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Database: UniProt
Entry: E9DY47_METAQ
LinkDB: E9DY47_METAQ
Original site: E9DY47_METAQ 
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
//
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