ID A0A0D2D6J7_9EURO Unreviewed; 2920 AA.
AC A0A0D2D6J7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=PV06_08661 {ECO:0000313|EMBL:KIW38823.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW38823.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW38823.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW38823.1,
RC ECO:0000313|Proteomes:UP000053342};
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 Exophiala oligosperma CBS72588.";
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 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}.
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DR EMBL; KN847340; KIW38823.1; -; Genomic_DNA.
DR RefSeq; XP_016259039.1; XM_016410017.1.
DR STRING; 215243.A0A0D2D6J7; -.
DR GeneID; 27360735; -.
DR VEuPathDB; FungiDB:PV06_08661; -.
DR HOGENOM; CLU_000178_8_2_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000053342; 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:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
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; IPR044107; PIKKc_ATM.
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; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053342};
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 1834..2438
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2546..2857
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2888..2920
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 744..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2283..2310
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2920 AA; 327284 MW; 9F47557724D0E323 CRC64;
MAEVKLIVAA IGKLEADTQR VRTEGLEALK SALCQGRTTS RINVLEDDVF HKIFELLYTI
IAREKSAFTR AVKPTTKNNA ASRLEVAAAA FRLVVEAGSS NVSFKTALSV LDHVVDTLPL
SDGSFCKPLK TDYLKAFRSI LEYSPHAEHM RPKNWQGYVD FVLEALSLGL EDDQVDDDLV
TSRETSMASR SGLQLSIRHS QRSRRTLGKD IASYVEDLAV ALKGLTSVTN APVPTRSAAI
AEVLISLLNS TTRGQEPLFE ILNNIIFVSL TENVALIRSM LMELIPIIRR LWVSKSSLLR
EQMLITLFTC RYFFLSTSEP WPHVGVDRIE ALMRTILSEY HHRNEREILH FDDMRPDAEG
SDQPLRLRQF LPLRESSRAL SCFMTLSVVS CLILGLVASG KSMRPEQYSE DTSRKRQKTQ
SPFDEVLQSA AVSPGQERLV SLQILLFLLD QPHTLDEKLF VGVSKLIPAL THEDGNVQTW
TFLIFSRVLV SPQSTTSSSI DWLRVYEAAQ GALSIPAAAR AACQLLNVIL ETEVLGSALT
GASLHNAVFG GSNNGPCLFT DTALTLLTTA LGSGLFETGK LFEDFCLKTL SWLTARWTLP
PTLDRLSNSQ IAFHGRPSLL YLLLTSMCGS YDRPLPREDW SPSHPLWRAS LIPFDDLDFL
RYLLCLPPHE PKGAQTLGHG SPQIDSVTAS HTTKAVIDFL NGRLSDFMCS WESIRSERGF
