ATM_ASPFU
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 03-AUG-2022, entry version 114.
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 Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
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=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}.
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 RefSeq; XP_753387.1; XM_748294.1.
DR SMR; Q4WVM7; -.
DR STRING; 746128.CADAFUBP00005895; -.
DR GeneID; 3511168; -.
DR KEGG; afm:AFUA_5G12660; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_8_2_1; -.
DR InParanoid; Q4WVM7; -.
DR OrthoDB; 80538at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
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:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
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; IPR016024; ARM-type_fold.
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; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR InterPro; IPR021668; TAN.
DR PANTHER; PTHR11139:SF72; PTHR11139:SF72; 1.
DR Pfam; PF02259; FAT; 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; SSF48371; SSF48371; 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; 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 139..175
FT /note="Polar residues"
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
