ID   ATM_EMENI               Reviewed;        2793 AA.
AC   Q5BHE2; C8VRE5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Serine/threonine-protein kinase tel1;
DE            EC=2.7.11.1;
DE   AltName: Full=ATM homolog;
DE   AltName: Full=DNA-damage checkpoint kinase tel1;
DE   AltName: Full=Telomere length regulation protein 1;
GN   Name=tel1; ORFNames=AN0038;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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 (By similarity). {ECO:0000250}.
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   -!- 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;
CC   -!- SUBUNIT: Associates with DNA double-strand breaks. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC       {ECO:0000250}. Note=Localizes to nuclear DNA repair foci with other DNA
CC       repair proteins in response to DNA double strand breaks. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AACD01000002; EAA65357.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF90326.1; -; Genomic_DNA.
DR   RefSeq; XP_657642.1; XM_652550.1.
DR   SMR; Q5BHE2; -.
DR   STRING; 162425.CADANIAP00002718; -.
DR   PRIDE; Q5BHE2; -.
DR   EnsemblFungi; CBF90326; CBF90326; ANIA_00038.
DR   EnsemblFungi; EAA65357; EAA65357; AN0038.2.
DR   GeneID; 2875815; -.
DR   KEGG; ani:AN0038.2; -.
DR   eggNOG; KOG0892; Eukaryota.
DR   HOGENOM; CLU_000178_8_2_1; -.
DR   InParanoid; Q5BHE2; -.
DR   OMA; HACSVIR; -.
DR   OrthoDB; 80538at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0016572; P:histone phosphorylation; IEA:InterPro.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR   CDD; cd05171; PIKKc_ATM; 1.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015519; ATM/Tel1.
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; PTHR11139:SF72; PTHR11139:SF72; 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   SMART; SM01342; TAN; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Chromatin regulator; Chromosome; DNA damage; Kinase;
KW   Nucleotide-binding; Nucleus; Reference proteome;
KW   Serine/threonine-protein kinase; Telomere; Transferase.
FT   CHAIN           1..2793
FT                   /note="Serine/threonine-protein kinase tel1"
FT                   /id="PRO_0000227702"
FT   DOMAIN          1734..2334
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   DOMAIN          2438..2750
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          2761..2793
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT                   ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          2444..2450
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2616..2624
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2636..2660
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2718..2748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2727..2746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2793 AA;  312284 MW;  4CE89A90D235FF36 CRC64;
     MKGEITLDGA IALLSSDKTK DRTDGLADLK HILQKNKRNS NLQSMSDKAC HKIFESLFRL
     VSTEKTFYNR ANSKGASSSK AAATRLSACA SVVRTAVETF LRNLRIKSVR AILDHITNVL
     VSPDSSLFEL LSVDYTKCLS TILHYPPHVE HLGVEEWESV LKFCLKVVNV RNDHNSQQST
