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
//