ID A0A1B8DE64_9PEZI Unreviewed; 2490 AA.
AC A0A1B8DE64;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=VE04_02388 {ECO:0000313|EMBL:OBT57197.1};
OS Pseudogymnoascus sp. 24MN13.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622150 {ECO:0000313|EMBL:OBT57197.1, ECO:0000313|Proteomes:UP000092157};
RN [1] {ECO:0000313|EMBL:OBT57197.1, ECO:0000313|Proteomes:UP000092157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24MN13 {ECO:0000313|EMBL:OBT57197.1,
RC ECO:0000313|Proteomes:UP000092157};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24MN13 {ECO:0000313|Proteomes:UP000092157};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV456061; OBT57197.1; -; Genomic_DNA.
DR STRING; 1622150.A0A1B8DE64; -.
DR Proteomes; UP000092157; 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; 1.25.10.10; Leucine-rich Repeat Variant; 1.
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; 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; 2.
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:UP000092157}.
FT DOMAIN 1466..2034
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2148..2457
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2458..2490
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2490 AA; 278205 MW; CD3BAFCE48112A96 CRC64;
MGNPSRMPLG QYATNGDSID TGLGAFEPPP STLAAKLVNK LSGSHKPSLQ GSQDSFGLLV
SEVSKFDKTR NEHTTPEEIR ENNYRVVYVL TKARLGPVCS DESDPFAKKE RVLDDAAQVL
DLFITSIKET PEILTKVGTQ NDLVRTGRGV PLWIWLWPRL LRLLGNEGCE PLWSKVKELF
HTAFDVSRAL DVEFWGVGLQ FLTYLRHCAD ASLHNVAAIS TSTIALPLAT IEDDLSFQSR
LGFVENGCTY NLRGGSDSFH HTQQLLTLVA ELSLSSFVDG QLYESTSHRY MAWVFDSFLE
LRTTAARSAA YKTEQDEIHS CSISVDAVHR LVSSQAQHID APAQRKGYRV LAHLCSELVA
YSTPFSDFVD RVKLAAILLD LASACEASGS VSQVVAINLL PVLDKAIVLA APTDADLKSC
ILLLRQKCQN IPPQSAPTAL ENKALELQFR SLCFKDLPSI GNDNDGGPQT KRRKIAPHSL
LEEITEEAYM LLGAQKATDL DGLSHIAADC FSHLEDTNRC KALKLLGMIP CASAHTLMVF
RDKNGEFGEP ECTVCGSSSK NEPTIDAASS RDVPAPVSTS VPVIAVQADP ILHQGPQSAD
MAKVEAQAVA ILSALLKVGD FELSRKPRIL AMLVVRKFAL HFEGAQFMDL ESSVLGQWCL
TSLRSSVREL RIAAGRTVPA FLRDGNNVDV EVMRRNRVNA INILRQFSGE TPPHLTETWV
LTWGQIARVS KDRELNLTLL RLVEYLGHTN QIISGLAFTE ILSTAEVHGI PVGQMFSPFW
RTIAHTAVSD LQNRPQTVQL MAELLSISVP EFLVETQAYT LPWLVLAKKT DIITKISQAR
EDDDPSKAII SNMVAIMPLL LVQAVPDIET FIMGLLRGVS TAFDKIDLVQ CLGIGAIEIA
VELLKNAGDE DDSKKSRVRH ALNILAAHCD IIPSDGEQSK DKIGAFLEQY SLGIMSHFSE
LVNDTRVWQS PNEKKRSLRG IEELVKVGKS HTRSALPQIH ACLQSALSND HLRTAAFQAW
GTMIRSFDDE EVSVMLETTF AIIIQHWQFF DSSTREYARK LIEYLLTKRF QTLGVNADLL
PSLAQIPELQ SCEERLVKMR SKPDVKQEYQ IFSRRISHEH ASVVTQGLTE LASYLNKNQE
FLQASAVSEQ PEKVVGELLR AILDACVQFN DSNTDVARLA GECLGMIGCI DSNRVETVRK
RKEIVVLSNF DGSADTTDFV LFILQEVLVK AFASATNPRA QGFFSYAMQE LLRRCDFSVV
VSQYRSHQID TGDAEKLHKK WLGLPESVQM TLSPFLSSKY TVTAMATNPV QYPIFQSTKS
YNVWLRAFVL DLLQKPQNAN ASLIFDPLSR VIRIQDTSVA NFLLPYTVLH SVALGSDQDR
SDILGEILAI LEHDTSTDSH NDLNNVKLCS EAIFRMLDYL ARWAQEEKAA LGLLSTRTNS
DTEEKSRRHL RLQLVAKLLS AIPAQIISRR AVECKSYARA LFHWEAHIRK VRKNNEPIPK
SMLLRLQDIY TQIDEPDGIE GISAHLYVLD IDQQVLGHRK AGRWTAAQSW YEIKLAENPS
DTEAQVNLLD CMKESGQYDA LLNYVEGIEQ SSSIVSKVLP FATEASWATS RWNMLEKYVA
KAPVEIAGDF NVNIGRVLLA FRDRDFNVFD AAIKSLREHI AGSLSADTTS SLESCHDSML
RLHVLTELDM IAHSSDDAPQ RQQVLSSLDR RLEVVGAYLN DKQYLLGLRR AAMQLSRDTF
TEANIASAWL TSARVARKGN SVHHSFNAVL HASKLGDDSA MIEHARLIWR EGHHRKAIQS
LQGAIDNNAF ISHNQAPSEL ETGQEGNRDQ QNLLAARAHL LLAKWQDDAG QTHSTALRSQ
YQFAAKLSMT WERGHYYLGR HYNKLLESEK TMASDQQIVP YLTGEMARLV IENYLRSLSY
GTKYVYQTLP RILTLWLDLG MQITQPVDAK YGTKEFAATL KIKQKEQIAS IHLRFDKYVQ
KMPAYIFYTA LPQIVARIAH PNQEVYQYLH QIIVKVVSTH PQQALWTLLA VTTSTQTERK
TRGASILQTL FSSSRKLSPA GVDLKSMIQK GQKLSQQLLV ACTAGDFPTN RTTFVSITKH
LGFNPKQCCP SPLAVPIESA LTATLPTLAD SVGSHKAFSR DVITIDGFAD EVMVLSSLQR
PRKLTTRGSD GKLYGLLCKP KDDLRKDQRL MEFNSMINRS LKRDAEASKR QLYIKTYAVT
PLNEECGIIE WVDGLKTLRD ILLGFYKSIG VAPNYTELRV LLKDASENDD KLFIFKDKIL
AQLPPVFHQW FVQQFPEPSS WFTARLKYTR SCAVMSMVGT ILGLGDRHGE NILFEEGNGG
TFHVDFNCLF DKGLTFQQPE RVPFRLTHNM VDAMGVYGYE GPFRPSAGIS LRLLRQHEET
LMTILEAFVY DPTLDLLESK NKKRRERDPA LQKVPNTPQG VLKSIRRKMR GLLEGDSVPL
GVEGQVDELI KQATSTKNLV GMYIGWCAFF
//
