ATM_CANAL
ID ATM_CANAL Reviewed; 2873 AA.
AC Q5ABX0; A0A1D8PQ18; Q5AC91;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=CAALFM_C603010WA;
GN ORFNames=CaO19.13026, CaO19.5580;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017628; AOW30232.1; -; Genomic_DNA.
DR RefSeq; XP_719142.2; XM_714049.2.
DR SMR; Q5ABX0; -.
DR BioGRID; 1222167; 1.
DR STRING; 237561.Q5ABX0; -.
DR PRIDE; Q5ABX0; -.
DR GeneID; 3639263; -.
DR KEGG; cal:CAALFM_C603010WA; -.
DR CGD; CAL0000195481; TEL1.
DR VEuPathDB; FungiDB:C6_03010W_A; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_8_1_1; -.
DR InParanoid; Q5ABX0; -.
DR OrthoDB; 80538at2759; -.
DR PRO; PR:Q5ABX0; -.
DR Proteomes; UP000000559; Chromosome 6.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; 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..2873
FT /note="Serine/threonine-protein kinase TEL1"
FT /id="PRO_0000227698"
FT DOMAIN 1830..2425
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2530..2839
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2841..2873
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2536..2542
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2706..2714
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2726..2750
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 2873 AA; 328078 MW; DC599311ED219947 CRC64;
MSTSDINKTI ALLQSSKIKE RNDALNNLEN IAASKFRLNP KQFRQLTQAI LALIKHESQI
YFNNKSTTVD SRLSQASYNL RLLTEKSIED TRIDFKYRTY LDLCMGIKDQ FFVHSELLEP
CSIDFIKTIT SILNLSYVKE HLNRKEWSIL YIFLVSLINN ILDDCEGSFS NNGNNEKLLI
DLYTALQNLL QCESSVSINY LQLYDNDNYF KLLRILDKTS ELLKKENVII IIIFRIINKL
ITVIATEKFK FVNKLIKIGI RLMVYFHHSH WEKLQEQFLI FINLPGTHDL INLHNLPKLI
GDRYILSEIS TQEDGDSINS QADNQDEVFL YNLGVLIHHL MKKLMSGSFE LKTEDIGMCT
INNSITWFNL KTIYSDSQNY KPWLLTLGVS RLLKSYYDLK QFINKQSNDP QTSLLLYSNG
SPNKNKRQKL GSIADTISDS NSAIELCNKL IHSKESSDNQ VLGLKLLTFY LELYTFEKPK
EQSTESDSMD TTIGENTTFD FVISTTDNTF IDKNVVMKNI LITFDDNSMN FWSSLCARSV
LLDEILQSNH GGFKFKKSFS IQLLKLSLLL LKEPEVANIA CNIIFKLVFE QKTNLSELID
DSVIIQLETL IDLSEINGPY KITEESFQFW YAINKLAIEV NLSKKNFLGR RIQDWMLAKW
DITFSPGADF VSVGSSLANF IYWLSGNSIS YSPTTTQKST YEGDIYEFYY FAQSYDSLEK
FLCLKSVSDS SETIKFDIIS IASSDRIDAI LNKVNSTFMV FDRSSVTSGS LFCWIIVLSN
IVAKVRSMKF VTHELTGLQF QLSAGLNSFK DITLSCEEII DVMEMVNKFL PTDPDTIQIF
