ID A0A072PHU4_9EURO Unreviewed; 2497 AA.
AC A0A072PHU4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, 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=A1O9_03716 {ECO:0000313|EMBL:KEF58873.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF58873.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF58873.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF58873.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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:KEF58873.1}.
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DR EMBL; AMGV01000003; KEF58873.1; -; Genomic_DNA.
DR RefSeq; XP_013261463.1; XM_013406009.1.
DR STRING; 1182545.A0A072PHU4; -.
DR GeneID; 25278650; -.
DR VEuPathDB; FungiDB:A1O9_03716; -.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000027920; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027920};
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 1252..1827
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2001..2321
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"
SQ SEQUENCE 2497 AA; 279318 MW; 42D5BF7D06AB7698 CRC64;
MALQAQAPDP SERIFVELRS KNDEIKNKAA TELKELITLL SREWPPERFS AFYDRVTNRI
SNLIVQAPDS SDKVGGILAL DRLIDCEAVD AAQKASKYSN YLRAALKSND FLVLDAASRA
LGHLARPGGA YTAELVEAEM TSAFEWLQPE NKQESRKLAA VLLIREMAKN SPTLVYGFIP
QIFELIWNAL RDPKDLIRRI AAQSVSACFG VMVARDAQFQ AHWFAKIYSK ALEGFRPNTT
VDEILGSLLI LMELLQQGNM FMHDFYRNAC EIVLRLKDHR DARIRTQVVQ IIPVLAEYAP
LDFINNYLHK FMIYLQAQLK REKERNQAFI AIGQIAKAVG SSIAQYLDGI VLYIRESLSA
KTKNRAAVDE GPMFRCISML AGAVGQTLSK YMEALLDPIF ACGLTEPLEN ALEDMAHNIP
PIRSTIQDKL LDLLSLILVR SPYRPLGCPP NRTPPLPSFA KDYGGLPAEY KDSEITLALM
TLGKFDFSGH ILNEFVRDVT LRYATNENPD IRRAAALTSC QLFMQDPILH QTSNNAIQVV
GEVVDKLLTV AVGDPDADIR MTVLRALDKK FDKHLARPEN IRCLFLAVND EVFAVREAAI
EIIGRLTTVN PAYVFPPLRK LLVNLLTGLG YSNTAKQKEE SARLISLFVA NATSLVKTYV
EAMVSALLPK ATDPNPGVAS TTITALGDLT SVGGEEMVHH LPQLMPIMID ALQDLASHDK
REAAMRTLSS LAVNSQYVID PYIDYPELLG ILINLIKTEA HEELRTDAIK LVGVLGALDP
YKYQQLSESV AEKQSKAEVQ PVSDVALIMQ GLTPSNEEYY PTVVINTLMQ TILADHTLVQ
YHSAVIDAVV TIFKTIGMKC VPFLGQIIPG FLGVIRSSHP SRLESYFNQL SVLVNIVRQH
IRAFLPEVIA VIREFWNVSR QVQSTILSLV EAISKSLEGE FRRYLAGLLP LMLAVIENDS
DLRRESSIRI LHTFLVFGAS GEEYMHMIVP AIVGILENPA APTNARRAAI DTLGKLSRTV
NVTDFASLMV HPLAKLLASP EKVSTNSSER SLKTAALDCI CALIYHLGQD FIHYLPLVER
ATKAGQINSE RFQKLVENFK TGKTLPVDFY PEEQYGLAAE DTTYANITSQ RLPVNQQHLK
NAWDTSQKST KEDWQEWMRR FSVELLKESP SHALRACASL AGVYQPLAKD LFNSAFVSCW
TELYDQYQEE LIRSIEKALT STAIPPDILQ TLLNLAEFME HDDKSLPIDI RTLGKYAAKC
HAFAKALHYK ELEFEQDQNS HSVEALISIN NQLQQSDAAI GILRRAQLFG EVELKEAWFE
KLQRWEEALA AYQKREKIEP ENFDIVMGKM RCLHALGEWK MLSEIAQEHW NSASTENRKN
MSALAAAAAW GRGEWDLMDN YISVMKESSP DRAFFGAILA IQRNNFHEAH NFILRAREGV
NSEITTTIGE SYNRAYGVVV RTQMLAELEE IISYKQSDGM TARQNSLKLL WNKRLLGCQS
NVEVWQRMLK VRALVLTPTD NPDIWIKFAN LCRKSDRIGL AERSLASLGG AGDPPGGPGG
APPPVAYARL KFNWATGSQQ SALAFLRDFT MRLADDFQVN TSLASGVHNE RMNSMNGLDM
NGHDALAQRR KHEELDKCAK LLAKCYLRQG EWQSYLLRGD WTSPRAQEAV RDILNSYQAA
TQYNESWYKA WHAYALANFE VVTSMVSHTD QDKVRTLPEH AIQAHVVPAI GGFFKSIALS
KTSSLQDTLR LLTLWFAHGG HSEVNQAVIE GFASVSIDTW LEVIPQLIAR INQPNPRVRA
AVHRLLAEVG KAHPQALVYP LTVAMKSAVA RRANSATQIM DSMRIHSPIL VEQADLVSHE
LIRVAVLWHE LWHEGLEEAS RLYFGDQDVE GMLATLAPLH ELLDRGAETL REVSFAQAFG
HDLAEARAFC NTFRRSKEIG DLNQAWDLYY AVFRKIARQL PQLMSLDLKY VSPRLKDAHD
LDLAVPGTYV SGKPIIKIIS FNHVLTVIPS KQRPRKMTLK GSDGIPYDFV LKGHEDIRQD
ERVMQLFGLV NTLLTNDTES FKRHLNIQRF PAIPLSQNSG LLGWVPNSDT LHNLVKEYRE
SRRILLNIEH RIMLQMAPDY DNLTLMQKVE VFGYAMDNTT GKDLYRVLWL KSKSSEAWLD
RRTNYTRSLA VMSMVGYILG LGDRHPSNLM LDRITGKIIH IDFGDCFEVA MHREKYPERV
PFRLTRMLTF AMEVSNIEGS FRITCENVMR VIRENKESLL AVLEAFIHDP LLNWRLNTRE
SPPRPHFRSE RRQSIIDAPG TNADAYDRSP MEVNNPSALI TGGAAQSHVG APPGRRHRRS
SILDPAMGGG TILDAAKGGD QNAAAQEAKE VQNARALQVL ARIKEKLTGR DFKPSSPGSA
SAAVHANLRA DLNGLGLGLN LGHMDGKLNG YGQNGRTSAA MMDGGPAKSI AIAGSVPETT
MAGVGGLGVA EQVDRLILEA INVENLCQHY IGWCSFW
//
