ATM_KLULA
ID ATM_KLULA Reviewed; 2761 AA.
AC Q6CP76;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=KLLA0E06963g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382125; CAG99350.1; -; Genomic_DNA.
DR RefSeq; XP_454263.1; XM_454263.1.
DR SMR; Q6CP76; -.
DR STRING; 28985.XP_454263.1; -.
DR EnsemblFungi; CAG99350; CAG99350; KLLA0_E06975g.
DR GeneID; 2893812; -.
DR KEGG; kla:KLLA0_E06975g; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_8_1_1; -.
DR InParanoid; Q6CP76; -.
DR OMA; LDKFCGL; -.
DR Proteomes; UP000000598; Chromosome E.
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; 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..2761
FT /note="Serine/threonine-protein kinase TEL1"
FT /id="PRO_0000227704"
FT DOMAIN 1692..2294
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2404..2710
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2729..2761
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2410..2416
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2579..2587
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2599..2623
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 2761 AA; 317046 MW; 547D44B0DAF2B350 CRC64;
MSFSFEVSVI VTGLSSLKLK TRNDSLDNLN LLLKTSPTEV PVKAFSPILD AIITIIESEK
TRYEKTRLEN GKDARIELYE NRLGSAAYTL RLFVERNCER FKPKHIKLLS MTLFELMTRP
RSRSLITSVA DHLTYSLVAL CGSPVFQCNF ELHQWISLSH DISDAVTYHL DVSYNDKIIA
NLLQTLLELF QIDTIGIEDI ATPVVRMTIK YLTLITKENT NTRTILTLVN SAILRLHLIR
FQDVINLSYY TIKHLLRIKL TNENNIGEIA RFNLMISEVL YNKTPIIVGE DKDQSYVNKE
KLLPALQDYL IHSLKQYDHT KFTLDCVTFI DGPASSKFNW YSFSDICQNE KNCLEDIWLY
ALSLTMMLKA NYQFLEYKES SLAGGSLLFK RRKVKDTFAH MLKDSLTYDD FLCNCIDSDS
IKIKTTGLHI GLLYLSIFDC SNIELSHLKE ELFRCSQDVR FMLLCLSCFI PMCSQSKNSF
SPEEEIRLFK MCVPLLKTSN GCKTACSLLY KLIEFQLEPI KDKSVLQQMS DLYLLSDVNG
PALVCNESFK FWMHLHYYAK TFQTVKSPIT YVFSWLYARW DQLFTLVVSE THFYVFASWL
CGCTHTTFPT FEYSRPSLFH DTWMGLSEER ASITGFSLTI RTIELRKQKF APVFCEEAER
VRFMYKLFDL IDESAISATF IDRAIQVLRT IESLVGQRNY TDYLSRFKEI FLLSSSVIDF
GQNAQIFSVM EGMISLKDSL LRHIIMDILP TEKVLSTFMQ RLAEHTQQTS HQDEFLSHHA
KPEAGSIPIS EMIEIGFEFA LQVHSVSKAF DPLSSFILYS KKLSLPMLNR TLPNLITYLE
