ID ATM_CANGA Reviewed; 2763 AA.
AC Q6FRZ9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 122.
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=CAGL0H04609g;
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138;
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}.
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DR EMBL; CR380954; CAG59928.1; -; Genomic_DNA.
DR RefSeq; XP_446995.1; XM_446995.1.
DR SMR; Q6FRZ9; -.
DR STRING; 284593.Q6FRZ9; -.
DR EnsemblFungi; CAGL0H04609g-T; CAGL0H04609g-T-p1; CAGL0H04609g.
DR GeneID; 2888643; -.
DR KEGG; cgr:CAGL0H04609g; -.
DR CGD; CAL0131518; CAGL0H04609g.
DR VEuPathDB; FungiDB:CAGL0H04609g; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_8_1_1; -.
DR InParanoid; Q6FRZ9; -.
DR OMA; IYMGWSP; -.
DR Proteomes; UP000002428; Chromosome H.
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:SF6; -; 1.
DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 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; 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..2763
FT /note="Serine/threonine-protein kinase TEL1"
FT /id="PRO_0000227699"
FT DOMAIN 1715..2294
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2403..2712
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2731..2763
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2409..2415
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2578..2586
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2598..2622
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 2763 AA; 319038 MW; 3CF36DFF08660AD7 CRC64;
MENYQIRTLQ DQLTSSKLRD RNAGLQELQS ILKDNPGFIA NEQINGLLNT LLSLLENEAG
KYIDSIEDDT DSRQRKENIS ISRFSNITYT LRLFIETVIE KFKLSHLKLT ISAVKDLFYN
DARIIVPVIN DVTYCILAIV KSEIFGNKIG PSQWLDVAEY TLWLIKITSS NRSNIRALTN
SLDTFYVLLI KGSISLSKVA KEALVIITNL IVFEKGETAT TNVLLSISSN LVARLHCQHY
YDTTSLIIEC WKLYTRIGKT NNFNLLNDIS KIDIFGGGLL QNQIPIMPGQ EIMGSRISHS
VVLSTLQDYI PMKVKEMLDV DHSLTIGIYD DLNNSNMDLT YNTFAKTHCK DLAWLRLFGL
YDTLCLYYRL SNQERENNAT QILKKIKYEG SLQSNLNQCN SLLDYSQSLL ESGDPLIQLL
GCKLFFLLNL DHPIACNTEL IDRLCINTNN ISLTSWHLAC IFTNISYDLW NFDETLYLKV
LKYITPLLST SEVNIMACLI FNKLLHSLTR EPIDELSSLV NSIIASPDSV LPIEISSVTC
EAWQHIFVFA INNLKVDNSL LLDSFSKWIN HNITQTIHIE HLKLIFEFFL WSLDVVVGST
SHNKQHNTYN LLNLKTSDSA LAIWYFYENQ RKFLTQTIQT SSQASVNTKS MVCPITSTNI
