ID A0A1B8DXA9_9PEZI Unreviewed; 2493 AA.
AC A0A1B8DXA9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=VE03_06954 {ECO:0000313|EMBL:OBT63761.1};
OS Pseudogymnoascus sp. 23342-1-I1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1524831 {ECO:0000313|EMBL:OBT63761.1, ECO:0000313|Proteomes:UP000091879};
RN [1] {ECO:0000313|EMBL:OBT63761.1, ECO:0000313|Proteomes:UP000091879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23342-1-I1 {ECO:0000313|EMBL:OBT63761.1,
RC ECO:0000313|Proteomes:UP000091879};
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:UP000091879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23342-1-I1 {ECO:0000313|Proteomes:UP000091879};
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}.
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DR EMBL; KV455020; OBT63761.1; -; Genomic_DNA.
DR STRING; 1524831.A0A1B8DXA9; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000091879; 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:UP000091879}.
FT DOMAIN 1470..2038
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2152..2460
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2461..2493
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2493 AA; 278533 MW; D8F9116B3FEF6AF7 CRC64;
MGNPSRMPPG QQATNGDSMD TGPGAFEPPP STLAAKLVNK LSGNHKPSLQ GSQDSFGLLV
SEVSKFDKTR NEHTTPEEIT ENNYRVVYVL TKARLGPVCS DESDPFAKKE RVLDDAAQVL
DLFITSIKET PEILTKVGAQ NDLVRTGRGV PLWIWLWPRL LRLLGNEGCE QLWPKVKELF
HTAFDLSRAL AVEFGGVGLQ FLSYLRHCAD ASLHNVGAVS ASTITLPLAT IEEDISLPSQ
LGFVENGCTY NLRGGSDSFH HTQQLLTLVA DLSLSSFVDG QLHESISHRY MAWVFDSFLE
LRTAAARSVA FKTEQDEIYS CSISVDAVHR LVSSQGHPPH APAHRKGYRV LTHLCSELVA
YSTPFSDVID RVKLAAILLD LASACEASGS ISQAVAINLL PVLDKTILLG SQIVEPGDTD
LKSCILLLRQ KCQNIPPQIV PTALENKALE LQFQSLCFKD LPSVDNDNDG SPQTKRRKIA
PRSLLEEITE EAYMLLGAQK ATDLDGLSHI AADCFSHLED ANRCKALKLL GMIPCASADT
LRVLRDKNGE FGEPECTICG SRSKTEAIID ASSSRAAPTP VSASVPVNAM KASTITHLGA
QSADMAKMET QAVAVLSALL KVADFELSRK PRILAMMVVR KFALHFEGAQ FMDLESSALG
QWCLTSLRSS VRELRIVAGR TVPAFLRDGN SVDVEVTRRN RVNAINILRQ FSGETAPHLA
ETWVLTWGQI ARVSKDRELN LTLLRLVEYL GHTNQIVSGL AFTEILSTAE AHGIPVGQMF
SPFWRTIAHT AVSDLQNRPQ TVQLMAELLS ISVPEFLVET QAYTLPWLVL AKKTDIITKI
SQAREDDDPS KAIISNMVAI MPLLLVQAVP DIEAFIMGLL RGVSLAFDKI DLVQCLGIGA
IEIAVELLKN AGDEDDSKKS RVRHALNILA AHCDIIPSDG EQRKDKIGAF LEQYSLGIMS
HFSELVNDTR IWQSPNEKKR SLRGIEELVK VGKSHTRSAL PQIHACLQSA LSNDHLRTAA
FQAWGTMIRS FDDEEVSVML ETTFAIIIQH WPLFDTSTRE YARKLIEYLL TKRFQTLGVN
ADLLPSLAQI PELESCEERL VKMRSKPDVK QEYQIFSRRI SHEHASVVTQ GLAELANYLK
KNQEFLQASA VSEQPEKVVG ELLRAILDAC VQFNDSNKDV ARLAGECLGM IGCVDSNRVE
TVRKRKEIVV LSNFDGSADT TDFVLFILQE VLVKAFASAT NPRAQGFFSY AMQELLRRCD
FSVVVSQYRS HQIDTGDAEK LHKKWLGLPE SVQMTLSPFL SSKYTVTAMA TNPVQYPIFQ
STKSYNIWLR AFVLDLLQKP HNANASLIFD PLSRVIRIQD TSVANFLLPY TVLHSVALGS
DQDRRNILGE ILAILEHDTS TDSHNELNNV KLCSEAVFRV LDYLARWAQE EKATLSLLST
RSNADTEDKS RRHLRLDLVA KLLSAIPAQI ISRRAVECKS YARALFHWEA HIRKVRKKNE
PIPKSMLLRL QDIYTQIDEP DGIEGISAHL YVLDIDQQVL GHRKAGRWTA AQSWYEIKLA
ENPSDTEAQV NLLDCMKESG QYDALLNYVE GIEQSSSIVP KVLPFATEAS WATSRWNMLE
KYVAKAPVEI AGDFNVNIGR VLLAFRDRDF NVFDAAIKSL REHIASSLSA DTTSSLGSCH
DSMLRLHVLT ELDMIAHSSD DASQRQQVLF SLDRRLEVVG AYLNDKQYLL SLRRAAMQLS
RNTFTEANIA SAWLTSARVA RKGNSVHHSF NAVLHASKLG DDSAMIEHAR LIWREGHHRK
AIQSLQGAID NNAFISHNQA PSELETGQEG NRDQQNLLAA RAHLLLAKWQ DDAGQTHSTA
LRSQYQFAAK LSMTWERGHY YLGRHYNKLL ESEKTMTSEQ QILSYLTGEM ARLVIENYLR
SLSYGTKYVY QTLPRILTLW LDLGMQITQP VDAKYGTKEF AATLKLKQKE QIGSIHHRFD
KYIQKMPAYM FYTALPQIVA RIAHPDQEVY QYLHQIIVKV VSTHPQQALW TLLAVTTSTQ
TERKTRGASI LQTLFSSSRK LSPAGVDLKS MIQKGQKLSQ QLLVACTAGD FPTNRTTFVS
ITKHLGFNPK QCCPSPLAVP IESALTATLP TLADSVGSHK AFSRDVITID GFADEVMVLS
SLQRPRKLTT RGSDGKLYGL LCKPKDDLRK DQRLMEFNSM INRSLKRDAE ASKRQLYIKT
YAVTPLNEEC GIIEWVDGLK TLRDILLGFY KSIGVAPNYT ELRILLKDAN DNDDRLFLFK
DKILAQLPPV FHHWFVQQFP EPSSWFTARL KYTRSCAVMS MVGTILGLGD RHGENILFEE
GNGGTFHVDF NCLFDKGLTF QQPEKVPFRL THNMVDAMGV YGYEGPFRTS SEISLRLLRQ
HEETLMTILE AFVYDPTLDL LENKNKKRRE RDSSQKVPNT PQGVLKSIRR KMRGLLEGDS
VPLGVEGQVD ELIKQATSTK NLVGMYIGWC AFF
//
