ATM_ASHGO
ID ATM_ASHGO Reviewed; 2768 AA.
AC Q751J3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=AGL287W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54204.1; -; Genomic_DNA.
DR RefSeq; NP_986380.1; NM_211442.1.
DR SMR; Q751J3; -.
DR STRING; 33169.AAS54204; -.
DR PRIDE; Q751J3; -.
DR EnsemblFungi; AAS54204; AAS54204; AGOS_AGL287W.
DR GeneID; 4622673; -.
DR KEGG; ago:AGOS_AGL287W; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_8_1_1; -.
DR InParanoid; Q751J3; -.
DR OMA; LDKFCGL; -.
DR Proteomes; UP000000591; Chromosome VII.
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:0042162; F:telomeric DNA binding; IEA:EnsemblFungi.
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:0006975; P:DNA damage induced protein phosphorylation; IEA:EnsemblFungi.
DR GO; GO:0006302; P:double-strand break repair; IEA:EnsemblFungi.
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; 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; Coiled coil; DNA damage;
KW Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Telomere; Transferase.
FT CHAIN 1..2768
FT /note="Serine/threonine-protein kinase TEL1"
FT /id="PRO_0000227695"
FT DOMAIN 1825..2308
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2417..2724
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2736..2768
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2423..2429
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2592..2600
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2612..2636
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2696..2722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2141..2204
FT /evidence="ECO:0000255"
SQ SEQUENCE 2768 AA; 315374 MW; 5D6F08B3DDF04F95 CRC64;
MEQYVASAIN LLSSPKLKER SQALTDVAAI VKDNPDTLTS KSVGALVQSL IDILDAETRK
FDELCRRRPE AGARVELAQG RLNSVVAVLR LVLETIPDRL RAKQFRGLVL SLPELLGWAI
REQVHDMLQP LSACLQALTE CHTFKLKVDD GQWRTLVRAS AEDLVALFGI NCTHKSIAKL
AGALTSLIRM DAVGFKDVCE ELLLIPVRYY QNTDKETANM RSILQLCNLL VLKGHLIKFH
GVQYLIHCTM QHLLQFTLPG TDYILEEIAV FTLFSAELMI HEVPYIPGDL ESGRYFGKEV
LSELYQQFIV HLLENYRPQK LQLKDLEYRL LLDRRQWYQL DDFQISPHAS HIEWLQLQGI
SNMLCSYYAF QHRHPVMDIS QVKRRRLSDT YNSFLLNSQY GISFATSCID SNPVSSQLLG
LQLAACVTSF HECPKYQLEE LLDAILRRFE NANLVGWCCL AMLPLCSQLD LVISETVLQK
LLKLTLPLLK IPTLSAVASA LISKLLDYQQ RTLTGSNMLQ QCYDLYELSD IIGPAVVSNE
SFRLWQSLHI YGGDFRGKDG SSAADRIANW LFAKLNTVSP LDESQNSFPH FLGWLAGCQL
