ID A0A420HBV0_9PEZI Unreviewed; 2811 AA.
AC A0A420HBV0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Serine/threonine-protein kinase Tel1 {ECO:0000256|ARBA:ARBA00014619, ECO:0000256|RuleBase:RU365027};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|RuleBase:RU365027};
GN ORFNames=GcM3_205008 {ECO:0000313|EMBL:RKF54926.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF54926.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF54926.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF54926.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(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 ECO:0000256|RuleBase:RU365027}.
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 ECO:0000256|RuleBase:RU365027};
CC -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|RuleBase:RU365027}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365027}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769, ECO:0000256|RuleBase:RU365027}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKF54926.1}.
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DR EMBL; MCBQ01020571; RKF54926.1; -; Genomic_DNA.
DR STRING; 62708.A0A420HBV0; -.
DR Proteomes; UP000283383; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038980; ATM_plant.
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; IPR014009; PIK_FAT.
DR InterPro; IPR021668; TAN.
DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF11640; TAN; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01342; TAN; 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, ECO:0000256|RuleBase:RU365027};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365027}; Chromosome {ECO:0000256|RuleBase:RU365027};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365027};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365027};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365027};
KW Reference proteome {ECO:0000313|Proteomes:UP000283383};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU365027}; Telomere {ECO:0000256|RuleBase:RU365027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365027}.
FT DOMAIN 1859..2467
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2529..2811
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2779..2811
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2811 AA; 318664 MW; 14F9E794C7348502 CRC64;
MSSDGSDFQL DAILASITST KQKDRHEGLN HLKNFFEKPR KTTLSTFNDK TFHKIFFVLF
KTTLSEKQAF LRNKKSAKQL EICAEIMRLV VIAAIPTIKP KTVHKLVEHL TQVLTPFEGI
ISHQPLIKNY VKSLRIIFQH PPHLEPLKTN KWLDVVDICI EGICHAISVD EQESLTVTSK
SSTSSLSYGS ATKSQAELNK CTHQAILIRH IIEELFQILF LLISTPNSPI SERYVIISDT
LVQFLQSKTP STNKTNQLAF ATINVILRFT RIESISHSKS ITRSVIPLIS RFLHGKFVFK
DEMLKFLRDE MLTFICLVHP YLESMVVDKK YHDLLPEVIG LLEAMRLDYS KRSDRDQLQL
