ID A0A0G2HE73_9PEZI Unreviewed; 2451 AA.
AC A0A0G2HE73;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=UCDDA912_g06631 {ECO:0000313|EMBL:KKY33408.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY33408.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY33408.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY33408.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY33408.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY33408.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-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:KKY33408.1}.
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DR EMBL; LCUC01000246; KKY33408.1; -; Genomic_DNA.
DR STRING; 1214573.A0A0G2HE73; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000034680; 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:UP000034680};
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 1251..1848
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2023..2349
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2419..2451
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2451 AA; 277610 MW; ABB63E202C58F1FF CRC64;
MANQASRPLE IALENLDTLL REIKSRTISE DQRKRFARQL RDAIVERCHR ELAPENFAIL
SAQLQKAISN LIIHGNDTAE RLGGVYIVDT LVDFEGIDMA TKYTRFTQNL RQILRGKDIN
PMRPAAEVLG KLCRPGGSII SELVEAETKN ALEWLQSDRI EERRYSAVLV LRELARNAPT
LMYAYVGMVF DMLWAGLRDQ RHLIRATSAE CVSACFRIIR ERDQELKQIW MDKMYNEALQ
GLKAGSVESI HASLLVLKEL LEQGGMYMQD HYQEACDIVS RFKDHRDPTI RKTVVLLIPD
LANYAPSEFA STRLHGFMLH LSSMLKKEKE RNDAFLAIGN IANSVKSAIA PYLDGVLIYV
REGLSVQSRK RGSVDPVFDC ISRLAVAVGQ TLSKYMEALL APIFACELTP KLTQALVDMA
FYIPPVKATI QERLLDMLSK VLCGQPFKPL GAPQPNTLPS VPVIQKDPKD PLAYEHRKAE
IKLALNTLGS FDFSGHVLNE FVRDVAIKYV EDDDPEIREA AALTCCQLYV RDPIVNQTSY
HALAVVGEVI EKLLTVGVSD LDPTIRRTVL AALDERFDRH LSKAENIRTL FFALNDEYFP
IREVAISIIG RLARYNPAYV APSLRKTLIQ MLTELEFSNV ARNKEESAKL LSLLVQNAQE
IINPYVDSMV KVLLPKASDK SPSVAATILK ALGELCAVGG ESMLPYKDEL MPMIIEALQD
QSSAQKREAA LHTLGQLASN SGYVIEPYLD HPQLLELLQN IIRSEPQHGP LRQETIKLLG
ILGALDPYRY QQVEERTPEI SRRVESTAMT DVSLMMTGLT PSNKEYYPTV VINALLNILK
DHSLVSYHAQ VIDAIMNIFR TLGLECVSFL DRIIPAFLMV IRSTNGPRRE SYFNQLAMLV
SIVRQHIRNF LPEIVDLLQE FFPDKPPTLQ STILSLVEAI SRSLEGEFKV YLAGLLPMML
HVLEHETVPK RTASEKVLHA FLVFGSSAEE YMHLIIPVIV RTFEKPSNPT VLRRSAIETI
GKISRQVNLN DFAAKIIHPL TRVLQTNDMT LRMAAMDTLC ALIQQLGRDY LHFSHTVGKI
LRDNGIQHSN YDLLVNRLKE GGVLPQDLSS ETRFVDQVDE TPFADLGTKK LEMNAIHLKS
AWDTRGKSTK EDWQEWLRRF STTLLTESPN HALRACASLA SVYLPLAREL FNSAFVSCWS
ELYEQFQEEL ILNLENAIKS ENVTPDLLNL LLHLAEFMEH DDKALPIDIR VLGREAARCH
AYAKALHYKE LEFLQDQSSG AVEALIVINN QLQQSDAAIG ILRKAQLYKD GIQLRETWFE
KLERWEEALA FYNKREAEIP DDQAVPVEIV MGKMRCLHAL GEWDALGQLT GTTWANSSPE
VQRLIAPLAT TAAWGLGKWD SMDNYLQSLK RFSPDRAFFG AILALHRNQF REAAQNIEAA
REGLDTELSA LVSESYNRAY QVIVRVQMLA ELEEIIVYKQ TDAKKQATMR RTWEQRLKGC
QRNVDVWQRM LRLRALVITP TENMHMWIKF ANLCRKSGRM SLAEKSLKQL IGSDAPLESM
IPFWNDRSVR PNIPNQVVYA VLKYQWELGQ QATHKDTDVS EKALRCLRLF TAESAKAFEL
IRAGPMQSHQ ANGDNFHLSH SLGYPDSHGS HDAYLSQQRA TVDEAVLLAK CYLRQGEWMI
ALDTDNWQHT HVREILTCYS QATKYNSTWY KAWHAWALAN FEVVQALSSN GEGVPSRVDH
AVVANHIVPA VHGFFESISL SQGSSLQDTL RLLTLWLTHG GYSEVTSAVT EGFTHVSVDT
WLEVIPQLIA RINQPNKRVQ QSVHHLLADV GRAHPQALVY PLTVAMKSWQ GSRRSRSAAQ
IMDSMRQHSS KLVEQADTVS HELIRVAVLW HELWHEGLEE ASRLYFVVHN IEGMFAALEP
LHQLLDRGPE TLREISFVQT FGRDLTEARE WCRQYEVSHD VNDLNQAWDL YYQVYRRIYR
QLPQMTSLEL TYCSPKLMEA KDLDLAVPGT YKSGQPVVRI MSFDTTFSVI SSKQRPRKLN
INGSDGQSYT FLLKGHEDIR QDERVMQLFG LCNTLLANDS ECYKRHLNIQ RYPAIPLSHS
SGLLGWVPNS DTVHMLIREY RESRKILLNI EHRIMLQMAP DYDNLTLMQK VEVFGYALDN
TTGQDLYRVL WLKSKSSEAW LERRTNYTRS LGVMSMVGYI LGLGDRHPSN LMLDRITGKI
IHIDFGDCFE VAMKREKYPE RVPFRLTRML TYAMEVSNIE GSFRITCEHV MRVLRDNKES
VMAVLEAFIH DPLLTWRLTS AASPAGPNFT SEREQALVGA QAPRGRRASI LDADPAALRA
AQAAVSMTND NAMAGGPPRA RARTNSSAAP VVGSLGMNGA NGVNGQQNQD PTEIQNARAV
EVLDRVSQKL TGRDFKPGEE LDVLTQVDKL IVEATKLENL CQHYIGWCSF W
//
