ID E9DY47_METAQ Unreviewed; 2887 AA.
AC E9DY47;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 71.
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=MAC_02545 {ECO:0000313|EMBL:EFY91382.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY91382.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY91382.1,
RC ECO:0000313|Proteomes:UP000002499};
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).
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-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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|ARBA:ARBA00004574, 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; GL698482; EFY91382.1; -; Genomic_DNA.
DR RefSeq; XP_007808885.1; XM_007810694.1.
DR STRING; 655827.E9DY47; -.
DR GeneID; 19246856; -.
DR KEGG; maw:MAC_02545; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_8_2_1; -.
DR InParanoid; E9DY47; -.
DR OMA; HACSVIR; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000002499; 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:SF5; SERINE/THREONINE-PROTEIN KINASE ATM-LIKE ISOFORM X1; 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; 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};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, 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:UP000002499};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU365027};
KW Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365027}.
FT DOMAIN 1738..2339
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2444..2757
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2775..2813
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 177..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2728..2763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2887 AA; 322644 MW; 1D677F9C62066D94 CRC64;
MASSHMSTVM SLTSDVKSGS IKACDKAVDG IGLLICDKSY HQIFEALFNV VIRDRPALYD
KSKKESARKL AAARLTKCAS AIRMTAARGA PRLGRKTLLA LIDHITQILP DPDGDFVAPL
IQDYVKALSE VLSRQPHVEF LARQDAKPWE ACVDFLLDIA AYIIPSEAHS SLISVARPSP
APDASTPRST IRSNNSNQSQ KRAGLAEGEP LRDALEGLQH LSQASNAPIG RRGRNVTELA
LRVLDMKHLS LGSMQAMCFS ICNTVFVRTQ AEDLEYALSL VKKLLPLMSY WWRAEKVSQD
ELIKGLRNEI SKTIYLAHPH IEHISNEWNE EIRNDIENLV DPLWQEYSKR GEPFRLQLHD
LTFNQWTLPS GTMHLNLFGI RNHNSEGESH WALVQNLSFL ESILLKRGGI SARDTADNGE
QPRKRQRTRE CLSRLRLKLR SRDVGTQRTA LQLLPFLVEG FGIAGEDLTS ILDDLVACVS
NKDQITASWA LVASASCTSL PRTNESDGDQ WKQLWHLAVR SDIDGIVTTA DVNGPGLVCD
TSLALMLHLL HARNARLPSA SQATSNHIIR WVFLKWNPNE SAFASSVSVL IQPLELVNLL
