ID E9ETX2_METRA Unreviewed; 2912 AA.
AC E9ETX2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 2.
DT 27-MAR-2024, entry version 77.
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=MAA_03471 {ECO:0000313|EMBL:EFZ00875.2};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFZ00875.2, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFZ00875.2, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2] {ECO:0000313|EMBL:EFZ00875.2, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:EFZ00875.2}.
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DR EMBL; ADNJ02000003; EFZ00875.2; -; Genomic_DNA.
DR RefSeq; XP_007819660.2; XM_007821469.2.
DR GeneID; 19257757; -.
DR KEGG; maj:MAA_03471; -.
DR HOGENOM; CLU_000178_8_2_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000002498; 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; 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; 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; 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; 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 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 1844..2445
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2550..2863
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2881..2912
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 169..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2834..2871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2912 AA; 324826 MW; CF852225BC82C05B CRC64;
MSTVMSLTSD VKSGSIKACD KAVDGELDWL FCDKSYHQIF EALFNVVIRD RPALYDKSKK
ESARKVAAAR LTKCASAIRM TAARGAPKLG RKTLLALIDH ITQVLPDPDG DFVAPLIQDY
VKALSEVLSR QPHVEFLARQ DAKPWEACVD FLLDIVAYII PSEAHSSLTS VARPSPAPDA
STPRSIIRSN TSNQGQKRAG LAEGEPLRDA LEGLQYLSQA SNAPIGRRGR NVTELAIRVL
NMKHLSLGSM QAMCFSICNT IFARTQADDL EYGLSLVKKL LPLMSYWWRA EKVSQDELIK
GLRSEISKTI YLAHPHIEHI SSKWNEEIRN DIENLVDPLW QEYSKRGEPF RLQLHDLTFN
QSALPSSTMH LSLFGIRNHN SEGEGHWALV QNLSFLESIL LTRGGISARD TAGNSEQPRK
RQRTRECLSR LRLKLRSRDV GTQRTALQLL PFLVEGFGIA GEDLTSILDD LVTYVSNKDP
ITASWALVAS ASCASLPRMS ELDGDQWKQL WHLAVRSVSI PTTCRAACLL LHRIIEKDLL
PYNTISEDID GIVTTADVNG PGLVCDTSLA LMLHLLHARN ARLPSASQAT SNHIIRWVFL
KWNPNESAFA SSVSVLIQPL ELVNLLRVCC GVQPLRWNEI AASSGTSLGA TWRTQHEMAR
FNEYLLLLKR GEPSYDIQPC IYRSDSGRQL QPAADSHSFY PSKKLAFELF SPKFDDLVEL
CSTWLKKPSD GGTQISLDRF QSLLSACIVG SLLLPQFADL NTPQSTSMES NLVDLAERSL
