ID A0A167X6B4_9HYPO Unreviewed; 2836 AA.
AC A0A167X6B4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=AAL_07578 {ECO:0000313|EMBL:KZZ89685.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ89685.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ89685.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ89685.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ89685.1}.
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DR EMBL; AZGY01000024; KZZ89685.1; -; Genomic_DNA.
DR STRING; 1081109.A0A167X6B4; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000078544; 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; IPR003151; PIK-rel_kinase_FAT.
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; PF02259; FAT; 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 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 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:UP000078544};
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 1766..2367
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2472..2785
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2804..2836
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 599..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2758..2792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2758..2783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2836 AA; 315305 MW; C4F24194ADD65567 CRC64;
MAAARGAPKL GRKTLLALID HITQILPGPD EGFVEPLVPD YLKALSEVFS RVPHVEYLAR
QDATSWEACV DFLLDIAAVA LPDGVSSSVL PSLKASPAPK MSAARLTVTF SNQTQDQRKG
SAVDNDRLRD ILEGLQYLVQ AGNAPLLRRA AQVTNLAFRI LSMKHLSLGS MQAMCFTICH
IVFSRTHADD FEFGLSLVKD FVSLLSYWWR AEKVSQDELI RNLRNEISKM IYLAQRHLEN
LLNDKDDDFR PELEVLADTL WQEYSRRSEP FRLQIHDLTF NPSSLPAGSM CLSLFGVRNH
NLDGESHWAV VQNLAILESL LLQQSKTNAN MSLDNSEQPR KKQRTGERLS RLRLKLRSNH
VGLHQTALQL VPFLVHDCDM TDDYLYSLLE DLTVRMADKN TVTASWALVA AASCIAFSRP
SLARSDQWKQ VWHFAVRSIS LPATCRTACL LLHSLIERDF LPYSSISEDI SSIVTTADVN
GPGILCDTSI LLMLQLLHLR NIRLPSASQT TTNHIVRWAF LKWNPSDLTF AASVALLTHP
LELVNLLRLC SGTEPISWKV PAAGSGSALG ETWRLYLEME SFNEYLLLSR RKGSHAGCQT
YPHGSSADRQ KTSAADPSSF HPSKKLTFEL LQPKLDDLLD LCDTWSRRPS EGGSQISLDR
FQSLLSACMI GSLLVSQFSD LNMPQASTVQ SKIIVLVEKS LNVAMDSIEP FVFVESALRT
LRSCMPGLQA SDLTCLHSQH HTLLSVIAAA ARVLNERQSV STFGSASDFM EIDDDLNSQS
SGAASMTILT PLPRLNVQLC VSSRAFHIET KKRLNLIRRL HDNPCQIGLL PAEWIADLLN
TTDDELLNCR ALLLEISTTD LVVGIDNALS IIQRLGEVIS LAEYQCCEVA VTTCIDVVDG
LHNLWLTDNS DLADSVGDLY NYFVKVCLPS NLFSAKAQVS TARLLFTLLV ARPSYGSDLG
LDSCRTSLLN ILASGPMQVK CFVAEKIADV FDLFVLMLHD EIFVDVLASL PANSDDTSGI
AFRLLALSRL ACRWPTLLRR CIYHIFETPG KVARSIEYAK RCLADISESL SLRSIKELFQ
LFSRQLMYTW MEHDAIEDIP FTIFGFEDLT DLLQSAQAEA AALAIMRIQK PAIATLASSL
STTVRSLITN NFPEILSYSM AFGDAHGSLE NGKGEDFIRE ILGHKAMVEA IRINFVDIAA
SLLDLVDQED HFERVLRKHE SLSYAADNLE TIKGFSHSAN RLPSNQQPMF RAKFIIHDIF
RLCQIVDMGY QDLWTPAVTI SIIRRLFNTV HPALGSLHAC SVVRKARLVV CLAGPAALQS
YCVEMLLNSA QSYIVDPVCA DDALGLSQYI LSGGADYLAE RPSFVAGYAL STLASLRVFL
ESSQSNTTQE SAFKATMDRA QKFHEWFSRY LAEYTSLMFH SDSQATLFRS ITHSAAHIRS
SGNAQKGTSE SKLLLDILCD GLFGHRLLNE SSRELALKLL CSDFSIPEAI ADDIIDTDKA
SVEQSSRIWK SCAAHNMSNT YLAWAGRVVG RSFAASGEIP SGVLKESRLG FNGETGKDLN
GSEFELLSLV QYLAADQNSR IAGLAEAALR IVVSKATELE DEPLVAACQK TLSESLFSAS
QWGHFHFHLQ SGPKSRMKPH TRSGWDCAID APGWLHAVSA SLASCVPDSI LLSVLPPILA
EVPDFAEKAF PFILHLVLGF QLEQQQETVK QQVSSSLKEW LQCMTPGATQ NLKLMVDSIL
YLRTREYPKE TSMADRLYWL DIDFATAAQT AARCGMHRTA LLFAELAVSD SGRSHRRSAV
HLERGLDETL LTIFENIDDP DAYYGLSEEA SLSRVLSRVE HENEGSSSLA FRGAKYDAHL
RLRAKEAVDD GQALIKALGT LGLSGLSHSL LQTQQHSDTD NALINSTYNT ARRLEMWTLP
APANSSHHDV VLYQVFQCIQ SSADTSAVRS AIYEALGSIM RNITISSLNA TNIRSRLTVL
AALTELDDLL SMSGASEIGN IFGKFTERSG WMRSGSYGDV SKVLSCRETT ISMLCQHASL
LRHATLGPRA LRQMQVETMI LASGIYRYHG ATQESLNIAT ELDEMIGLCE DLGLHVDAAI
KIEVANSLWD HGEMGTSIRM LQAIDRDSSL SKQSIAIKKS DLLSKIGHKV SLARLESPHD
IQKSYLGPAL KELRRESNSE AGSVYHQFAT FCDEQLQDPD GLEDLGRLQG LRKAKNDEVN
ELKALIDSTE KSQLRTRYNH VLAKEKQWLE LDEKELKRVE QTRSEFVQLS LENYLLSLIS
SDDFNNDALR FTALWLERAG EETTNRAVTK HLPLVPTRKF APLINQLTSR LQSQDSTFQK
LLFELVCSIC VDHPYHGMYQ IWSGAKARAQ QKDEVAVQRV KATERVAQRL ASSKSVADIW
LSIDKTSKYY HGLAMDRNPN KYKSGAKIAL KDSAAGQYLL SCLTRYRIPP PTLQLEVSIT
KDYSGVPMIT KLEPTMTIAS GVSAPKIITA VGSDGVKYKQ LVKGGHDDLR QDAIMEQVFA
AVSSLLKLHR STQQRSLGIR TYKVLPLTAS SGLIEFVPNT IPLHEFLMPA HERYHPRDLK
GSQCRKEIYN VQNRTAETRL NTYRKVTDRF RPVMRHFFME YFADPDEWFA RRLAYTRSTA
AISMLGHVLG LGDRHGHNIL LDTKTGEAVH IDLGVAFEAG RILPVPELVP FRLTRDIVDG
MGITKTEGVF RRCCEFTLDA LREEQYSIMT ILDVLRYDPL YTWSISPLRL SKLQKARDED
GVGGGETEPH EAAETKKARN SHGATNEPSE ADRALEIVRK KLSKTLSVTA TVNDLINVAT
DERNLSVLYS GWAAYA
//
