ID A0A0D2FHR7_9EURO Unreviewed; 2497 AA.
AC A0A0D2FHR7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=PV04_05666 {ECO:0000313|EMBL:KIW66330.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW66330.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW66330.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW66330.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) 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; KN846959; KIW66330.1; -; Genomic_DNA.
DR STRING; 5601.A0A0D2FHR7; -.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000054266; 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; 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 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}; 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 1252..1828
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2002..2317
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2465..2497
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2279..2309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2322..2346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2282..2309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2497 AA; 280111 MW; F838A60AEAF675C9 CRC64;
MAQQGPGPDP SERIFTDLRS KNDEVKNKAA AELRDLITLL SREWSPERFS AFYDKVTTRI
SNLIVQAPDI SDKVGGILAL DRLIDCDAID PAQKASKYSN YLRAALKSND YSVLDAAARA
LGHLARPGGA YTAELVEAEL TSAFEWLQPE TKQESRKLAA VLLIRELAKN SPTLVYGFIP
QIFDLVWNAL RDPKDLIRRV AAQSVSACFG VMVARDAQFQ NHWFAKIYSK TLEGFRPNAT
VDEILGSLLI LNELLQQGNM FMHDFYRNAC EIVLRFKDHR DPRIRTQIVQ VIPVLAEYAP
LEFINNYLHK FMVYLQAQLK RDKERNQAFV AIGQIANAVG SAMAQYLDGI ILYIRESLSA
KTKNRAAVDE GPMFKCISML AGAVGQTLSK YMEALLDPIF ACGLTEPMEQ ALEDMAHNIP
PIRATIQDKL LDLLSLILVR SPYRPLGCPP NTIPPLPSFA KDYGGFPAEH KDYEITLALK
TLGKFDFSGH ILNEFVRDVT LRYATNENPE IRRAAALTCC QLFMLDPILH QTSNNAIQVV
GEVVDKLLTV AVGDQDADIR VTVLRALDRK FDKHLARPDN IRCLFLAVND EVFPVREAAI
EIIGRLTTVN PAYVFPPLRK LLVNLLTGLG YSNTAKQKEE SARLISLFVS NATSLVRTYV
EAMVSALLPK ATDTNPGVAS TTIKALGDLT SVGGQEMVQH IPELMPILID ALQDLASHEK
REAAMKTLSS LAINSQYVID PYMDYPELLG ILINIIKTEA HEELRTDAIK LVGVLGALDP
YKYQQLSESV AEKQSKAETQ PISDVALIMQ GLTPSNEEYY PTVVINTLMQ TILADHTLVQ
YHSAVIDAVV TIFKTIGMKC VPFLGQIIPG FLSVIRSSPP PRLESYFNQL AVLVNIVRQH
IRAFLPDIIE VIREFWNVSR QVQSTILSLV EAISKSLEGE FRRYLAGLLP LMLGVIENDS
DLRRESSIRI LHTFLVFGAS GEEYMHMIIP AVVGIFENPA APPNARRAAI DTLGKLSRTV
NVSDFASLMI HPLAKILSSP EKVVTNSSER SLKSAALDCI CALIYHLGQD FVHYLPLIER
STKAGQINSD RFQKLIENFK SGKPLPVDFY PEEQYGSTAE ETTYANITSM RLPVNQQHLK
NAWDTSQKST KEDWQEWMRR FSVELLKESP SHALRACASL AGVYQPLAKD LFNSAFVSCW
TELYDQYQEE LIRSIEKALT SPNIPPDILQ TLLNLAEFME HDDKSLPIDI RTLGRFAAKC
HAFAKALHYK ELEFEQDQNS QSVEALISIN NQLQQSDAAI GILRRAQVFG EVELKEAWFE
KLQRWEEALS AYQKREKIEP ENFDIVMGKM RCLHALGEWK ILSEIAQEHW NSASTENRKN
MSALAAAAAW GRGEWDLMDN YISVMKESSP DRAFFGAILA IQRNNFADAQ TFIVRARDGV
NSEITATIGE SYNRAYSVVV RTQMLAELEE IITYKQSEGN SEKQESLKML WNKRLLGCQS
NVEVWQRMLK VRALVLQPTD NSDIWIKFAN LCRKSERIGL AERSLSSLGG GGNLAANLVD
APPTVAYARL KFTWATGHQE TALAALRDFT TRLADDFQQT NTALANGVHN DRLNNQNGLD
MNGHDLLAQR KKHEELEKCS KLLGKCYLRQ GEWQSFLLRG DWTSPRAQDA VGDILNSYQL
ATQYNETWYK AWHAYALANF EVVTSMASHT DQEKVRSIPE QAIKGHVVPA IAGFFRSISL
SKTSSLQDTL RLLTLWFAHG GHSEVNQVVI EGFTSVSIDT WLEVIPQLIA RINQPNVRVR
AAVHRLLAEV GKAHPQALVY PLTVAMKSSV TRRANSATQI MDTMKGHSLR LVEQADLVSH
ELIRVAVLWH ELWHEGLEEA SRLYFGDGNV EGMLATLAPL HELLDRGAET LREVSFAQAF
GHDLAEARAF CNAFRRSKEI GDLNQAWDLY YAVFRKIARQ LPQLMSLDLK YVSPRLKDAH
DLDLAVPGTY QSGKPITKIV SFDHVLTVIP SKQRPRKMTL KGSDGVSYAY LLKGHEDIRQ
DERVMQLFGL VNTLLNNDTE SFKRHLNIQR FPAIPLSQNS GLLGWVPNSD TLHNLVKDYR
ETRRILLNIE HRIMLQMAPD YDNLTLMQKV EVFGYAMDNT TGKDLYRVLW LKSKSSEAWL
DRRTNYTRSL AVMSMVGYIL GLGDRHPSNL MLDRITGKII HIDFGDCFEV AMHREKYPER
VPFRLTRMLT FAMEVSNIEG SFRITCENVM RVIRENKESL LAVLEAFIHD PLLNWRLNTR
ESPPRPHFRS ERRQSIIDAP GAQHEDYDRS PMENVHNPAA MAQGTSHVGA PPGRRPRRSS
ILDPAMGGGS VLDKILDSNN SAAQEAKEVQ NARALQVLAR VKEKLTGRDF KPSAPGTPSY
AATQALRADL NGLGLESIMN SSTGATNNNT NGAIDPRNGM LDLGNMKQRE VVAGTAPETT
MAGIGGLGVS EQVDRLILQA TNVENLCQHY IGWCSFW
//