RRRESSYSIQ PCIYRSDSGR QLQPAADPHS FYPSKKLAFE LFSPKFDDLV ELCNTWLKKP
SDGGTQISLD RFQSLLSACI VGSLLLPQFA DLNTPQSASI ESNLVDLVER SLVVALDSVE
PEAFVEATLR VSSTSVGISL GLMDLDDEFD SQSSRATSAS NPMPVPRQNA QLSTSPRVFH
VETRMRLGLL RAIHDDSSQN DLLPEVWIDD LLLMSDDDLL CCQALLLEIS NSDLVVGSES
AYNIIQRLGS IISTSDYQCC EVALTTCIDV LDGLHNIWLN DNQDLAEGVG DLYNYFIKVC
LPSNFFSAKA QMSMARLLFS LLSANPGYGT NLGLASCRTS LLNILSTGSM QVKCFVADRI
AGIFDLFILM LHDEIFVDVL ASLPTNPADT SGIAFRLLAL SKLACRWPTL LRRCIYHIFE
TPGKISQSID YAKWCLADIS STLKLKSPKE LFRLFSRQLL YTWMEHDFIN DIPFAIFGFD
DLEDLLRSAQ AEAIALAVMR TQESTIAVLA NLLGTTEGDL IKRNFSTALS YSMAYGDAFS
ETRNEKGEDY IRKKMGGKSY VEAIYINLVD TIATFFDLID QEDNLEKIFR KHEDISYAAD
NLEAIKKLAC SSSKLPPNQQ PMFRAKYIIH DIFRLCQGTE FQFQDLWTPA LVLSVARSLF
NTVHPALGSL HACSVLRKVR LFICLAGPVA LESYCLEMLL NSVRVFIVDA ECADDALGLT
QYLLSGGREY LTQKPSFLAG YALSTLASIR VFLELSQSST TQESQFKATM NKTQKFHDWF
SKYLSEYISP AFQDDEQSNL FKSITYSAAH IRSSGNAEKG TSESKLLLDI LRDGATGSRL
LNESSRELAL KLLCGDFTIP ATIREDIVET DTAATEQASS VWKSCEAQDL SKNYLSWAGR
VVGRSFAASG DIPEGVLKES GLSFYGHVAP SPNGSEMGLL YLLQDLTADQ NSMVAGLAEA
ALRKAVSQAL EHEDEPLIVA CQRSLSESLF TASQWGSFCS PDMKATQNSK LDGGQSVWED
NISSPSWLRR ISTHLASTVS DSILLSVLRP ILTEVPGFTE KAFPFIVHLV LCFQLEQQQA
AKRQFSSAMK EWLRDERPTA TQNLKLLINT ILYLRTQEYP KESSIADRMH WLDIDYAAAA
ASASRCGMHK TALLFAELAS SEVSRSSRRS SAHREHDIND TLLTIFENID DPDTYYGLPE
DASLSKVVAR VEYENEGSKS LAFRGAQYDS HIRLRRREAE TDGQALVKAL GTLGLSGLAH
SILQTQESLG VSNPSVDNTF TTARRLQMWN LPAPGNCEHH AVILYQAYQS IHNSTVLSDV
QNAIYEGFGG IMKNIANCNL NATALRGRLA ALAALTELDD MLNISDPSEI PSMITKFKNR
SEWMRSGMYG DVGQVLSCRE TSISMLCQHI GLLKHAKMSA DVLRQMQVES MILSSGIYRY
HQATQESLNI ATALSDMIPL CEHLNLHVDA AIKIEVANSL WDHGEMGTSI RMLQAIDKES
SLPKQSIRVN RSDLFSKIGH KVSLARLENP HDIQKTYLAP ALKELKREGS SEAGSVYHQF
ATFCDEQLQD PDGLEDLARL QNLRAAKNDE VKDLKTLIDS TKDSQLKAKY AHVLSKEKQW
LELDEKELKR VEQTRSEFVQ LSLENYLLSL ISSDDWDNDA LRFTALWLER SAEDSTNKAV
MKHLSLVPTR KFAPLMNQLT SRLQSQEGAF QKLLFELIYT ICVDHPYHGM YQIWSGTKAR
AQQKDDVAVQ RVRATEKVAQ RLSANKSVAN IWLSIDKTSK YYHGLAMERN PNKYKSGAKI
PLKDSAAGQY LVNYLARYRI PPPTLHVEVS VTKDYSDVPF ISKLEPTMTI ASGVSAPKII
TAVGTNGIRY KQLVKGGHDD LRQDAIMEQV FAAVSSLLKL HRSTQQRNLG IRTYKVLPLT
ASSGLIEFVP NTIPLHEFLM PAHERYYPRD LKGSQCRKEI FNVQNRTTET RLSTYRKVTD
RFHPVMRYFF MEYFVDPDEW FVRRLAYTRS TAAISMLGHV LGLGDRHGHN ILLDSRTGEA
VHIDLGVAFE AGRILPVPEL VPFRLTRDIV DGMGITKTEG VFRRCCEFTL DALREEQYSI
MTILDVLRYD PLYTWSISPL RLAKLQKARD EEGGGEEPEP SDTAEAKKAK KQNGRTNEPS
EADRALEVVR KKLSKTLSVT ATVNDLINMA TDERNLAVLY SDLNMYKLKR SYLKIHSFFY
TAYVFFVAIT LPECACSLEL VISCTFCVST EPATSDSISR ETPSIRPWIN TRTALKAPRR
RFGNPTR
//