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Database: UniProt
Entry: G4U7E0_NEUT9
LinkDB: G4U7E0_NEUT9
Original site: G4U7E0_NEUT9 
ID   G4U7E0_NEUT9            Unreviewed;      2484 AA.
AC   G4U7E0;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=NEUTE2DRAFT_98670 {ECO:0000313|EMBL:EGZ76638.1};
OS   Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ76638.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ76638.1, ECO:0000313|Proteomes:UP000008513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
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. ATM subfamily.
CC       {ECO:0000256|ARBA:ARBA00010769}.
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DR   EMBL; GL890999; EGZ76638.1; -; Genomic_DNA.
DR   STRING; 510952.G4U7E0; -.
DR   eggNOG; KOG0890; Eukaryota.
DR   HOGENOM; CLU_000178_4_1_1; -.
DR   Proteomes; UP000008513; Unassembled WGS sequence.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00892; PIKKc_ATR; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR012993; UME.
DR   PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR   PANTHER; PTHR11139:SF69; SERINE/THREONINE-PROTEIN KINASE ATR; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF08064; UME; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SMART; SM00802; UME; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Kinase {ECO:0000313|EMBL:EGZ76638.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW   Transferase {ECO:0000313|EMBL:EGZ76638.1}.
FT   DOMAIN          1468..2035
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2149..2468
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2452..2484
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1360..1387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2484 AA;  279658 MW;  BF707B64C2CC0590 CRC64;
     MASGVHGKTV KGGALEESFP EDAQPQPGSA PPQSTLAAEL VEGLPNESRR AKPDEVTEIK
     RLCTIIEQEK DKAGSDLEKT HEERLAYNHI LFYVCAGPVL DVVKTNDPFA DFASLQLKAQ
     NTLSLLKLAV QETPDVLKQT TDGNEFLLRG PEPLWLWFQP RLLALLGRSK LLGITSAIED
     FFHFTLQTVA ERVPLWDLGP GLLQYFQASL HAILEHFQSN PLADMNARNS NLDIQLPPDT
     FLRALDLDDP DTPSKFFYKI RDSEHAIRHA ISLFHILKST ILPVGAAEPP LLYRGNIAWL
     MDVFQPLFSV LVHWSPQLKI SLAPYVQTAI DLAEAADDTL RPKAISALAL ICGEVFDRSE
     QYLGEDEFGL ATRKALSLAL LHLVKEADSH RSLMQLFESR VVIPAVSFAT ASLPNSDLWV
     VSAETSFSQV PEELSSSKFV DVTLRQQVGL LGLDPVVDDG EPAPKRRKLV EHQTLSADIV
     EEICRVANLP ISEDICSLED SLIDAFPKLT ILRQCRVIEL ISFVPCATDN TLGLEEGRLG
     SLALSSASSE CSHCSIFGYS AFTQACDDAV TKTTAFKILE KLVKSPGFRD SRRPRVYAMV
     RLQRMLRHTV LPEFRDLEQS ILGQWCVQSL RSSIRELRIG AGRALPVLLD PDVPDFVRPI
     ARGNQNIVLD ILKLITDEDA LHLRETCILA WGQAGRVVSV DHLNLILIKL VEYLGYNNSV
     VSAMAVNEIL NIATYRGITP LQLFAPYWEN MAVLVVKDLV SAPQTTRLVA ETLQLSIKEL
     LCLLQKHALP WLVLAKNLGV IEKIAEARGE KSTSQPCIDS ANFPSIIALL LIQDVPDVEE
     HAMELLCVIS PKFKEPNPGE LNSDEKRPVS VRDRLAEILR VEPLGVLFEL FKASGGADER
     KKALIRKGIS ILATRSSPIT EKGAEPPHII ERFLEKYTLG LVSRLSERIT DIDVPIPDRR
     RCLRAMEEMI RVCRSSVTTA RSQISACLLS ALGCDELRSD AFSCWSVMIM NMDEMDVPNL
     LDTTLWVITH HWTCFDDSTK QQAQEVLDAL SKTNGHDLVK ATASMTTFNH LTDLAEHRKR
     LGLLSQSGLT RQDLFRTFCR RLRHDHPGVI EQALTELLEL LRQHQDYIQA SALAEQPKSF
     IPGLTRSVLD CAAKYNGWQP GIMRLCAECM GIIGCLDSNR MESNREQKRF VVSQNFMDFR
     ETADFVCFML ENVLVKAFLS TTDTKFLSFL SYAMQELLAK TGIKLAYQSQ GQGQHETLYK
     RWRSFNDITK EILTPFLTSE FIVSSGMIGL DTNYPIFHPQ KSYETWLKTF VLDLLRNPQN
     PNSAILFPPL CRLIKVHDPC VSEFLLPYVV LHAVIGSEGP SQTPNESQML VGEEGSTRAE
     AHEKKTNGSE WRKKVMSELK TILEYQPPET ATHSEKEEVK LCYEAVFRIL DYFKNWLHIK
     QSQSASKEKD ARWCPLVEEV LSSLDPELVA RRAIDCGQYA RALLFLEPHI ESRRDQAIGD
     EATRLMRSVH DIYTQIDDPD GLDGISACMK DLGFKEQALS HRKAGRWTAA QTWYEIQLAE
     SPDDVNLQLD LLTCLEESGQ YDNLLSFAEG IDKTPSSLSK VMPFVLEASW ATGRWQIMEK
     YLRSYTEGDV TDIFNIGVAD ALLCLKEGDG ERFQELLQAM RDKVASSMTL SATSSFRTCH
     DVMLKCHVLE DLEMIANAEP VEGEGHAPLM KALERRLEVL GAYVSDKQYV LGVRRAAMEL
     MRTKFGDEEI SSSWLATARL ARKSGSTHQS FNAVLRAQQL GDSSAVIEYA KLFYKDGQHR
     KAIQLLQRAI DDDLFNDGMM AIDTPTSSKN QQSHRNLLKA RAHLLLAKWL DSTGQTHAGA
     LRSKFQEAAK THPQWEKGHY YLGRHYKKVL ESEKALSPDD QSDAYLTGET AKLVIENYLR
     SLNFGTKYVH QTLPRILDLW LELGTQVDAP SLGMVTLSAE LQSRRRTILH ELYKHFNRHL
     PKMPAYIFYT ALPQIVARIA HPNQDVFRVL EQMIIKVVEA HPRQAIWSLF SFMTGRTNGA
     RRHRGQKVLD DLRAIAKRVD ETGYDLKQLL KMGEKLAEQL LLACNKGDFQ SNRTVKASIT
     RDLNFNHKCT PCPLVVPIET CLTATLPTLT DNTRKHKAFS GDVITIDRFL DDVLVLGSLA
     KPRKLTARGS NGQLYGLLIK PKDDLRTDQR LMEFNGLINR SLKRDTESSK RQLYIRTYAV
     TPLNEECGII EWVDGLKTLR DILLGIYKTR NITPNYGQIA ELMKQACTSD DNLHLWSRSV
     LGMFPDVLPE WFISQFPDPS AWFAARLRYT RSCAVMSMVG TILGLGDRHG ENVLLEEGNG
     GVFHVDFNCL FDKGLTFAQP EKVPFRLTHN MIAAMGIYRY EGPFRNCSEL TLKVLRQQEE
     TLMTILEAFI HDPTLDLQRT KKRTHDVVKL NPTSVVESIK RKVRGLLPHE KIPLGVEGQV
     EELIKQATDP KNLAAMYIGW CPFL
//
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