ID   ATM_ASPFU               Reviewed;        2796 AA.
AC   Q4WVM7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   02-SEP-2026, entry version 128.
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; ORFNames=AFUA_5G12660;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; 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   -!- SEQUENCE CAUTION:
CC       Sequence=EAL91349.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000003; EAL91349.1; ALT_SEQ; Genomic_DNA.
DR   SMR; Q4WVM7; -.
DR   STRING; 330879.Q4WVM7; -.
DR   EnsemblFungi; Afu5g12660-T; Afu5g12660-T-p1; Afu5g12660.
DR   KEGG; afm:AFUA_5G12660; -.
DR   eggNOG; KOG0892; Eukaryota.
DR   HOGENOM; CLU_000178_8_2_1; -.
DR   InParanoid; Q4WVM7; -.
DR   OrthoDB; 381190at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
DR   GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   CDD; cd05171; PIKKc_ATM; 1.
DR   FunFam; 1.10.1070.11:FF:000025; Serine/threonine-protein kinase Tel1; 1.
DR   FunFam; 3.30.1010.10:FF:000019; Serine/threonine-protein kinase Tel1; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR038980; ATM_plant.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR063142; HEAT_Pincer_Tel1.
DR   InterPro; IPR063223; HEAT_Spiral_Tel1.
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; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR   PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF30717; HEAT_Pincer_Tel1; 1.
DR   Pfam; PF30718; HEAT_Spiral_Tel1; 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; ARM repeat; 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..2796
FT                   /note="Serine/threonine-protein kinase tel1"
FT                   /id="PRO_0000227696"
FT   DOMAIN          1740..2337
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   DOMAIN          2441..2753
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          2764..2796
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT                   ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          139..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2447..2453
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2619..2627
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2639..2663
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2724..2750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2796 AA;  315100 MW;  02AE740706AC29E7 CRC64;
     MCVIQRLTYA YLIRTSLNDK ACHKIFESLF RFISVERSLY NRASSKGACA SRLSACASVI
     RTAINVFLRN LRTKSIRAIV DHITEILQVP GEGLWEHLGA DYLKCLTTLL RYPPHLEHLA
     ANEWDKVLNL CLRSIGAPED GDSQSSDHNG HPSTLDDFLD ASSRSTPSRR TSSLALREKQ
     SGDKRIVAEA IVCIQLLTAT PTAPVQVAAE KVLRGLGTFL KLSPIAGSEH QAAFNSINTV
     VMRVIFDQSD LVRMFLLDLI PVIRHLWSTK LMGLKDELLV TILLCMIILT DATRRAPTDS
     LALSIENLLD TIYSEYTKRS EKDILQIDEL IFDRTSFTQI IDLALQPRLE VPRSEHNLTV