     WSPHSSVMDD YIGASGGRST PSRMTPSLAV REKPKGPTGV VEEALSCIKI LSGVPNAPLQ
     DNAESILLGL ASYVGSPSLS GSGHQTAFSA INAVAMGIIF DNSELVRVTL LDLVPVIRQH
     WTTKLMGLKD ELLVTTMLIV TFLIDEIRRK PDEALIAVID GLIHTLQREY FRRSEKDILQ
     VDELVFDTNS IGQHEKFRLW PRLESPRSEH NWTVVWIMAR LLELSEELTT RLSTHCPPEA
     ETPSKRQRIS SKIDDVFRDS TASFGIRRVC ALQLIPFLLN HYACIDSKVS LLERLIPNIN
     DDNATISSWT MIAIACIAAS PQADKPPLKR YWQQAWDLTS RASTSQLTSR AACYLQNSIL
     QYSLLDYAAV AETINSMLSF VRLNGPSTVS DASLELWASV IRMTAQINPG SVSNASVQIC
     ELVDIYDIWD AETTVSIQKS SQSDPNDLGI LDLLQAKSES FLHTWQSLSE DKSRHVTPDI
     VQILTSFCIT VALYTSCLPE QPGPRLQTLL SNSRPTAIHR ALYGLLTPLS EVLESQRQSH
     KQRLYALNDD TMDLDDPFGP STDQVEEASN ILCTNRSDLP LFQDSASFHR YMTILISIYN
     RMYSQQSEPQ QHVTRALEDY LNDLDEVDLL AAHDLLPYVY QSCARTDRQT QLVLLENLGE
     KCLQTYELER CENSHLLCIQ MMCSLAMSWT RGTQDSLSDS AADIYTWFTT IFLKKGRASS
     SVLIAFAKLL GVILSLNPAY SSDQSSPSPK TTLFKIISDG EVLVKFNAGS LVPQLFGQFL
     LEDHDNVFND VLECLPRDPT WEEGIAVRLF LLAQLASKWH TLLRRSIYHI FETPAQVHHS
     LWYAEKCLRS VSDALGLQDA KEIFRLFSSQ ILYTWTETQS IKSMPFSIFG YANLNDMICD
     AQDEIVGQIM MRASESDAAE LSEILGRPFV GLLTDSFYKA EAYTIAHDIS TPPREGSQPK
     GVENRLKKIL GAEVFVTLIE AQFPQIVATF FGSLDFFQQV EKAFSKRESF QEALVTLKRI
     TEKGAARTVL PPNQQPSFRA RYLLDELEFL CKRSGYELET IWTPTLASYV CRTLLESIHP
     ALGSLHACSV LRKIKILICV AGPVMLSDYP FEMIIHGLQP FLVDISCSED AVAIFWYLLE
     AGKTYLCEQP GLMAGIAVST SLSLGRFLAS PPVNSRQESQ LQAVVGNLRT FCRWFDGYLR
     SYTSPALDDE SSRSFRRFTC SLQTIVEQES SGSGANETDL LLEVLKDRES KSGLLSKPIS
     DRVISLLCST SKAALGYHLT TIERDEDAIL NAVTVCQTLR DFNPGTEYRS WAARVIGRAF
     AATGKISDAL LREQDLTLFR SSSTQSGTDI LCRSKANILE VLGSKLLNSR QTGPIERTLQ
     LIISNLANFP DFEPCVSAIS PSVMKALTWS PYQCPGISLN ALEAKELENV HGWDLSLSPS
     YWARNVGLFL SKAAAEDPVI GSLSNILYLI PDLAVQLLPY ILHDALLAEI RGKVAEVRDS
     ISQIFNETLR AGAENSIPHA RLIIKCVLYL RNQPKPGEET IVDRDDWLDI NYAVASSAAS
     RCRLPKTALM FLETHVSRCT ASSRRSSVAK YDLPAGLLHD IFKNIDDPDF FYGVQQTSSL
     DSVIETLEHE SSGFKNLLFQ SAQYDSEIQM TGSGNAYGVL KALNSTNLQG IANSMIGALG
     NSSDTAVPLG SMLKAATNLR QWEIPISPLN TSPPATIFRA FQALNTPGPL VDMRASIGES
     YRSNLNLINS DRRSATSLRT AMRTLGILTE IEEVLGSGSA AEIDQKWEEI SARTSWLKNT
     DVQEVGEILS SHETLFSSIK QKDYLRSAFN LSDIDAQLLE VKVIRQSLHI ARNHGIAQAS
     LRSAVYLSKL ANHSVSLGLN IEGVAKFDLA NVLWDQGEMA PSIQILQQLK DRNDLHKQAI
     PISRAELLVT LSQGHHIAEA RLEKPEAIIQ NYLTPAVKEL KGRSEGEDAG RVYHGFAIFC
     DQQLQNPDGL EDFARIEQLR NRKEKEVVAL DAMLKTAEGK ERDNLKFHRT KTKQWFDLDD
     REYQRLKRSR EAFLQQCLEN YLICLRESEA YNNDVLRFCA LWLAQSHSDI ANSAVSKYIA
     GVPSRKFAPL MNQLTSRLLD VSDDFQALLS ELIYRICSDH PFHGMYQIFA SSKSKGGRDQ
     SALSRNRAAA KLADIMRNDR HIGPLWVAVH NTNINYVRFA VERLDDKAKS GAKIRLNKLA
     PGIRLEQDAV NQRLPPPTMK IDIRVDCDYS DVPKLAKYLP DFTVASGVSA PKIVTAIASN
     GVRYKQLFKG GNDDLRQDAI MEQVFEQVSS LLKDHQATRQ RNLGIRAYKV LPLTSNAGII
     EFVPNTIPLN DFLMPAHQRY YPRDMKPSAC RKHIADVQTR SFEQRVRTYR QVIEKFHPVM
     RYFFMEKFNN PDDWFGRRLS YTQSTAAISI LGHVLGLGDR HGHNILLDER TGEVVHIDLG
     VAFEQGRVLP VPEVVPFRLT RDLVDGMGIT KTEGVFRRCC EFTLEALRQE SYSIMTILDV
     LRYDPLYSWT VSPLRMKKMQ EQDTSDGPPV LPGSTTDQQR PTNEPSEADR ALTVVAKKLS
     KTLSVTATVN ELIQQATDEK NLAVLYCGWA AYA