ID U1GKJ2_ENDPU Unreviewed; 2456 AA.
AC U1GKJ2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=EPUS_06030 {ECO:0000313|EMBL:ERF72401.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF72401.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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; KE721107; ERF72401.1; -; Genomic_DNA.
DR RefSeq; XP_007801910.1; XM_007803719.1.
DR GeneID; 19240977; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000019373; 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; 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:UP000019373};
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 1250..1823
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1997..2312
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2424..2456
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1101..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2297..2320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2456 AA; 276319 MW; 2283E287D4626206 CRC64;
MAQQVQNLDP TRRLFEELKS KNEDVRTRAS NELRETLNSL SREWSPEKFT EFYNSVSSRI
NSLVQSPEPY EKLGGLWALD RLINIEGVDA ALKTSRFVSY LHNALRSNDY VVLDKAAQCL
GHLAKPGGAL TAELVESEIQ SAMESLQSDR QEGRRLAAVL VIRELAKNSP TLLYGFVPQI
FELIWIPLRD SKELIRKISA EAVSACLAII VARDAQFRQQ WFSRIYDDAL DGLKSLNVDW
IHGSLLILQE LLLKGAMFMH DFYRNACEIV LRLKDHRDAK IRAQVVQTVP ILADYAPVDF
INNYLHKFMI YLQAQLKRDK ERNAAFVAIG SIAKAVGSSM APYLDGTIVY IRESLSAKNR
NRAGVDEGPV FKCISMLSYA VGQTLSKYMD ALLDPIFACG LSKPVEQALV DMAHYIPPIR
AAVQEKLLDM LSLILIGTPY RPLGCPDNRT PPLPSFAKDY GGFVGEHSDA EITLALWTLG
TFDFSGHILN EFVRDVTVRY SENEKPEIRK AAALTCCQLF VHDPIVHQTS SHSIQVVSEV
IDKLLTVGVG DPEPDIRLTV LKSLDSKFDR HLARPENIRC LFLAVNDEVF AVREAAITII
GRLSTVNPAY VFPPLRKLLV NLLTGLGYSN TARHKEESAH LIRLFVRNAS RLIRTYVEPM
VAALLPKATD PNPGVAATTI GALGELASVG GDEMKHHIPE IMPIVLEALQ DLGSHSKREA
ALQTLGSFAI NSGYVIDPYL DHPQLLGILI NIIKTESHEL LRQDAIKLLG VLGALDPYRY
QQISEGTAES KSNVETQAVS DVALIMQGLN PSNEEYYPTV VINTLLQTIL RDHSLVTYHS
AVIDAIVTIF KTLGLKCVPF LGQIIPAFLA VIRSAPTSRL GPYFNQLAIL VSIVKQHIRA
FLPDILEIAR ECWNKSNQVR STILSLVEAI SKSLEGEFKK YLAGLLPLLL GVLEQDIDPT
REASIRILHT FLVFGSSGEE YMHLIIPAIV RMFDSPTAPV SSRKAAIDTL SKLCRLVNVS
DFSSTMIHPL AKVIGTPPEK VATNAAERQL KTAAMDCISS LLFQLNQDFI HYIPLVNKAA
KVGQISNHTY NKLVSKLQKG ESLPQDLNSD ETHGPLGEDN SYSAVESKKL PVNQEHLKNA
WDTSQKSTRE DWQEWMRRFS VELLKESPSH ALRACASLAG VYQPLAKDLF NAAFVSCWPE
LYDQYQEELV RSIEKALSAA NIPIDILHVL LNLAEFMEHD DKALPIDIRE LAKIASKCHA
FAKALHYKEL QFEQDQNGST VEALISINNQ LQQTDAAIGI LRKAQYYSEV ELKEAWFEKL
QRWEEALDAY NRRENIEPQN FDVIMGKMRC LHALGEWKVL SELAQDHWQE ANGDQKKQMA
ALAAAAAWGR GQWDLVDPYL SALKEDSADR SFFGAVLSLH RNSFEEAERF ISKARAAVNA
ELTAIIGESY NRAYNVVVRT QMLTELEEII TYKKGASDPR KQEQLRKTWD RRLLGCQQNV
EVWQRMLKVR ALVINPSENL EMWIKFANLC RKTARSSLAE RTLASLENVT RDESGNVPPQ
VSYARLKYNW AIGNQQNTLI FLKDFTARLS EEYAHYNATL VNGVNGDRNN GIGAPALNSQ
DSMATRSKML EATKYTKLLA KCYLKQGDWQ AHLHKGDWSS DHVREGVRDI LNSYSAATQY
NRTSYKAWHA WALANFEVVT SMDSHADQER VKLPENIILD HVVPAVRGFF KSISLSTTSS
LQDTLRLLTL WFAHGGHHEV NLAVTEGFQS VSIDTWLEVI PQLIARINQV NQRVRLSVHR
LLSEVGKAHP QALVYPLTVA IKSNVARRSH SATQIMESMR QHSPTLVEQA DLVSHELIRV
AILWHELWHE GLEEASRLYF GDQNVEGMFA TLAPLHEMLD RGAETLREVS FAQAFGHDLA
EARHFCNVHK QTQELGDLNQ AWDLYYTVFR KIARQLPQLM TLDLKYVSPR LKEARNLDLA
APGTYHSGRP VIKIVEFDHV LTVIPSKQRP RKMTLKGSDG MPYTYVLKGH EDIRQDERVM
QLFGLVNTLL NNDADSFKRH LNIQRFPAIP LSQNSGLLGW VPNSDTLHNL IKEYRESRRI
LLNIEHRIML QMAPDYDNLT LMQKVEVFGY AMDNTTGKDL YRVLWLKSKS SESWLERRTN
YTRSLAVMSM VGYILGLGDR HPSNLMLDRI TGKIIHIDFG DCFEVAMHRE KYPERVPFRL
TRMLTFAMEV SNIEGSFRIT CEAVMRVIRE NKDSLVAVLE AFIHDPLLNW RLNVRESPPR
PHFRSERRAS IIENIPVNLD NPANHSPPSP VTQPPGNPYR HRRSSVLEAL PGGLSSIRSP
NNPQDAREVQ NARALQVLAC VKQKLTGRDF PPTSTTGQGN SILTPAQRLE ASTAGSMDLG
AIVAAAALDG SAGGHMGMER RGEGELLVAE QVEKLIKQAT NTENLCQHYI GWCSFW
//
