ID A0A423VKV3_9PEZI Unreviewed; 2476 AA.
AC A0A423VKV3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-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=VPNG_09733 {ECO:0000313|EMBL:ROV91568.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROV91568.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROV91568.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROV91568.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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}.
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:ROV91568.1}.
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DR EMBL; LKEB01000090; ROV91568.1; -; Genomic_DNA.
DR STRING; 1230097.A0A423VKV3; -.
DR InParanoid; A0A423VKV3; -.
DR Proteomes; UP000285146; 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; 4.
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; 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:UP000285146};
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 1278..1874
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2049..2379
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2444..2476
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2331..2353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2476 AA; 280307 MW; 7FF560A167DD676B CRC64;
MANQTSRSLE TYLETLDTLV REIKSRTISE DQRKRFTRQL RDLLAIWQRG TSFNISGPLY
AYVYAPSPTG HQADQLQELV PEHFSIVSAQ LQKAISNLII HGGDTAERLG GVYIIDTLVD
FDGIDMATKY TRFTQNLRQV LRGKDINPMR PAAEVLGRLC RPGGSIISEL VEAECKNALE
WLQSDRIEER RYSAALVLRE LARNAPTLMY AYVGMVFDLV WSGLRDQRHL IRATSAECVS
ACFRIIRERD QELKQIWMDK MYGEALQGLK IGSVEFIHAS LLVLKELLEQ GGMYMQDHYQ
EACDIVSRFK DHRDPTIRKT VVLLIPDLAN YAPSEFASTR LHGFMLHLSG MLKKEKERND
AFLAIGNIAN SVKSAIAPYL DGVLIYVREG LSVQSRKRGS VDPVFDCISR LAVAVGQTLS
KYMEALLAPI FACELTPKLT QALVDMAFYI PPVKATIQER LLDMLSKVLC GQPFKPLGAP
QPNTLPSVPI IQKDPKDPLA YEHRKAEIKL ALNTLGSFDF SGHVLNEFVR DVAIKYVEDD
DPEIREAAAL TCCQLYVRDP IVNQTSYHAL AVVGEVIEKL LTVGVSDLDP NIRRTVLAAL
DERFDRHLSK AENIRTLFFA LNDEYFPIRE VAISIIGRLA RYNPAYVAPS LRKTLIQMLT
ELEFSNVPRN KEESGKLLSL LVQNAQEIIH PYVDSMVKVL LPKASDQTPS VAATIMKALG
ELCAVGGEDM LPYKDELMPI IIEALKDQSS TQKREAALHT LGQLASNSGY VIEPYLDYPQ
LLELLLNIIR SEPQHGSLRQ ETIKLLGILG ALDPYRYQQV EERTPEIQRR VESTAMTDVS
LMMTGMTPSN KEYYPTVVIN ALLNILKDHS LVSHHAQVID AIMNIFRTLG LECVSFLDRI
IPAFLLVIRG TNGPRRESYF NQLATLVSIV RQHIRNFLPE IVEVVQEFWP NSSATLQSTI
LSLVEAISRS LEGEFKVYLA GLLPLMLDVL EHEPTSKRVA SEKVLHAFLV FGSSAEEYMH
LIIPVIVRAF EKPSNPTFLR RSAIETIGKI SRQVNLNDFA AKIIHPLTRV LQTSDLNLRT
AAMETLCALI QQLGRDYLHF SHTVGKILRD NGIQNSNYDL LVNRLKEGGV LPQDLSSETR
FVDQVDETPF ADLGTKKLEM NAIHLKSAWD TRGKSTKEDW QEWLRRFSTT LLTESPNHAL
RACASLASVY LPLARELFNS AFVSCWSELY EQFQEELILN LENAIKSENV TPDLLNLLLH
LAEFMEHDDK ALPIDIRVLG REAARCHAYA KALHYKELEF LQDQSSGAVE ALIVINNQLQ
QSDAAIGILR KAQLYKDGIQ LRETWFEKLE RWEEALAFYN KREAEIPDDQ AVPVEIVMGK
MRCLHALGEW DALGQLTGTT WANSSPDVQR LIAPLATTAA WGLGKWDSMD NYLQSLKRFS
PDRAFFGAIL ALHRNQFREA AQNIEAAREG LDTELSALVS ESYNRAYQVI VRVQMLAELE
EIIVYKQTDG KKQATMRRTW EQRLKGCQRQ VDVWQRMLRL RALVITPTEN MHMWIKFANL
CRKSGRMGLA EKSLKQLIGS DAPLESMIPF WNDRNTRPNI PNQVVYAVLK YQWELGQQIT
HKGTDVSEKA LRCLRLFTAE SAKTFELLRA GSIQTHQANG DAFHLSQSLA YPDGHVGNQD
VYPPRATVDE AVLLAKCYLR QGEWMIALHK DNWQNTHVRE ILTCYSQATK YNSSWYKAWH
AWALANFEVV QAVSARADGG ATRIDHAIVA NHVVPAVHGF FESIALSQGS SLQDTLRLLT
LWLTHGAYSE VNTAVTDGFA LVSIDTWLEV IPQLIARINQ PNKRVQQSVH HLLADVGRAH
PQALVYPLTV AMKSWQGSRR SRSAAQIMDS MRQHSAKLVE QADTVSHELI RVAVLWHELW
HEGLEEASRL YFVVHNIEGM FAALEPLHQL LDRGPETLRE ISFVQTFGRD LTEAREWCRQ
YEVSHDVNDL NQAWDLYYQV YRRIYRQLPQ MTSLELTYCS PKLLEARDLD LAVPGTYKSG
QPIIRIMSFD TTFNVISSKQ RPRKLNINGS DGVSYTFLLK GHEDIRQDER VMQLFGLCNT
LLANDSECYK RHLNIQRYPA IPLSHSSGLL GWVPNSDTVH MLIREYRESR KILLNIEHRI
MLQMAPDYDN LTLMQKVEVF GYALDNTTGQ DLYRVLWLKS KSSEAWLERR TNYTRSLGVM
SMVGYILGLG DRHPSNLMLD RITGKIIHID FGDCFEVAMK REKYPERVPF RLTRMLTYAM
EVSNIEGSFR ITCEHVMRVL RDNKESVMAV LEAFIHDPLL TWRLTNAASP AGPNFTSERD
QVLAGPPVGR GRRPSILEAD PAALRAAQAA VSINNEGPLA GGLPRARART NSSVMPPGSL
TNGANGVNGQ QQNQDPTEIQ NARAIEVLDR VSQKLNGKDF KPGEELDVVT QVDKLIVEAT
KLENLCQHYI GWCSFW
//