ID A0A2C5ZIA9_9HYPO Unreviewed; 1989 AA.
AC A0A2C5ZIA9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=CDD80_5521 {ECO:0000313|EMBL:PHH79154.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH79154.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH79154.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH79154.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) 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 -!- 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}.
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:PHH79154.1}.
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DR EMBL; NJES01000055; PHH79154.1; -; Genomic_DNA.
DR STRING; 2004952.A0A2C5ZIA9; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000226431; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 CDD; cd00892; PIKKc_ATR; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic 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; IPR012993; UME.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF124; SERINE_THREONINE-PROTEIN KINASE MEC1; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000226431}.
FT DOMAIN 965..1537
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1651..1960
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1957..1989
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 1989 AA; 224401 MW; B3B6EFF2D037C7B8 CRC64;
MASLSSLVVD GAKRRKLSSK DSPSSMLEAI YEALQVKETG DDDVVVFEQL FLTGFETASE
DRQCLAVELL SRICCAADES FSMDPEARCL ICEGARDSGA LRPSSSKSEA RLVFCKLIRL
PKFLESQRPR VVAMIGLRRL VHHCEDGDFL DLERSGFGDV LIPGPGQWCL QSLNSSLREL
RVAAGRTLPT FMPQKPTPVL DEDLLHRNRK CSIAVLKKTS DQHQPRLVET RIMAWAQLGR
VATEDELNLV LIKLLEYLGS SNGLVSAFAF NELLRLAESR SITPRRLFEP FWKNMAYMAT
KNMVQRPQQS RAIAELLQIS VNELLLLIQS HALPWLVLDR QVDVIQKIAE ARKEKEPWRP
LMDNSNLAAT LALLLVQDAD NMESFTLSRL NDVSPHFHSL TLLDLFQADP VSIALELLRF
AAGADAARQQ VIHKALHLLA TTILRNNKDT KVKKSNVIGR FLQSHVLGLM AKLTDVINDS
VSTHPPVLEQ RSCVRTLEEL IKVSDEFQIS ACLLSAISQD ALREASLSCW VALLANFEEE
DVEMLIEPTF FIVRRYWAVF NRGTRRAAQE MLDFLLDKHA PIIMSYINKI PSLSPIAELA
DVESRLSALR PALATDEALR AFAERVAHHN SGVVHQALTE LVPYLRDNQS ALYTSAVSQR
PDSAVTSVLR ALLDCASKYN GVQLDMSRLC VECVGLIGCL DSNRIESVRE HRSIVVLDNF
EGVGEATDFG LFLLQEVLVP SFLSATDTKL QGFLSFAMQE LLIRCDIKAA CAMQNTGMRG
GNDVYRKWIA LPEYTREIVT PFLTSRYMVE RMEKVIVEYP IFHLGKPYGN WLRLFVVDLL
RNGQNEHADT LFEPLTRVIR VKDLSTAEFL LPYLVLHVLV GPRSSKEDRE RVVGELLVVL
RYNPAETASY LEKEEMKKFC HAVFRVIDYA MRWIQAKRSK GRLSSVDKEN LSRIQGILDE
IPAELIAQRA LECNEYARAL FHLEQHAQKL ELKSEREPDD RIKLLERLQH IYANIDEPDG
LEGISAHLPA LDIKQQILTH KKAGRWTAAQ TWYEMELAEK PDNADLQIEL LRCFQQAGQH
TRLLNYVESL RTEGSNNKVT PFAVEAAWVT GQWESLSKFT GRFHGDVVQD FNMSMATLLD
ALHNKSSSDV LSQIVGSARE KIASEMTASA TMSLQAAHQL LLRCHVLTDL EIIVNLKPGD
EEERRKTKSL LDGRLEVIGA YVNDKQYLLG IRRAAMELLR PSYTDADVSS LWVASARLAR
KTGSLHQSFN AVLQASRLGD DAATIENAKL LWRDSHHRQA IQMLQGAIER NNLTTQGGTA
SSVNTNVAAS TKLTLPQKLV AARAQLLLAK WLDAAGQSHA SALREKYQQP PRTHHAWEKG
HFYLGRHYKK IFDSERPLKV SDQSENYITG EVTRLVIENY LRSLNVGTKY LYQTLPRVLT
LWLEMGTLPD KPLEGKASLS RDTHRKRVEQ LNLLHAFLDR YIHRLPAYVF YTALPQIVAR
IAHPNVSVFE RLTRIIVKVV EAYPRQALWS LIGIMTSKQV TERKARGTQI LQALRTVSKR
VEGTSYDLKQ LLRAGEKLAD QLLIACNNGD FSGNKSVQAS LSRDLRFQHK CTPCPLVVPV
ESSLNATLPA VSEHVKKHTA FSRDVVTIDC FLDEVLVLSS LAKPRRLTAR GSDGKCYMLL
IKPKDDLRTD QRLMEFNGII NRALKHDAES SRRQLYIRTY AVVPLNEECG VIEWVPGIRT
MRDILLNLYA SRRIQPDYAA LKSLMEEAST SEAKVRIFTD DVLGRFPAVL PVWFLQQFPS
PSAWFTARLR YTRSCAVMSM VGTILGLGDR HGENVTLEEG NGGVFHVDFN CLFDKGLTFQ
KPERVPFRLT HNMVAAMGVY GYEGPFRKSS ELTLSMLRQQ EETLMAILEA FIYDPTLDLQ
KEKRHSRRGD SGVKLQPQSV VDSIRRKVRG LLPNESIPLS VEGQVEELIK QAVDARNLTA
MYIGWCPFL
//