DDLEITENNV INGSFFNLRN LRLRTINHQA EQNWAFLKTI GVLERLISLV YEHNSMDYNQ
NHEHPVKRQR ICEVSDRLVE SINNDDSRIK LAGLQLLPFI LENLEISHFR LKILLSHIHI
CTNSKNDKTI TWALLAVASC SFQHEAPKIE SSEWMKFWLV GTRSLIHPST CRSASTVLHA
LLKNKLVQHD EVGEVIHSVI NAAETSGPAS ISDASIYFMA YLLRTRAIEV PNASTIAAQQ
VIRWLFGRWK PADRYYAMHN SAHTQPKHVL LLLETCLGLD KKEVPTSTLS CGPVAQEWQN
CLANIRTTHY LLLIDVPSQT SKVTEINPPF SSFLFSLDSK ASIFATSRFQ STRKLILDQL
YSTCIGVLDG WRTYKTDHPS NIPKEMFCSV IYNCIVTLLI LNPTMVFESD RYQNLMLKTL
ELAKELVNTI SIHQNTNQRD AETLTETLIQ AIHPYLPSCG LHMCSSLAKD TPHLLQFFVL
IADTLEENRK VQNLSQYTNS DVMELDDDFL FTPDRQNFLS RPNISNMPRS YLAFKFWQGS
FEILVYGKLF LLATINATPN FDGVLPTAFI DYLLSLNDEE FLSCQKLIVE ILASDIIIDD
AGSQGIIERI GYILSCDLLD RCEVTLVLSA EILAALKPFH FSSTQSGVAE QALQIYQWLV
STVIGKNLAS AEVQKSISIL LIFVLRSSNP GYGESESTLS ARSCFFDILR NSTLEVRFFI
ADKINTIFEI STIKDYDSIF IDILEILPTN ADWFEGICFR IFVLAKLGST LPTLRRRCLY
YIFEIPTKTN ETSPHATHCL KEFSSSLGIS TAQVLFKAYA SQLLYTWLEH EDFKEIPYHI
FGFNSLRDLA QIIKHEATAL MKMRDQEDSI RQLASILCSD EKQLIQDSFT KVMAYCTAYD
ISNPRRTCKY SSESRVKKCL GDDLFYKCIE NHFAEIIAVF FNCLDQEQTA KAFFLKTPGL
EYAGRIIERI DSFSSSEVVL PTNQQPLFKV KYLVAEIQQL CSHTRHTFEN LFTPAMLTSL
VRSLLKTSVD VIGSLHACSV LRKIKVLISL SGKVAIMGYP LEMLLHSLRF FLPKIECFDD
TIGMIQYLLD AGAPFLVDNP GFVSGISLSI LGSVKLVKTS NFGKLHENLH QSTKSKTQNF
HAWIGNYLEN YNSPLLSDQQ KKDFRSLTSY ALEVKSVGNA NSESPESGLL LGLLLDEGSD
KKILNSKSRE IALSILIKEF RGPTSCNIDV CGDDERSLIY APAILRSYRL SSAKEFQVWS
AKVVGRAYAS SGYIHEEFVR ESKIIKTRDS AEPNEGLEGS ISALLILLKD LTTSHDLKVI
GVAESAFRYI VTNANKELTE ICKRVLPKTL LVASTWDPYQ LPPSETLDST GLTSDVEEFI
SIHKTLREGW LHDFSVALVT SAPKETLLTA LRKILSEVSG FSDRAFPYII HLILSSHYRG
GLYKQEISSA YNAWLENPTI KKSHKKMLLE SILYLRTKIL PGEKSPADRA YWLDIDYLKA
CSAAIFCGMF KTALLFIEES CSLLTKPLRR SSTTIKDYIP PVELHANILL QIYKNIDDLD
LYYGIKQKPD WNNLLGRLEY EKDGFKSLAF KGAKFDSHIR RGSTTSTSDV QSMVKAFDVL
GLSGVSNSLL QAHQNICLSA SSIDSLFRTS RKLEQWDIPV PNAYSSNSTT IYKVFQTINT
ALNHDSVKKG IDEGLIFVMD TIIEKELSTT DLHEALQTLA ALVEIDEVFG SCGSYEFENV
FARFRGRTKW MKVGNPNDVI PILSCRRTSL SILSQRQNLQ EMMKIKALDS RLIEVQTALL
SSKIIRAYNN LQESLTVTTS LIDLIKPCHD VGLHVEAAIY LESAKTLWDQ GEASSSIGML
QALDDIKLLK NQSIVVDRSS LLSKIGHQIS VAKLEKADII IEKYLTPALE ELNDQFKGNE
AGQVLHQFAS FCDQQLQDVD SLEDLERVKK LSKAKAEEVK HYDKLIANAQ SLESKREYVS
RQIKAKAWLM IDERDLRRQI AIREELLSHC LENYLLSLVS SENHNRDALR FLALWLEHSR
QHVANHAVAK HIKKVPSMKF ASLMNQLTSR LQDTNEEFQE LLFQLIMQIC TDHPYHGMYQ
IFAGAYSNAN EKDETAVSRK NATKTLAHRF YDMPTSKNIW LAISTVSRAY CSLAAEKSSR
YKAGKNFQLN DSTAAMTLNT VIKKYPLPSS TRKIPFSVTL DYSDAIMEQV FEQVNELLNT
NRSTQQRRLK IRTYKVLPLT NVAGIIEFVP DTMPLHEYII PAHERFYPKD LKASRCRSEI
AAVQTKGPDV RIKVFKAVID RFHPVMRYFF TENFFDPDEW FFKRLAYVRS TAAISILGHI
LGIGDRHAHN ILLDRKSGEI VHIDLGIAFE MGRILPIPET VPFRLTRDII DVRTSEKKLI
NEPGEAARAL TGVNKKLTKT LSVYATVNDL INQASDEKNL ALLFAGWAAY A
//