     VWVMAKLMRL SEESTAQLSH PAGETPSKKQ RLNSASDQVF RDCVMSSGNR RVCALQLIPI
     LLQGRLTMES KASLLQRLIP YILDDNGVIA SWTMVAISSI SDSSLELWAI ITRLCAQTNP
     GSVSNASKQI CSWLREAWVI GTVTDRIQTA QVAAFARPLD LLNLFLACTN RQFEMPTPQF
     RGPSGIVAKG WHFYQSNREL LHYLFHVDGM LVPSSLHGRD DCISLQLATR KDHNDDIVLD
     LLQAKSEMFL QAWRSVSDSK SHHVTVDVVQ ILASFCIVAV LYTECIPEQL HTQIKDLRGN
     IQQLWDSLCS FMASRELVFV QYCLELLCPF LPQGGRVGFE KSVVNSSLYR LVSPLGAILE
     NHRQDQKRLL SSDEEEPMDL DDQLLQSNDL LAENMCIINS NRESVPLFHD SATFQRSMTI
     RLSIFNIAYG SVVQPDQPAR SALVEYLTDL DEADILSSKD FLPDVYRACA GYERTSLLDL
     LEDMGEKCLQ TYQLERCETS QVLCIHMLDS FIKSWTTGDG DHLSDSASDI YNWVTDVLLV
     NGRASSRVSI AFSRLLEEIF STNPAYTSGE SNPSPRTTLF MILQESDILT KYNVGNLVPK
     LFRHFPLKDH DAIFDDILES LPRDPDWTEG IALRLFILAR LASQWHTLLR RSIYHMFETP
     AQLPHSRWHA EKCIRHVASV FGLEDARQLF RLFSSQILYT WTENESVMTM PFSIFGYSTL
     EDMLSDVQDE IVGQIMMRAN EHEASELSTR LKIPFIELLA TSFYKAEAYS IARDISTPPG
     QSSQPKGVEN RLKKILGADR FVSLVEKQFP QVIATFFGTL DQCEQIERAF SKRANFQEAF
     SILKSITAKG ASKEILPPNQ QPSFRARYLL DELEFLCKRS GYELETIWTP TLASYVCRTL
     LESIHPALGS LHACSVIRKI RILICITGPV MLRDYPFEML LHALRPFLTD IHCSEDALGM
     FWYLLDAGRS YLTENPSFTA GIAVSTLLSF RKFLASTSAT MQESESVAVL TIVQTFLQWF
     EDYLKSYESP HLSPEAHAFF QRLMESSRRI STPDKELDGT EECNLLLEVI QDRNSKTRLL
     SQSISDHILS LLCASFKSAP NYHQGLVERG YDAIADSVAL YQTLQDFSPT KEYRLWAARV
     IGRNFAATGM ISDDLLREQQ STLFEPRMAK LSLHMSCQSK ARILQVLCSM LQNSSPLEVG
     LVERTLQLIV SNLAGAPGFE NYEEIISPSL LKALIWSPYQ CPSIPLPASQ TKNHDTIVRW
     NPGISFAHWA RSIGLFLTKA APQDPVIGPL RNILHVIPSL AVRILPYILH DVLLTEPDGV
     ANVRKTISDV FQQGLHEADA HSIPHVRLII NCLLYLRNQP RPQEATIVER DEWLEIDFAV
     ASRAANTCGL PKTALLFLEI QASRAVSGSR RSSLVKYEPP PDLLHDIFRN VDDPDLFYGV
     QQSSSLESVM ETLEHESSGF KNLLFQSAQY DCEIQMSGDA DAHGLLKALN SSNLQGIANS
     LTSTLRGSKS SVSFDSMMQA AIDLRQWDLP VSPMNHSPSA ALFRTFQSLN TSTSLVDVSN
     SVNESLLAIL GSLGSTSRSA MSFRAAMRDL GIVTEISDVL SATSLEELSE EWRKIAERNS
     WLKATSVDEV GEILKCHEAL FSSIKTRDYL KSAVGLSDRD AQLLEVKVIR QSLSITRSHG
     IPQVSLKSAM RLSKLADLCV VQGINVEGAT KFDLANVLWD QGEMAASIRM LQQLDNQGDL
     HKQAIPISRP ELLVTLGHHV AEARLEKPEA IIQGYLGPAV KELKNRSEAE EAGRVYHGFA
     TFCDQQLQNP DGLEDFRRAE QLRNRKEKEV LGLEEMMKNA EGKEREALRH YRTKTKQWFD
     LDDREYQRLR RSREAFLQQC LENYLLCLKE SDMYNNDALR FCALWLGKSD SEIANKAVSK
     YLNQVPSRKF APLMNQLTSR LQDTSDEFQN MLFALIFRIC VEHPFHGMYQ IFASSKSKGG
     KDPSALSRNR AASRLVDCLK NDKRIGPTWV AVHNANISYV RFAVDRLDEK VKSGAKVPLK
     KLLTGQRLEQ DASTQKLPPP TMKIAIRVDC DYSEIPKLVR YHPEFTVASG VSAPKIVTAV
     ATDGHKYKQL FKGGNDDLRQ DAIMEQVFEQ VSSLLKDHQA TQQRKLGIRT YKVLPLTSNA
     GIIEFVPHTI PLHDYLMPAH QRYFPKDMKP NMCRKHISDV QTRSFEQRVK TFRQITEHFH
     PVMRYFFMEK FNSPDDWFSK RLSYTRSTAA ISILGHVLGL GDRHGHNILL DERTGEVVHI
     DLGVAFEQGR VLPVPEVVPF RLTRDLVDGM GITKTEGVFR RCCEFTLEAL RQESYSIMTI
     LDVLRYDPLY SWTLSPLRMK RMQDAQEAGD GPPMISGAAE DQRSANEPSE ADRALTVVAK
     KLSKTLSVTA TVNELIQQAT DERNLAVLYC GWAAYA
//