VVALDSVEPE AFVDATLRVL RPCMPGMTTA DLNRSHSHHS SFLHILTTIS RVLDHRQSST
AVGTSLGLMD LDDEFDSQSS RATSASNPMP VPRQNVQLST SPRVFHVETR MRLGLLRAIH
DDSSQIGLLP EAWIDDLLLM SDDDLLCCQA LLLEISNSDL VVGSESAYNI IQRLGSIIST
SDYQCCEVAL TTCIDVLDGL HNIWLNDNQD LAEGVGDLYN YFIKVCLPSN FFSAKAQMSM
ARLLFSLLSA NPAYGTNLGL ASCRTSLLNI LSTGSMQVKC FVADRIAGIF DLFILMLHDE
IFVDVLASLP TNPADTSGIA FRLLALSKLA CRWPTLLRRC IYHIFETPGK ISQSIEYAKW
CLADISSTLK LKSPKELFRL FSRQLLYTWM EHDSINDIPF AIFGFKDLED LLRSAQAEAI
ALAVMRTQES TSAALANLLG MTEGDLIKRN FSTALSYSMA YGDAFSETRN EKGEDYIRKK
MGGKGYMEAI YINLVDTIAT FFDLIDQEDN LEKIFRKHED ICYAADNLES IKKLACSSSK
LPPNQQPMFR AKYIIHDIFR LCQGTEFQFQ DLWTPALVLS VTRSLFNTVH PALGSLHACS
VLRKVRLVIC LAGPVALESY CLEMLLNSVR GFIVDAECAD DALGLTQYLL TGGREYLTQK
PSFLAGYALS TLASLRVFLE SSQSSTTQES QFKATMNKTQ KFHDWFSKYL SDYVSPSFQD
DEQCNLFKSI TYSAARIRSS GNAEKGTSES KLLLDILRDG ATGSRLLNES SRELALKLLC
GDFTIPATIR EDIVETDAAA IEQASSVWKS CEAQDLSKNY LSWAGRVVGR SFAASGDIPE
DVLKESGVSF YGHVAPSPNG SEMGLLYLLQ DLTADQNSMM AGLAEAALRK AVSQAIEDED
EPLVVACQRS LSESLFTASQ WGSFCSPDTK ATQDSKLDGG QFVWEDSISS PSWLRRISTH
LVSTVSDSIL LSVLTPVLTE VPGFTEKAFP FIVHLVLCFQ IEQQQTAKRQ LSSAMKEWLR
DDRPTAQQNL KLLINTILYL RTQEYPKESS IADRMHWLDI DYAAAAASAS RCGMHKTALL
FAELASSEVS RPSRRSSAHR EHDINDVLLN IFENIDDPDT YYGLPEDASL SKVVARVEYE
NEGSKSLAFR GAQYDSHIRL RRREAERDGQ ALVKALGTLG LSGLAHSILQ TQESLGVSNP
SVDNTFTTAR RLQMWNLPAP GNSEHHAVIL YQAYQSIHNS TVLSDVQAAI YEGFGGIMKN
IANCNLNATA LRGRLAALAA LTELDDVLNI ADPSEVPSMI TKFKNRSEWM RSGMYGDVGQ
VLSCRETSIS MVCQHISLLK HAKMSADVLR QMQVESMILS SGIYRYHQAT QESLNIATAL
SDMIPLCENL NLHVDAAIKI EVANSLWDHG EMGTSIRMLQ AIDKESSLPK QSIRVNRSDL
LSKIGHKVSL ARLENPHDIQ KTYLGPALKE LKREGSSEAG SVYHQFATFC DEQLQDPDGL
EDLARLQNLR AAKNDEVKDL KALIDSTKES QLKAKYAHVL SKEKQWLELD EKELKRVEQT
RSEFVQLSLE NYLLSLISSD DYDNDALRFT ALWLERSAEE STNKAVMKHL SLVPTRKFAP
LMNQLTSRLQ SQEGTFQKLL FELICTICID HPYHGMYQIW SGTKARAQQK DDVAVQRVRA
TEKVAQKLSA NKSVANIWLS IDKTSKYYHG LAMERNPNKY KSGAKIPLKD SAAGQYLVSY
LARYRIPPPT LHIEVSVTKD YSNVPFISKL EPTMTIASGV SAPKIITAVG TNGIRYKQLV
KGGHDDLRQD AIMEQVFAAV SSLLKLHRST QQRNLGIRTY KVLPLTASSG LIEFVPNTIP
LHEFLMPAHE RYYPRDLKGS QCRKEIFNVQ NRTTETRLST YRKVTDRFHP VMRYFFMEYF
VDPDEWFVRR LAYTRSTAAI SMLGHVLGLG DRHGHNILLD SRTGEAVHID LGVAFEAGRI
LPVPELVPFR LTRDIVDGMG ITKTEGVFRR CCEFTLDALR EEQYSIMTIL DVLRYDPLYT
WSISPLRLAK LQKARDEEGG GEEPEPSDTA EAKKAKKQNG RTNEPSEADR ALEVVRKKLS
KTLSVTATVN DLINMATDER NLAVLYSGKK SR
//
