ID A0A0F8B2V5_CERFI Unreviewed; 1654 AA.
AC A0A0F8B2V5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=rad3 {ECO:0000313|EMBL:KKF95791.1};
GN ORFNames=CFO_g1846 {ECO:0000313|EMBL:KKF95791.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF95791.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF95791.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF95791.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-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 -!- 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:KKF95791.1}.
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DR EMBL; LBBL01000078; KKF95791.1; -; Genomic_DNA.
DR Proteomes; UP000034841; 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 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 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 Kinase {ECO:0000313|EMBL:KKF95791.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW Transferase {ECO:0000313|EMBL:KKF95791.1}.
FT DOMAIN 623..1205
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1318..1625
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1622..1654
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 1654 AA; 186532 MW; A230297CFAF38712 CRC64;
MFEPFWKYLS YVVVKNFAGE RRRCTKVAEL LGLDLIDLLV LVQRHALPWL VLESDIETIR
AIAAAMSKEV TPLLMSKGNL PPILALLMVN SVENTEAAAM SQLCRVGDEF KNSDLMALIR
SELVPTIHEL FKHAATRDDD KRRAVLCALK WCSVRLMSSR DPKRKSPDVI GYALEPHMLG
LVSSLTEVIN IAVTSQQVTV EQTQCIAAME EMIKICKSHV RTGRAQISAS LLSVMTMEEL
RRPALSAWAA MVLNLDEADA VLLLEPTYYV VIQYWIMFDA ASKTMAEKLI LDLYAKYPEM
FNDNIFKIPS LRHTPALAKL EDELGVIKKA ALEATSVKKM FSVYVERITH ENSECLGLIG
CLDSNRVEAN KEQRSIVVYN NFTKEHDKAE FGFFLLTEVL LKSFSSTTDT RMQGFLAYAM
QELLERCDIK ALVTGPGTRG GNDIAREWAL LPSGDKELLN TFMFSRYVLN SNIPPTAQMP
SFRPDGEYSQ WLKEMVFFLI QNPQNPNAAL IFEPLMRLVR VKDTSVAEHL LPYVFCHVVI
GCESSIYKKL NEELLAILEF DPTNIHSPEE KRHRNRYYES VFSILDYMMR WVHKKKVAPR
LDNAQTAELE RVQKFLDNIP PQLIAQRAIT CNQYNRALFH LELHIRETST KKGHIDGENK
EELMAQLQEV YAQIDEPDGL EGISAHFQVL DLEQQVLSNK KAQRWTAAQT WCEYRLSEEP
ENTDIQMELL TCLKNSGQYD VLLSYAESLR QHPALENKIS SFAVEAAWAT GRWEDLNKLV
RSYNGNILDD FNLSIGEIFR CLYNKEYESI PDTITMIREK ISAALTTTTT SSLQACRDLL
LQCHVLSDLE MILANKPKTP QETPPNNDAI MASLSRRVGV LGSFASDKHY VLGVQRAAMN
LMCDSYTNLN ISSLWLASGK MSRKAGLLQQ SFNSVLHASH LGDGSAIIEN AKLLYKEGHG
RRAIQILESA IAGNKLSAQS QQAQPSVKTS GTGSVTSSKG ADYAQKLLIA RAQLMIAKWL
DATGQTNVLA LREKFQEAAK TCQAWEKGHY WLGRHYKKLL EYESKLTPDE QTDATLMGTV
ARVVIENYLR SLNFGTKYLH QTLPRIITVW LEFAALFDES PTARAAMAHE LKRRRLAELN
AIHACIEKFT RRLPAYVFYT ALPQMVARIT HKNADAVKLL VNIIAKVVAS YPQQALWGIF
PLLMTPRNAE RSSRGKEILS VIRAADPKLD GRPVAEIIRK GEKLAAQLVW LSQTGDFQSN
RSTMTTLNQL KFNANACLPS PLVVPAESCL MAKLPTLPES SKRKHQPFSG DVVTIHSFEQ
EVLVLGSMAR PRRVIAIGSN GQKYKLLIKP KDDLRADQRL IEFNNVINKA LKKDPESSKR
QLYVRSYAVT PLAEEGGIIE WVDGLKTLRD ILLMLYKQRG LSAINYQQLE NLCKAAANDA
TLFTRDVLGK FPPVLHVWFI DNFPDPTSWF TARLRYTRSC AVMSMVGTIL GLGDRHGENI
LLEEGNGGVF HVDFNCLFDK GLTFSTPERV PFRLTHNMVA AMGIYGYEGP FRQCSELTLA
TLRAQKETLL TIIEAFIYDP TIDLLKDKGR RARPDGRVRM NPQSAHEGVK RRLLGFLPNE
LIPLGVEGQV DELIKQAVNP KNLAAMYIGW CSFL
//
