ID A0A094DBB8_9PEZI Unreviewed; 2416 AA.
AC A0A094DBB8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=V497_02920 {ECO:0000313|EMBL:KFY61508.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY61508.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY61508.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 -!- 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}.
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:KFY61508.1}.
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DR EMBL; JPJZ01000715; KFY61508.1; -; Genomic_DNA.
DR STRING; 1420910.A0A094DBB8; -.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000029268; 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: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; IPR021133; HEAT_type_2.
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; PF13513; HEAT_EZ; 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; PS50077; HEAT_REPEAT; 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};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 700..732
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1240..1833
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2008..2325
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2384..2416
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2321..2356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2340..2356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2416 AA; 273265 MW; E912A7CA46BD3733 CRC64;
MSQQAVDLLN RLVGELRSRN DDARKRAAIE LQDLVVVTAR DFPQERFIEF YNVVNGKITQ
LISHGNDSND RLGGIMALDA LIDFNGVDSA QKTTRFAQSL RSVLRGKDLV AMQPAAVALG
RLCRPGGSLI SELVESEVKT ALEWLQSDRV EERRYSAVLI LRELGRNAQT LMYAYVQHVF
DLIWVGLRDI RLLIRETAAE AISAYFQIIR EREQARRLQW QSMIYEESRV GIKMGTVESI
HGSLLVIKEL LQQGGMFMHE HYPEACEIVF KMKDHREPVI RRTVVLLIPE LANYSPTDFA
QTYLHKFMVF LSGMLKKDKE RNDAFLAIGN IANAVKSAIA PYLDGVLIYV REGLSLKSRR
SGSVDPVFDC ISRLAAAVGQ TLSKYMEALL DPIFACELTP KLTQALVDMA FHIPPVTSII
QERLLDMLSN ILCGEPFKPL GAPTPNSIAA VPIVSKDSKD PLAYEHRQAE IKLALNTLGS
FDFSGHVLNE FVRDVAIKYV EDENPEIREA AALTCCQLYI RDPIVNQTSY HAIQVVNEVI
EKLLTVGVAD PDPHIRRTVL AALDERFDRH LAKSENIRTL FFALNDEVFA IREVAITIIG
RLTLVNPAYV VPSLRKVLIQ MLTELEFSDV ARNKEESAKL LSLLVQNSQR LIKPYVDPMI
SVLLPKARDP SPTVAATILK AIGELATVGG EDMIPYIDQL MPIILEALQD QSSSQKREAA
LKTLGQLASN SGYVIKPYMD YPQLLEILQS VIRGESQRGP LRQETIKLIG ILGALDPYKQ
QQVEEKSPEM QLRSESNQMT DISLMMTGLT PSNKEYYPTV VINALLQILK DQSLVQHHAV
VIEAIMNIFR TLGLECISFL DKIIPAFISV IRASPANRLE SYFNQLAILV TIVRQHIRNY
LPDIVEVLQE YWNVSPSLQA TILQLVEAIA RSLEGEFKIY LASLLPLMLG VLEKDASTRR
QPSEKVLHAF LVFGSSSEEY MHLIIPVIVK VFEKPQQPSF IRKSAIDAIG KISRQVNLND
YASKIIHPLA RVLGGSDPSL RLAALDTLCA LIFQLGRDYL HFVSTIKKVL VAHQITHQNY
DLLVIKLQKG EPLPQDLSPE ERYYSQIDEA PFSDISNKKL DSNPVHLKSA WDASGKSTKE
DWQEWMRRFS VTVLMESPNH ALRACASLAS TYPPLAKELF NSAFVSCWSD LFEQYQDDLI
QNIELAVKSP HITPDLLGIL LNLAEFMEHD DKALPIDIRI LGREAGRCHA YAKALHYKEL
EFLQDQSGGA VEALIQINNQ LQQYDAAIGI LRRAQLYADS IALRETWFEK LERWEEALDF
YKQREQDSTE PGERIEIIMG KMRCLHALGE WDELSALAQD TFHTSTLDVQ RRIAPLATSS
AWGLGKWDLM DDYLSVMKIQ SPDRSFFGAI LALHRNQFHE ASLYIQKARE GLDTELSALV
SESYNRAYAV VVRVQMLAEL EELIVYKQSN DNPAKQETMR RTWETRLLGC QRNVEVWQRM
LKLRALVISP KENMQMWIKF ANLCRKSGRM GLAEKSLQQL IGNDDSLDAV LPYLNAEGHG
QYHREPSRHI TPAVNYAVLK YHWAVGHKAA ALDGLKIFSN DMAERLHASQ MAAHGMQDGH
GVNDMANGLT AVNGNAAPYA MSPKALADHT ELLARCCLKQ GEWQVSLNRG DWRHDQVGDI
LAAYSAATQF NPNWYKAWHA WALANFEIAQ SVNQRPEREI AVVPHNVLID HVVPAVRGFF
KSISLSAGSS LQDTLRLLTL WFAHGGNPEV NAVVIEGFAS VSVDTWLEVI PQLIARINQP
NTRVRQSIHA LLADVGRAHP QALVYPLTVA MKSAQTTRRS RSAGQIMDSM RQHSAQLVDQ
ADVVSQELIR VAVLWHEQWH EGLEEASRLY FGANDIEGMF ATLTPLHEQL DKGPETLREI
SFAQTFGRDL QEAREWCYTY KQSRDVGDLN QAWDLYYQVF RRIARQLPQL TSLELAYVSP
KLLHVRELDL AVPGTYQSGK PIIRILSFDS TFSVINSKQR PRRLRMNGSD GIAYAFLLKG
HEDMRQDERV MQLFGLCNTL LSHDSESYKR HLNIERYPAI PLSQSSGLLG WVENSDTLHV
LIREYRESRK ILLNIEHRIM LQMAPDYDNL TLMQKVEVFG YALDNTTGQD LYRVLWLKSK
SSEAWLDRRT NYTRSLGVMS IVGYILGLGD RHPSNLMLDR ITGKIIHVDF GDCFEVAMHR
DKYPERVPFR LTRMLTYAME VSNIEGSFRI TCENVMRVVR DNKESLMAVL EAFIHDPLLN
WRLTGAHSPG EGPNFRSDRR GSIMAADQRR PSILDAHIPP SELVAQDPTT APGGPPSARP
RGRTNSTAVT EPGQDHTEIQ NERAVQVLNR VKEKLTGRDF KPDEELSYIN QVDKLLIEAT
KLENLCQHYI GWCSFW
//
