ATM_DEBHA
ID ATM_DEBHA Reviewed; 2948 AA.
AC Q6BV76;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 03-AUG-2022, entry version 110.
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; OrderedLocusNames=DEHA2C04752g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG85943.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR382135; CAG85943.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_457893.2; XM_457893.1.
DR SMR; Q6BV76; -.
DR STRING; 4959.XP_457893.2; -.
DR PRIDE; Q6BV76; -.
DR EnsemblFungi; CAG85943; CAG85943; DEHA2C04752g.
DR GeneID; 2900195; -.
DR KEGG; dha:DEHA2C04752g; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_8_1_1; -.
DR InParanoid; Q6BV76; -.
DR OrthoDB; 80538at2759; -.
DR Proteomes; UP000000599; Chromosome C.
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:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016572; P:histone phosphorylation; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; -; 1.
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; 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..2948
FT /note="Serine/threonine-protein kinase TEL1"
FT /id="PRO_0000227701"
FT DOMAIN 1898..2497
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2602..2915
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2916..2948
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2608..2614
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2778..2786
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2798..2822
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 2948 AA; 339163 MW; 8782CEE081A1F880 CRC64;
MSSFDINKLV SCLQSTKIKD RNDGLSSVEN LLNSKFKLNP KQFDVLVISM FTLIENEQIS
YLKNKASSAE FRLSYGSNCL KLLIEKSLDY NQELRNSNKP IKMKYKFYMS IIHSIRNYYF
IEDNILEPCA LDFTKILSSI TSQGFFKEHL NYEDWLHIYN LLIKSSSFIL DELTKINMHE
KLLVEIFTSL HFLIQADSSI SVNYLQLVSS SVPNNYFKLL KILSKTCNFF KKESMLTVLL
FKIINKLIIT LCTENFKFVN KLIQISIKLM ISFHQTQLDS LQVQFLIFMN LSATHSFLNL
HNFPKLIGDS SIISDDPFDS RQDISIRSSE DSSKTNQSID SITDGDNDEV ILYNVGILIQ
NLVSKLYSSN NQVKSEDINF MRKPTDDKNW FKLRSIYLRV SEYDEPDSLQ PWLFNAGLSK
FINSYFEFKK SLYEHNTINS LNTFNASIVR SDSIHQNKRQ KLNILSEALY HSNNILDFCN
KLIIDKTDYK VQQTGMQILT FYLEVYSPRV EISPLRNITS NNDVKLSGSS STKNSSILDM
SDSTLLNSTF DFPLTTNDSE SQFNVNLIFK NVINAFDTDE LNYWSLMATR AIIYDSLQRS
IKIEEKYFFQ LLKIALQLIK NKEVSRISCS LVYSIISRHS NEGLNKIMEK SLIIQIDNLI
DLSEISGPFS ICEESFQLWY SINKLVRNIN LARNFILAER IQAWLISKWD IAANINIGFW
YSNPSSHFEF VNFICWLCGI NIEQSNQQNL LDLYCGVLNE ANIFMNSYNE LEVFFLNNCN
