(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 111.
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}.
DR   EMBL; AE016820; AAS54204.1; -; Genomic_DNA.
DR   RefSeq; NP_986380.1; NM_211442.1.
DR   STRING; 33169.AAS54204; -.
DR   PRIDE; Q751J3; -.
DR   EnsemblFungi; AAS54204; AAS54204; AGOS_AGL287W.
DR   GeneID; 4622673; -.
DR   KEGG; ago:AGOS_AGL287W; -.
DR   InParanoid; Q751J3; -.
DR   KO; K04728; -.
DR   OMA; YEVIPLG; -.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR   GO; GO:0000077; P:DNA damage checkpoint; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0016572; P:histone phosphorylation; IEA:InterPro.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR   GO; GO:0010212; P:response to ionizing radiation; IEA:InterPro.
DR   GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
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; 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;
DR   PRODOM; Q751J3.
DR   SWISS-2DPAGE; Q751J3.
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          2443..2768
FT                   /note="PI3K/PI4K"
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   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
//

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