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Database: UniProt
Entry: A0A423VKV3_9PEZI
LinkDB: A0A423VKV3_9PEZI
Original site: A0A423VKV3_9PEZI 
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
//
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