ID A0A367L447_9HYPO Unreviewed; 2943 AA.
AC A0A367L447;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=L249_1461 {ECO:0000313|EMBL:RCI09191.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI09191.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI09191.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI09191.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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:RCI09191.1}.
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DR EMBL; LKCN02000016; RCI09191.1; -; Genomic_DNA.
DR Proteomes; UP000253664; 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: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; SM00146; PI3Kc; 1.
DR SMART; SM01342; TAN; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 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:UP000253664};
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 1828..2431
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2535..2846
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2819..2852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2819..2837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2943 AA; 326288 MW; D2DBDE8C25CC7716 CRC64;
MVDSDKGADR GDNTRARLVN APRRRAQKTR RKRCSRFAHS SDLCLFILPP PFVVNEPLNR
AGCLPPWTLP TYLPAYSFTP KTSNVKQLAR DIKSGSLRDR ERAVDADLTQ LLKNKAANLV
ALEDKGYHEI FEAVFGFVLS ENRVYRDQSK PQAKRNGSSS RLSKCAAALR VAVARGSVKL
GRKTLLALID HITEFLPGPD DRFIQPLVSD YVKALTEVLA RPYHVESLVR NDGGPWQKCV
DFFIKVAKCS LPDESQSSIV VPLGRDFSAP ALSAPRSTRS IAATQSQNRS HALEGGPLRD
SLEGLKCLVQ AANAPIASRS EDIMNLILGV LGLKHLSLGS TQTICFAVVN NVLASTHADD
LTFANHLVKS LLPLMGYWWR PDRVSQDELI KALRNEISET VILTHLHIEH LAVINGEAAV
RAQVQGLLEP LWLEYSRRNE AFRLQLNDIT FCPSSLPDGS LRLDLFGLRH YNVEGEGPWA
LVQNLALLEA ILLRPNNTQG NDEPEQRHKR RRLREGPSRL RLKLKSKDAG IQRTALQLIP
FLVATHTLER EDAIELFAEL VPHASDKSAV TASWALIACA RYVAELSSAD AVDIIDEPGY
ASSQSIHVSP LQLANLLRAC CGVRSIPWHG QQAVFGSTLG ETWRLQREIA PFMRYLLLLQ
PEGSESRSYE GERSPTGSQS SSPANPGNFY SSRKLTLELL HPKIEELRAL CESWQDKAAQ
RGSRISVEGF QCLLSACLAG ALLFPQISDL NSTQSSMVEA ELADIAEKSL AAALDSVESL
AAAHSALRLL RSCMPNLATE SLNHLHREQF CLLRIMAISS CSLAKRRLDT DSQDSDLMDI
DDDFDDSQIN KATTSSATSS FPRQVQQLYS SPRAFYIDTK ARLALLEALY NDSSQIGLVP
KLWLDSTLSM SSDDLLLCYG LLVEISTCDL LMSPEDGLNL VQRLGFTISK SEYRSCEVAL
TACIDVLDGL HSMWLGDSLV LADSAGDLYD HFIRAALPSG ILSPRAQSSM ASLLFTLLRA
DPDYGKNLGL DSCRTSLLYI LESGRMKVKC FIGERIASIF ELFILQLHDE VFVDVLNSLP
TDAGDAAGIA YRLLVLSRLA CRWPTLLRRC IYHIFETPGK ISHATDYATS CMADIADKLR
LSSPKKLFDL FSRQLLYTWM ENDLLKDIPF SIFGFDDLKS LLSLAQADAV GLAMMRGQEN
VGADLAQILG SSTKELLRSN FTTALSYCMI YADVSRIPGP IERIETILGS RAYAEVVSAN
FVDIVALCFN LIDQDSSPEK AFLRYPELAY AADSLKAIKN IAHSPADLPP NQQPTFKAKF
VIHNILKLCQ KIKLQIRNLW TPALVMSVTR RLFNTVHPAL GSLHACSVLR KVRLVLCLAG
PVAWETYCLE MLLNSVRSFM VNSECADDAL GMTQYLLVQG SRYLRQVPSF LAGFALSTLA
SLRVFLESSQ SSTTQESQFK ATMDKARQFH EFFRKYLADY TSSAFRSDIH ATSFKSITHS
AGLIRSSGNA EKGMPESKLL LDILQDGATG QGLLDESSRK LALGLLCGDF TIATDIASDI
IESDEDAVSY AGVVWRSCEA QKLSSSYLAW AGRVVGRSFL ASGYIPDGVL RESRLSQYKE
MAPPGLNGSE MGILCLLQQL ASNQDSVVVG LSEVTLRTVV SQALLKEDEE LLAACQTTLS
HALFLASQWG AYRSPPSDAL ETSISADAWT EDVASEQWLS RLSVCLARSV PESILLSALP
PSLGELKDLA EKSLPFVVHL VLYFQLRQPT AKRQLSAAIK EWLSSKARGA RNNLKLLINV
ILYLRTQEYP REASIDDRSQ WLDIDYASAA EAAARCGMFN TALLFAELAA SESTRASRRS
SQVRQLDINN TLLTIFENID DPDAYYGLPE DASLANVLAR VEHEREGSKC LAFRGAQYDS
HLRLRSMQAE ADGQALVGAL GTLGLSGLSN SLLQTQQELG FSGSAMETTF RTARRLEMWN
LPVPSTSEHH SVTVYKAYQS IQQAIDLSAA RSAVYDGLSR IMRGLTGSSL NATALRGRLA
SLASLTELDD LINVTEPTGM RSMLQKFQAR CQWMRSGLYD DVSEILSCRE TTTSLLSQHG
SFVSSAKLPV TSLRRMQVET MLLASGIYRY HQALQESLNI STSLNMLISV CEELGLHVDV
AVKMEVASSL WDHGEMSSSI RMLQAIDKGS SLAKQTIHVS RSELLSKIGH RVSIARLEKP
QDIQKTYLEP ALKELKRDSS GADEEGAVYH QFATFCDEQL QDADGLEDLE RLQSLRKGRS
DDVAAFKALI STTKESQLRS RYSHALSKEK QWLELDEQEL RRVEQTRSEF LRLSLENYLL
SLAASDEHNN DALRFTALWL ERSTEEATNK AVARHLHKVP TRKFAGLINQ LTSRLQNEDS
GFQNLLFNLV VSICTDHPYH GMYQIWSGTR VKPEDKDEVA VLRVKATQKV AQRLAETKDV
AGIWLSIDRA SRSYHFLAGE KVSEYKSGAK LALTKSKAGS NLMACLSKYR IPPPTMHLDV
LATKNYSDVP YMVKLEPMMT IASGISAPKI ITAVGSDGIK YKQLVKGGHD DLRQDAIMEQ
VFAAVSSLLK LHRSTRQRNL GIRTYKVLPL TATSGLIEFV PNTVPLNDFL MPAHERYYPK
DLKGSQCRRE LSEVQNQAVE TRIKTYRRVT ERFHPVLRYF FMENFLDPDE WFSKRLAYTR
STAAISILGH VLGLGDRHGH NILLDTKTGE AVHIDLGVAF EAGRILPVPE LVPFRLTRDI
VDGMGITKTE GVFRRCCEFT LDALREEQYT IMTILDVLRY DPLHTWSISP VRLAKLQKSR
RQEDGSEVAE QGGETTEAKE SSKAASGRFN EPSGADRALE VVRKKLAKTL SVKATVNDLI
NQASDERNLA VLFSAKANKR MIVDEHFAVS GPVTSLIQDV TSAPSPSSRL GTYWLLPTLR
LTP
//
