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 27-MAR-2024, entry version 124.
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; 227321.Q5BHE2; -.
DR EnsemblFungi; CBF90326; CBF90326; ANIA_00038.
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; 8448at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
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:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
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; 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; SM01343; FATC; 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; 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
//