NITSDIATIL AVASTVATGV WTKTGKHSQS AQQDPSHAKS RDTIEAFTRD QSEDMRRLVT
GRFCESTLQI YDKIVQSDDE AAPEAYQPVI ELALRLTSLV TDQDTTSSDS KNLSDFEIMD
IDTWDSQSSQ RGQHNVSSAM RIDLPLCSDT SSLLTRNKVE LITALQVIKS SRSLDPETAS
VVVDQILSLD PDSLLAARGA VKDFFGLNPG VTRIDAHRLL GDLAKRYMQD YRFERCEAAL
CFCLSTMQSL SRLWTTREET DDLRETALDI YDWFLNTALG KQIASRRVLL HITNLLDSLM
RQNASFDEEE LPSPRTSLLH ILKAGNVTTK YGLGKKLTRI FEKYVLSQHE AIFDDIVENL
PSDPDNKEGI AVRLHVIAQL GAHWHTVLRQ ATYHTFETVA NVPSTMPMAT ACIAEMCTTL
GLKSPRVLFG LFAPQIFYTW LSRGSLAQIP YLAFSYISLK ELALDNIAEL VGQIALRGSS
HAEELAVLVE QEWLSLLSDH FPYAEAYTLA SETSVPKQER IYDGSEKLIR KQLGSESYLR
LLRYNLPEIV ARLVITLQDD RAIDKSFEKN DETSALCAWQ EMASMSDSNT QIPLSQQPSF
RARCLLDELN YLYQRLDIQS TDVWTSALLI HVYRQLLERI YPALGSLHVC SIIRKIRIAV
SLAGPVALEG YPLEMILHNL RPYLTMFECA EDTMAIYQYL LKAGKAYLNK NPSFIAGLGV
AIFTSLIGFM GSSQDSTTQE IHFVSTMNKA QAFRSYLGDY LDSMSLAEGT EKARSTFQSL
VQHAKAITSS GNSSKSSSEG SLLQVLLADR ASEEPLLTNI HFDIAIGILC QHFQPATSRS
DDILEDDLQA AQFSPILGTI VKRINLNQPF RIWTAEIIGR GHIMRGLRFN ARREKSIEYP
SDVTQVEPDQ DAIHSYTSIV EFLLDLIWGS DFTASAYAEK TLQLIFSGMP DRSQDDVLQQ
KVERDLIHQL KYKHFPCPAI PLPQPSILTA ERLPSSTHEN GSWASDIVAE ISDSAAHDPV
LSFLKPIALA LSGSADILLP FAAHLVLLRE INAQQTFKDK LSHGFTSVFH SGSRSPEKPR
RLALQTLLYL QRCRFPNETN ITARNSWLDI DLGDAAIAAA ECRMWHEALL LLELQHSYAG
LQSGRSSRRS FASAKSVPGE VVAKVYENVD DPDFFYGKKQ EFDLAEVVSK MTHEGASQTS
LSLHSAMLDT RLRMGDQGQS FASIAQVTAS SLSAANMQGI SEAVRQYYED SGNNTELAMG
LLPNSDWDVQ PMNRSITYSK DMSTWLQDLY HTTKKQDLID KLDQSLLLLI DDMEASVSGN
AQTSDILTHL AIRGEIKQIM LAKSPEDLEV VWARIEARDE RVKLVEFERL SPILDGRESS
FAAMRRNVNL QAAFSLSPNQ ALRNEVRAAR HSLELASKFD VPQFCLNRTL YLSELNQVAN
QSGLEVDVAV RYDLARTLWS QDETAVSIGI LQKLKERDDT AKQAIPVTRA AILTELGHRI
AEARLEKPDE IISRYLIPSF EEIRGHENGS EAGRVYHNFA SFCDTQLQDT DNLDDFTRIS
KIRDRKDQEV RELEQMYKSS RDDRQKKQLK IHLDRARTWF KIDDEEWKRV RSNREELILN
CLENYLLSMK ASDDYPNDTL RLLALWLNQA ESREANKVVG KHLPGVPTIR FAPLVNQLSS
RLLDIKDDFQ KNLMDLMFRI CSDHPYHSLY QLFAASKSKA LKQDEVAVSR NHAAIRLSEI
VNKKSVSAAI WVALHNSCIQ FHRVASESLS EKEKRQGSKI QLRKLQSGQK LENVLSEAHT
RIAPPTLNIP LRPDHDYSSV PTFVKFDPMI SIAGGLSNPK IVTMTASDGQ RYKMLLKSGN
DDLRQDAIME QVFQQVSDLL KDHRATRQRN LDIRTYKVIP LTTNSGIIEF VKDTLPLHDY
LLPAHERFFP KDYKPNKCRK EIAEVQTKGL EQRLRTYRTV TANFHPVMRF FFMERFPDPD
DWFYKRLNYS RSMAAVSILG HVLGLGDRHG HNILLDENSG EVVHIDLGVA FEAGRVLPIP
EVVPFRLTRD LVDGMGLTGV EGVFRRCCNF TLEALRVDQE SIMTILDVLR YDPLHTWSIS
PLRLQRMQEN NEQAEATAAG AGAGASVAAG VDGGGGGMLP HDLASRREAN EPSEADRALT
IVAKKLGKAL SVEATVNELI RQATDERNLA ALFCGWAAYA
//
