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Database: UniProt
Entry: A0A074WFU7_9PEZI
LinkDB: A0A074WFU7_9PEZI
Original site: A0A074WFU7_9PEZI 
ID   A0A074WFU7_9PEZI        Unreviewed;      1884 AA.
AC   A0A074WFU7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=M436DRAFT_53559 {ECO:0000313|EMBL:KEQ70449.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ70449.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ70449.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ70449.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584717; KEQ70449.1; -; Genomic_DNA.
DR   RefSeq; XP_013424549.1; XM_013569095.1.
DR   STRING; 1043004.A0A074WFU7; -.
DR   GeneID; 25411797; -.
DR   HOGENOM; CLU_000178_4_1_1; -.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000027730; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; IPR018936; PI3/4_kinase_CS.
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: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   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          862..1434
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          1549..1872
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          1852..1884
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   1884 AA;  210868 MW;  165D367F4618FE05 CRC64;
     MLTELFESQD LQLSDRNRVL AILAIRSIVL HNRNPNELEL GKSFLAESCL KYLHSSSREL
     RVAAGRTLAA FLREGLPTEI RNNNRQVALK FLRALSTKDI IGQHETLILA WGRVAVVCGE
     KELNLALLRL VDYLGHPNSL ICSLAYSELE DIAETLSFSP QTLLKPFYRS VAVAVIQDLT
     TKPQKAQQLS EFLGMSVSHF LLLTQRDTVP FLVLTKKKDI LQRIASARSA ETSIQDICLQ
     PPANLAAVIS TLLYQSSGDV EGNATRCLAE VAPGFQSNDL GSLVRSNPVL IACEMLKTAG
     DEDASNASKA HQAIQIFAML VEGKPTHSKP NAKTNRMIIS FFEAHILGIM TEFSNSIDNT
     LSLSPSEKLR CVKAIEQMII LAKSKVSVAL PQIRACLQSA IDQPQLQEAA LSAWLTLVQV
     LEGDDVADMV DHTFALVAQH WDGLSSVLQM KIHDTISGMV KTHSNVIREK LMTIPSLASI
     PLMSKIGLEI QRLKKDERPE VHLRAFAKRL HDENVAIVTQ GLRELVPWLG ENQGFVHEAA
     VSEQPKATIA NLMRALLDVC TRYADHDSTV VDLSAQCIGI IGCLDPNNVD MSSSKRQVLV
     LSNFEKATEV INWVAIMLED VLVPAFRSST NARDQSFLAY VMQELVRFCG FNEAATARLR
     PSQAGPAHNR WSEMTESVRN TLTPFLSSRY LLNSSSSVQP KKRSYPVFAI EKRHSTWLRE
     WAYDMLWRGK GDNAEMVFPI LARIITRHDI SIASFLLPYV ALNIVLGGTV QEAKDIGVEM
     LTVLSTESIV ESEKEALRQC SENVFAVLDY MSKWLQEKKR TMAAYRTAAL RAGHPPSELE
     EVKDVGQIES VESIIRSIPA DIIAQRAMEC GSYARALFHW ESYIRSESQR QTNQDAKEHD
     AMFQRLHSIY SQIDEPDGLD GISAHLNILS PEQQAFQHQR TGRWSAAQSW YEFELVKEPS
     NISRQIDLLS CLKESGQYDQ VLRYASFYNG NSSQGGKNTL LSYITEACWT TERFDTLKDA
     LSDLSEESQT DFNVGVARVL LAMQEKKQDA VSAMVNNLRN TVVKGITSVS ASSLQACHDV
     LLKLHIVYEI GALSGAVHVP VAQDPAASSI LAVMDKRLAV VGSYISDKQY LLGIRRAVMR
     LSSVDFSKVS IGSSWLTTAR LARKTNVSTV AHYAVLNAFN CGDDAAKIEH ARLLWKDDQH
     RQAIRSLEGA IASNTFATHD QKAIDTSNSD EAQQKQNMLS ARAHLLLAKW LDASGQTQAT
     KVVVKYQYAA RHYSRWEKGH YYLGKHYNML LDASKTLPAH KQSDPFVSGE LTKLVIENYL
     RSVPFGSKYW YQTIPKIITL WLDLGMDCIQ KTRNDAQSEV MVKRSSWLDA IHKQMKKYFD
     RIPPYIFYNA LPQMISRITH PNTKVYEVLS TIIQKIVTAH PSQALWFVLA VCKASAPDRA
     SRGVAIINKL KDPKNRPKNE SAGLDLRVMI THGQKLSDGL LQACEIHIET RSANVSLSKD
     LNFNHKLAPN PLVIPLESTL TANAPVVQDA FHIRKFVAFA QERITIQSFS DEVLVLNSLQ
     RPRKLTVRGS DGKQYGLLCK PKDDLRKDQR LMEFNTMINR ALKRDTESSK RRLYIKTYGV
     TPLSEESGTI EWVEGIKPLR DILLKLYQRK GVQPNYNELR VFLGEASANP ANVDIFTEKV
     LKVFPSILHE WFAEMFPEPD SWFAARLRYA RSAAVMSMVG HVLGLGDRHG ENILLQEDTG
     GVFHVDFNCL FDKGLTFEKP ELVPFRLTHN MIAAMGAYGY EGPFRKSAEL TLGLLRQHQD
     TLMNILETFL HDPTTDFIGK KKRTTVGVPE TPQEVLDSVS GKLKGFLRGE TVPLSVEGHV
     NALIGQATDP WNLCQMYIGW CAFL
//
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