IQNFPSEKLV NIIKFDYPGL ADKDNRKSVP EDGFGWEFSR VRDATTPPST TSTSTISLAK
LNYKKIQSLE VSKFIMFTAD IEGKLQSDIL TAFLNYVETL ESDDFLPSLL FVVENIFTDH
SAHFIDEIQL AKLLRIINEK LLSTQNYERN EFVSVVISRF LSATAQVWIN SSDNSLASDF
YSLVSRLYSS GRDDLILTET SIVEYCRFLA HFITHNDERV LSNTDIKNEL LEKFSKSPNN
IKDRLANSFG ELVSLSTVQQ QGQIYSDLFD RFVNPEQSVE SAGTYTKFFT NLSQSSLHIL
RLALFNLLEC SRFPFFISYL EICLKEFCMI MKLDNANKLF KIFKFEILRN WWKYDSIDAF
PFVLFSYTDL SSFYRDNYRE LIAVALSTKS RSPEISNAFV EQLADLKQSH SETLVAESLS
IIVPLSYSKD GVRNDVFQIL LDYLKNSFKQ EFIDKLPLIV LEIIKFTEIS NEKSFESLGT
DGLVTMLLND TGFSSTIQTA GEMVISFDSS VQLLKKLVEK YHQPEHETFW SSRQIYFLIR
RLSISLKLAT TFEQKVIFLR KFKFVLVLGG KKSIDYAVSR LLVDTLCPLL SNEPKMSADV
FLILQSLTDV YSHRYTYDKS ISLIIQIINS LLETEAVDRS RALLDCIDDF VNTGDQDRAI
CQLLKSSVAI LKGQAVEIES SLIELCLEES GPDYIKQMIL ISRIFGNVVF ATTHSGSKLP
VVEKLLALSK NQIQEFSDGY KLWIANYLSD FYIEGGCKEQ IKALTFDEYE GIPVNDFENE
VRSFDFTLKS IEQYIYKDDF EAAACAESII GVLIRKYETS KREVSKFLNF ETTLEKHSDS
ILPIDFHTCV ILNDKADVEY LGDELIDIIN NFESFLSNGT ELWCTKLYLA LLQELAVETS
IAPLLSTFVI MVPEFAKTSL PVLVCNYLAI KRTHSQDRII SLLNEFLHTS KKSESSIKVF
LQILILIRVG AKIFKKPVFA NVFAKIDKLK FYQLACEVKQ FKTALMLFED VASDTNSDVH
LQDHYQTLQH VYESLDDDDL VFGLPERTTL EYSISMINRV GNSDDRLRFS SAGFDTDMIL
NQEPSYSNIV GSLSAAGLLG VSRALSKNTS FASNDDSQYE WSWKLSKWDL PISKNATKEN
EVIYKTLKQI HDFPMNSQDI CSSSLLNAVD NKVSATNMSV KEFKQEGINW LKTISTVASI
AEIANATGDN IIPMTNQFSE KTQWFGEVEF SMFENLLLAR QTTFGLINDR PISSLPSDTA
WMGALCDLVR YNNLARTNGE YQKMVTSTML VDVVSKKLQS SSLDMVAFNA NNLASFQTAQ
TLWCQGNTNV PVMIMKDLYA AGGIDMSENI LKVDKCLIRA MMVDWMSQSR QEVASSIMEK
YVMPTEELSN HMIDLQQQSK IFSILARFCE EQYKFKSLSE KISKLEKRVL NKENEIKDLK
KQYEKVTVTH AEQKQVQQYY NRLKKQFVSE SKDLESLRKS KQLFSSKAVQ YYMKSIIVDD
FEEENLDKFF SLWLEQSGNN ELNQSIQSNL LALPSYKLVS WCTQLISRLS NETNNFQILL
KKLIINMCLD HPHHSLYLLL SLKKHKPNTN EVLNPSLLSR CAAAQAIWDQ LLLQDHRYIS
DVLLPIDGFT DQCITLAAYK VSKGKSIDLT KFSAGDYWLN ELPAIPPPTE TIRVDPSKQY
KNVPVLHSID KKISIATSGL SLPKIANFIL SNGTEHRVLL KHGTDGIRQD SIMEQVFNKV
NNIFAKDREC NKRGLTIRTY NAVPLGPLSG IIEFVPNSMA FIDVISGYHQ MHDKISYDKA
REMMKSCQSG DKQKRIHSFE QIEAKIKPVM RYFFQETFLT SDSWFESRVK YTHGIATSSI
VGHILGLGDR HCNNILIDRS TGEPIHIDLG VAFDQGKRLA IPETVPFRLT RDIVDGFGVT
GVEGMFKKSC EHTLRVLRTN KEHIISILDV LRWDPLYSWT LSRFKKRKLQ EDETGPGVQP
EEEGSEAGTA IMTVIEKLNA NGLSTEAAVR ELIQEATSTQ NLALIYFGWS PFY