NNENEIPTAS LERLTQFLGS SLLAPSFDTS STSMKLLTRY LEGISKYWVM EDRSQVLTAD
CNDIFDWIVT QYDESSFSGV EALYELARFM TLLLEKYNLS NSSISGGKQR VFKILSGCIT
RLPKYLTNRV VSLLGTYVKR VGVTNQRILF KELLQRFNPP QESVETAAFF SLTCTKLSLI
NEFYLLNSIL HLLDNTNFSH LLLYVEKSLD TISTFYGLCS KQDLFHQCRY FIIDQWFTKS
AKSKIYEPSI WKVELFEFEF DEFCIRYQME LTSFFFAKSS TYYYIIDHLK KLLNLKQEAL
LTKYIAPTIA LSYVDSGVKD LIFDIAADLL GRKFPNVLTI NLDDVIYYFI KLSDLSNLAT
SLTFWCKIFN SSRFTNMLHY NSSNCMQLND NVAIAFPIVY KVLKKNVFTD IDDGRSFEYV
IQRLVMDLQN CVLIDQKIRV LRQIKLLVLF FEHKLTLFKD IDFFLLELSK FLFNADIFSE
VYGFILDLLE FSANNKMDVA RSLTELMRFC FTVTDSNVKK TLFPKVNPVL FNFCVSDGKQ
LYATCYALLT LETNSFGWND IAQVFKFQEV DRTSVSLLSD LFDNFDYDGS FDANLISPTT
IQNLISIPRD NARVSDKFRR WLGNILGEIV YTRPYDHIIP HHCSTLDLES GISGLLQILW
VQYQKADDIS LRFLLDHIQS IILQDESVLA EISSDSYSSL VNLKNLTDIS WEKFENCHGM
LNIKLGETFL TLTFTDRSCH YQKWISAFIC NILLVIVEKF PSFRILALLC DNTAFLHSAI
ISQLIKILLV SFPKQRSSFL SDILNRADEI FKTEDRTLKM EVITKVFSII RGMALNGVQN
ALYVYDKIKL QPVIPIMLSL GSEIWSLMIY EEFYGEYCTG KMLDYELLYQ IYSKIDEKDL
FYGLPLSSSL ASSLTLISKT KFNSYTNFAL SNGRFEEGLR NKDSSCLHEF ASVTSSNGFT
GLATMLDSNF ENPLLSANQY SWALKLNKWD LPIPEARDSF AKSAFSILKD VKEIPDFFSF
DDHILKVMDG GSLLKNSQLN LETMESLGLL VSLKKLGSAD MNTLTTLNNL RVHDTLNADY
LPENVFDILH WSRHFFIESK INNTSVIEHA PGSNFTLQLA KILNLVHAST FCRDQGRFQD
LINIVMTLEA AVDDITNNPA IGPSDTITLF CKRISTVESA RMLWANKESA MAINMLEDLL
QTNLTAVNVE NVSLADVQDI LMPDAVVDSQ LVEWSSFSRH RSPDVIFNDH ILYYERDVLN
INEPNLRSSI CYTYAEFCYK QSQKVDEGEL LYLKQKIAKA SNQLQEISSI YKNPKLRDAE
RKEAKRHHNR LSLQNHHDKD RYNKISSSRI AFVSQALHFF LTTLVHSNSR DAEVVDKFCS
LWFSYSTDDI INSKLQKEIG TVPSFKFLPW VSQMASKLAD SVSPFQDTLQ LTLKRMLYKL
PYETLYPLIS MSLQDSESKV IDPVTKSRVE VVNKIIAALD MYDSGRYGSQ FTRPVQAFCS
MSVALACHKI PPKMKFLQLD TLNIGKYWLE TLPKVHLPLP TLPVKITCSQ DGRREGRSYI
SSIDPKVLIS SSGLSLPKIA TFTVSDGTRH RVLLKGSNDD LRQDAIMEQV FKQVNKILKA
NKTTRKQNLS VRTYEVIPLG PRAGLIEFVA NSMSLHDILL NLHCNDEISF DKARKTMKAA
QNHSVEERVL TFSRITEKIK PQLRRFFFQS FVHAHDWYES RNRYTKSVVT SSIVGYLLGL
GDRHLNNILI DIKTGEPIHI DLGVAFDQGK LLPIPELVPF RLTRDIVDGF GVAGIEGLFR
NNCERVFKVL QDEKERLLCV LNVLKWDPLY SWKMTPLKKQ RLQAKFTGDY DEEEISVSDA
DFSELLEEDN NNDESIRALK GVESKLYGDG LSVEAIVQEL LSSATDKQNL ATIYMGWSPF
Y
