMLDKVT GKIIHIDFGD
CFEVAMHREK YPERVPFRLT RMLTYAMEVS NIEGSYRTTC EHVMRVLRSN KESVMAVLEA
FIHDPLLNWR LGTRESPLEP SFTSQRRASI MGDAVVPGER PESSFRPRHR SSIVPPGVAG
PNEPEAREEQ NARALQVLSR VKQKLTGRDF KPQEELNVNN QVDRLIREAT NLENLCQHYI
GWCSFW
//