KIQWLLNIID NYFTTSKNHS LKYTFAISLI YFINFIEKSG KVYTYLNQEL NQRLNSILIE
LDFLSFDKWE EGKQFIEIIC NQETFFNRLH NDVVFKDNIL LSLINLFEKE YSHFLNADNG
STAKTGNDIY LNQRSILRFR TDIKLMTQFF TCVDSNVPGK IGIYLDRLLL YSMGPNESLV
LDELLSWVTN PSNNQYYEVH SLEKLCQFLA KSLLNSKYQL SDFSMIRLGL FLTSTIELWV
NVKYNILNSD CNDFLIWITN NLVQNNFGET GTFVVLIRLF ISVLKHNSTV NSSCAIKTQD
LYSMLIFCMR NVAYSTLGNI VDELKAYMSK KSHKNRKTIL DDLVELFEPM PESVEKAASS
CFVLFGLLDC NDTNFVYTLD IFSNYGNIPH ISFFLKKAVK NYVNNYYQGN KIQLLNVHIL
EVIRQWTKRN DTDRQLYFNS VIGSLFGFGS IQEFERQYNR EICALIFSRS DSESLERNFF
SDRNTSKCEM LRRSLYLLIP LSYYDNGVGD MVFNKLKDSF RGQLESVLSS NFIIVMRYAL
KLCDCSDYTS VLNEMQRPNQ SSSLLELFMD SEMKNAINRM NIYITVHSVI KIFKNCGRSR
QTLLLDLRTL ILWIISDIQK SESSWEQNNH LRQLQLLVFL YEDTFLQSVL HIELMNWLSY
LLKIENIEAD VFLLLNCLLS LIKPNSLDKP DSLTLFFLNV LHFYVRNKEC LKIGDEDMNM
LSNNLSTVNS IALKLLTNGQ VTDLIYNQVG DLTSQMYFAE EVELFALLMT FAPPMPDYVS
HKMNKKFIEY VYKSNNLIDI DNFSLWFSDY STQYSSLILE LEENSSFCEK DGFGIDDMEI
VYDFSDSAVS AMYSVLFRSL ISIKPTIGFK SFALSNIICH LISINILKDK DLLSKFLRAT
KMKIAFSAKE IDETIIEHFG KSNCGCVISE HYLESEFFDT NIPYKDWLVK LCMFFISQIS
LNSKEIQWFI PLCYESMDFC KQNVCIFFLA AFSFDHRRMS STWKHIFSRL NDLTMASDCL
AKLTLLLSFI RLIRSGALQG RKEYSNLYQK IEFKGVIDAA LKIKDSKFAL QLFEEAYMCE
NGDYDVALLT SIYEQLDDVD MLYALPTPIS LNGFIKNANR LSPHSLKALQ LNGAYFDANF
NHLVDNGSHQ LVNTLTGMGF NALADIADLR TSCDNPADAY LRCLQLDKWD LPKPKAIDCK
IVSFYNTAYD LRNTNIEFVD LLQNAEIQLY KAKANFSSKL EWFETIREYV KTKRAIISLK
TDTDISRFKI DHVINPDRYL ENALISDIKI NWQFRYLMLK IYVEREKFAN EAMKCIPILE
LIHQTELSVD FHIQQTSLSR ILSMEAAMKR FHIADTNLVE QLSRHVSYVT ALALREFGET
KAPLTILSKL LSDKSYKLNY NTFVSDDEVR AQLIWDSYQA KVKSGIQIFE NDVEHWDVSI
NNIRSAPDTI YKVANFLNLE ISRLNGSDQL KEKQKSYRRT RQELKDIESV VKSSNLSNEE
LLVGQKHYHN LKTHMENDRL AIENICLTRK KLIKRALDYY VQILILTNNY DYDVLDRFCG
LWFENDDDDD INTDLTSKLS QIPTWKFLPW VNQFTSKLSL LKSKFQKQLW YIMKRLLYKL
PFETGYAVIN LQLYEKYSDK LDEKISEKIK AANLIFDQLQ NSQISVKEGE YLRTIQEFCY
ATLEIAELKV KGKNAQISLE TLNIGRYWIT ELPKKNLPLP TVTRTINSSQ YTLDSSRNIV
KVIGNITITS TGLSLPKVMT LLLSDGSRHK VVIKYGSDDL RQDAIMEQVF QQVNKIFGKD
VEMRRSDLHM RTYNVVPLGP KAGLIEFVNN SLSLHSILTD IHKDDNYSWL EARRSMKDVQ
SKSDKERILT YLDITKKISP KFRNFFFNSF IDANGWICAK RKYTKGVATS SMVGYILGLG
DRHLNNILID TTTGEPIHID LGIAFDQGRL LKIPELVPFR LTRDIIDGFG ITGVEGIFRR
TCEQVLNVLS RDSEKVMCVL NILKWDPLYS WAVSPFKKHK YMYDDNLEGH MTTATNNSKV
IERKLTPKLD SDENQQSYRA LKGVQEKLDR NGLTIEATVE KLIQEAVDES NLALIFNGWS
PFY
//
