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Database: UniProt
Entry: A0A0D1XZC7_9PEZI
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ID   A0A0D1XZC7_9PEZI        Unreviewed;      2454 AA.
AC   A0A0D1XZC7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, 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=PV09_01097 {ECO:0000313|EMBL:KIW08166.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW08166.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIW08166.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW08166.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-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-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; KN847531; KIW08166.1; -; Genomic_DNA.
DR   RefSeq; XP_016218035.1; XM_016353940.1.
DR   STRING; 253628.A0A0D1XZC7; -.
DR   GeneID; 27309070; -.
DR   VEuPathDB; FungiDB:PV09_01097; -.
DR   HOGENOM; CLU_000178_4_1_1; -.
DR   InParanoid; A0A0D1XZC7; -.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000053259; Unassembled WGS sequence.
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: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; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053259}.
FT   DOMAIN          1432..2006
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2117..2427
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2422..2454
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
FT   REGION          36..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2454 AA;  275354 MW;  4F5D681DE0D9AA35 CRC64;
     MKTRLSASTH YLTFHPSGAF YEWDFICSNE QRMASRSRNL RSTQNGQSGS MQSTNGNYLP
     PSTIAAQIVH NRSTVARSEP ENKALFGKLL QEYLRDPIVE DSSIETHAQL VQVVAEAGLD
     VLLSDDPFAL DSLVQQARDS LLVIRLTIIR KPDVLFYKGE GEEERPPLLL WLLAKILNLS
     GRRTLSLIQM DLRELLQSIF AVLSTKNRTL SCSFDFKMLL TDVVEDLLNT LERRQYEDDS
     DKPPIRAVVP SPNAMTRLWT PAGSLLVLPT GYQAVIRDPI QAQVLIMDIV AVLSHCSTGH
     SSDSFMSNSD ETLQFDCCHR ILDFCATAPS TTNEDHDRVF DSVASFLLSK IQKRCPRRKI
     HPAVDLLVHL LDHLRPQRYP NFSKTVLEAI EQLLQRCSSQ PNHAGLLQRN LLPVLQHIAH
     DFSQDVDDEF SAHVAGIIAR LTKTTAYLDG SSPPTKKLRL STIRSDIYED YRKGIAKEIN
     NLLFDIHETD FPILDENALQ RLREFDDAKR ATIIGCLGRL ACASAGSSAL ELDGSASSRC
     KICDSMAAPA ERAGVDAKIT KRAEESSIHL LSFMALCIED SSLCRSKIFR VAVANSIRQI
     SNHLDDSECS VLSWKGIGPW LMRSLQSSVR ELRIASAEAL VAYSRESLSE PVRSRNRLDT
     LDFFKCLADK NNLTDQETLT FAWGLIGRTC GDAELNLALI QLVDYLGHSH SLVSGAAYQE
     LLQLADSREC SPSELLRPYW SSLAMHVVKD IYACPQKVQQ LSELLGITVN ELLIQTQADT
     VPFLVLTRKK DVLLRIAQAR GPSINVQDLW LQPSKNLAAV LALLLIQPSE DPEQAAIALL
     KDASPAFAEE DLSALVKAES IPIACEILKH AADLPDVRKP QAHQGMRLLA CINEKKSTSR
     SSSKSGKHLS AFLDAHILGI MSHFTDIIDA PLQRQPMVEK HRALRAVQQL IILGDVQVSI
     VIPQIRATLQ SASKIPALVD QAFLTWAALV AAAGEDEIEL LIDQTFAMIA HHWNGYTSST
     QRRAYDTIAG LLKNHNAMVR DRIQMLPSLA GIEMLSKFES EIARLKATLD PILHFEAYAQ
     RCSDENSIIV LRALVDLGPF LEQHQKIIHE SAVSQQPSPV IARLSRALLD AVVRFKESDS
     TIPELAAKCL GAIGSIDPNK VDHMRERHEL LMLSNFGKAS EVVDFVAVML ERVIVDAFHS
     APTGRAQTYL AYTMQELLKF CDFRTAVYRP RSSQSGPKFQ RWMQIPESVR STLTPFFNTK
     YVLVHPSLPG DHDSFPILKP GMVHGTWLRT FVFSLLHKGT TENAQMVFPV LSRIIWGHDI
     SIPTFLLPFV VLNVVVGGND DDVRAINAEF LRVLSIDIDA IDASSAEEVK HCSENIFQVL
     DYLSRWLQVK KKLLGEFGGG RSVQVPNDYD EVTETSHISS VEAVLSSIPA DVISQRAVHC
     RSFARALFHW EQHIRQLADK AALKREDIEL DQQLRHLQHI YAQIDEPDAV EGMSTRLQIL
     DPEQQILEHK RAGRWTTAQT WFELSLIERP NDRGLQMELL SCLRSSNRYG SLLDTAQRLT
     VEHPDSIAQV LPFAVEAAWT TGKWESLERF LSSDAAKDVR DFNTEVGRLF LCLLKKDVSG
     FERLLSTLRA SIASAFSLST TSSLGTAHTH TIKLHALYEL EQIGALKDRV ITPDQLVDRL
     SKRLDILGAY TADKQYLLGI RRAAMQLSAM GFSKQQIGAN WLTSARLSRK AGLRDAAYDA
     VLHSTNLHDG AAMIEHSRLL WQDGHHRKAI QNLQSAIESN VFQSYTTSMI DDQSLTTDEG
     HSNKNQNFLV AKTQLLLAKW MDRSGHSKSE ELRAHFLQAC KSFSRWEKGH YYMGKHYLKI
     LESEKALPRA KQTDIYLTGD VQKLVIENFM RSMVFGAKYY YETVPKMLTL WLDLAADIYN
     AERNPRTLDQ QYHSLRVRKL EVVHKQVKKY VDRLPSYVFY TALPQVTSRI NHPHAKANEI
     LLHLIHKVIS IHPQQSLWSI LAVAKSRASD KSSKAGLVLQ QLRRTRSETS AVDVKLLIAH
     GEKLTNALLA ACEVTVESRS SRASLSRDLG FNHKLAPCQL VVPVEKALSA NLPTGIGGPC
     VRNHKAFPRN PITISSFLDD VLVLSSLQRP KKLTMRGSDG VNYGLLCKPK DDLRKDQRLM
     EFTTMIDRGL KRDVESSKRR LYIHTYAVTP LNEECGAIEW VDGLKPMRDI ILANYKTKGL
     RPDYGELRQL LDRACADPEK GSWKIFPEQI VPKFPAVLHE WFIDTFPEPD SWFTARLRYT
     RSCAVMSMVG NALGLGDRHG ENILLEEGNG GCFHVDFNCL FDKGLTFEKP ELVPFRLTHN
     MIDAFGVYGY EGPFRVASEL TLKILKQYED TLMTIMETFV YDPTTDFISK PKKRVVGVPE
     TPAEVLESVK AKINRLLPGE TVPLSVDGYA DALIRMATDP KRLAGMYIGW CAFF
//
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