VRDNTSSWIE IDIDNLSENK TSDDLLIRII ETGKNYLKEE SVSVEAFEWA ILEFRIVRLL
KDHDIHNQLI NSIQYQASDL LECINVMNAT SNISDFIKVL SRTNFMLMKG GSIEIISTSF
ELGNFFDKIS GNGLMYNANQ RLLQQDQCSN NDNIDMFHDE FTSTNEPKTN FQTESKSTIL
NCINLGYVDV SCVQALKCLL IRNKIQGDSS VKTFDLIVKF LESLRSPEVL YCLFYLCRLL
ESGDLERSEI PIVSWTRIIR ILGEGPLTNF DLERDELTII IVSKLLTISF PIWHDNPDDA
FKKDCLDMCS WLLQCGTKNL ILTEASCIEF LIFMIAYSRY NNQTIIENNE IKSLFIKTFT
KSTNNIKIKI LPSLVNYLKS ISVTDQMAIY KELFLNFDTP QQSIETCGTF CLFFCILSEA
SIQVTIAVIF NFMEYSRFEY FLPYIKGAFS LIYKRLNLKS TKELFNLFKY EILKSWWSYN
FDIKQFPYDL FDYDDISSFL SSNCKELIAV SISNANNSNS GFLEMISSVK ETDLASLVFD
SLTLAIPLAY TREGIRNDMF KKLSDILKDQ YRLQMKEKVT TIIFEVIKFT DMSNEKYIRD
LGPKNEVTLQ LFKNNSQILE TPGSVSISLH SSLDLIRGLV EKYSVNPKSF WQVNVLYFLF
RHISIILHNS VNVEQKLLCL RKFKLLIILG HKNIFSLQLA NLLITTLSPF LKESDLHEDV
ANILSIFRIQ KLGKYDESEF LPFIVKLVSC LVEVDGTITS INSRLLKTLE EYVTLSNKNR
KVHVILQASM NVLKSKPIEL TSSDIEFFLN DEAELKLCTM GVSNKHVMKL VSSIFMIVEF
YDETRLHENV VKLLLNQKDT QQSKKFKLWS AEYLANYYLN GGLNNKISHI VSLVENDTLL
EDTFESDISS MDNILNEILR YIVSDNLEIA ACAESILGVL IWKFKTRKSD VQKFLNFDKH
ENDYASFIVP LDFHSCILLN SNDDELRILG HSIKEIISNL GQSLEGISFE TWTSRLFLSI
TQELAKFTSI APLFSSFATK VDSFSKTVLP GFICYYLNTT GKEGASQVIK LLSEFAKLRS
YESDFIELLM QILLKIRIGA KKSIPIFMEV YSSLNINYFY EIAAKHKYFK TALMLFEDDV
SKHEKHIDWS SNSRLLSNIY ESIDNEDLIF GLPEETSLEY AINMINRRNE TSDQLKFDSG
LFDTNISFDL ERRNTGILNS MVRNGFLGVS KLVSKSLNNV DTNNASFEWA WKLNCWDIPC
PREANEEHQL IYKTLKQIHD YPSFASESCQ ESLLQTLHIK DAIINCCSSP KELRLNIERW
LISLTCISNI RDVLRYKESD FRISLHEFSQ RTDWFEQADF DMSENILLAR KAALQITGDL
SSDCMSLKKE SIWLCVLHDL IRYNSIAIIA KESQKSVNSI VMINEISKTK FSESDHLLRD
SISQLTKYQI ARTLWQQGHT SIPVIMLKES QQNEAINTSI SSMNITPSLI NANLVDWMSN
SRQDLASNIM AKYVLPTADM VTYVKELDQK AKVYEILANF CETQFRSLSL NDHVYKLEKS
VDLKKSEIEE LKSHYSRMPV AADEKKNAQR YYSKLKAQYI GELSDLNSLK GSICEFSDKA
VEFYLKSILT DGDNDENLDK FFALWLEHSN KDDLHVSISD NVLSLPNHKL ISWSTQLISR
LSSEPSKFQN LLKSLIVGLC YDHPYHSLYG LISLKKHESY ANKSSNVLLI SKSVAATDIW
QQLLTRGDNK INEILLNIEK FCNESIKLAE YKVSKGKSIQ LDSLKIGNYW LQVLPHIPPP
TINLPVDLST RYNNVIYFDR VVPKVSIATS GLSLPKIATF YLSNGSEHKV LLKHGTDDLR
QDSIMEQVFE KVNNIFRKDK ETRKRELKVR TYNAVPLGPE TGIIEFVPNS IALIDVIRPY
HSKIDTLKAD KARDLMKTCQ SEDKTERYKT YDKISKKISP VLKYFFFDNY VAPDIWFDTR
TSYTRGIATT SMVGHILGLG DRHCNNILLD KTSGEPIHID LGVAFDQGKR LPIPETVPFR
LTRDIVDGFG ITGVNGVFDK SCEHTYRVLR QNKDHILAIL DVLRWDPLYS WSLSPIRRKK
LQNEGDRNEV GNLKPQEDGS EGGRAVLMVS DKLTAGGLSV EAIVRELVQE ATSPHNLALI
YCGWCPFY
