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
//