KDAYEVNRAI HVNSYCLEWE YTSVERTFLL SIETSRRLSR NRTTPLQNMN YESSSISELF
YRILDKITSQ DDIEAYGWMC FGLQLIHHIR ELTYLVEYVN DLKKAICLRL GKMNFGNSQI
LLSCIRQTTS LPSCDILPLF FTEREIANII YTYKELKLTE VPEGPAEDDF AGPAKARHKL
YPLNHLYAGK QGFEIDYVVS FIIMCSDYET NGDAAEKVIE LFLQLARSLP TNLIFQALPT
LITYIGSNDR ENISEDTLLA LTEFTGSSLL TNEYNTSTLS ITYLSLFLKS ISRYWLSDTH
MPSLTADCND ILEWIFSRLG DSSCIGCEAI MAILDMTLHM LKNYNRSNSK FTFDKQHLFH
VLTTCLGRLP KFYICKVVHE LNSYVVRLGL KNQSIIFSEF AGLFDPPQRD AETAAYYSLT
LAGLGTISHM HLSNAILHVL PNLQHKHVSQ YALSFLKSVA GFHKLSGIRA LFHLCRFEIL
DIWSNKCAGL RDFSPIWNTA IFQFESFEQF INEYKHEVAA YYFAKLSPYH YLKSTLVNDD
KELPQLLEIS LQYAIPLAYI PGGIGDAIFD ICADQWSATN HTNVLKQQYL LIFDRLLHFA
DLTVFMEYFE SLQKVYTNSE LIHKMKKYTY NLHPKHLLSY SLRTALKVIH SKVLLGKLSI
QELRFLLTLN LQYLQESTLP DDRSQILRKI QIILVAYEQQ LEDASSVSDL LEILTDYLDD
PLLGNEVGAL IGSIVALGFN VKYTESLFLC IFAKLLPQLH EAKTANLSIL LNDISNTLTI
NNSNIIHGKW WHACIDALAG TSLFENTIYH DDSLLDTELL DHRALNLYSE ILSFLPPFTG
FPPNFVPKER VLRHLISQTT TFKLHDNFLL WKGHYIGMYH KFHGTIPQLA PNGPNQKLSI
DKLVKNYGLL NGIFELLEAI EKTTHARIKF ICQCINAVSL SHKDSLSTFT ADTQQFFGQL
SSKSVPLDLA LFFYMFPISN PSESMETFCR LHYPALTSDY SSWLVKLTMF ALDMLGRYIP
VVKCFEVLAT AITSRVEQLL NYWLLLLLYC DPNNGIRLLC TLISNIGLLK STKEGILKIK
YMLNLLLIVR SFHKLGYKEF DTIYDRISLQ DAYKVAAEVG EKYIACLLFE EFHMPNLARL
DVTYMKEIYK QFDDVDMIYG IPTTASLASA IELINQTQAT SLKSFMMNNG NFDAQYATHF
TGNIGNLVNS ASNNGFTGLA YALQNISSSK NTSATYNWCI ELDKWDLPTP DILDSTAKSI
YSIIKKTDIN TGTAEAAFKS TMLNALQFLE KTGVNEDNVS QLGSIVTMVQ LYNNNAEKLV
KSLHAQDRKI LKVKDFNDYY MDIKVRHVFL DHLIDSHKNR LSEEQSICLR FASICELSHL
SEVARGASDF QRSLDAVLLL EKSVLALPTN SSVEHYGLFK TFARRMSTIQ SAKMLWSQNE
TVMSIDMLKD LLHTPLSSNL IARARKQPFF QQMAILDINV KAQLVQWLSH SRQDVPERIF
KNYIGTSLQD IENYGDNPSR TEIVHTFGKF CYDQAKRFSE TNEVDIMARR VSKNKEELAA
LYQLYHDRSL PERERKEAKR HYARLLVRNQ QETETYNQLR DQRELFVTNA LLFFTQTLQY
DDLYDGEVID QFCGLWFEYS NDDNVSGKLL SNLQNIPEYK LLPWINQMAS KLADDESPFQ
KTLRAAMVRI LLKLPYDSLY VLIGMSLTGS RQNAKDSGSQ SRLVAVESLL KEVSKHDYGS
YATKYLLPVR EFCEMSVSLA SQKFAQNTRK IHLNNLKIGT YWLKELKGRK LPLPTAQSRV
SDRCGNSVSR SYITQVDPDV RIASSGLSLP KIVTFTLSDG TRHRALLKAG NDDLRQDAIM
EQVFKQVNKI LTSNKRTRKL KLRIRTYEVI PLGPQAGIIE FAPNSKSLHE ILAGYHKDDT
ISLEQARKAM KAVQGKSKEQ RIAVYVKITE SVKPVLRNFF YETFLDPEEW LLAKATYTKG
VVTNSIVGHI LGLGDRHLNN ILLDKFTGEP IHIDLGVAFD QGKLLPLPEL VPFRLTRDIV
DGFGVMGVEG LFRKNCEKVY GLLRKERERV MCVLNVLKWD PLYSWKMTPL RRQKLQGKLV
DGDSPSDSLV TSLPDSSDND ESRRALKGVE DKLLGNGLSV EATVQELVHR ATDVSNLAVI
FMGWSPFY
