ATM_ASPOR
ID ATM_ASPOR Reviewed; 2925 AA.
AC Q2U639;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=AO090120000393;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007166; BAE62976.1; -; Genomic_DNA.
DR SMR; Q2U639; -.
DR STRING; 510516.Q2U639; -.
DR PRIDE; Q2U639; -.
DR EnsemblFungi; BAE62976; BAE62976; AO090120000393.
DR HOGENOM; CLU_000178_8_2_1; -.
DR OMA; HACSVIR; -.
DR Proteomes; UP000006564; Chromosome 5.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016572; P:histone phosphorylation; IEA:InterPro.
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; IEA:InterPro.
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; 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; 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..2925
FT /note="Serine/threonine-protein kinase tel1"
FT /id="PRO_0000227697"
FT DOMAIN 1844..2467
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2571..2882
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2893..2925
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 172..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2577..2583
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2749..2757
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2769..2793
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2853..2879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2925 AA; 328517 MW; ECE656F9A991F45E CRC64;
MAEITLDRTL VLLSSEKQRE RSEGLAVSLF VLIVVFVIDP CISSRSSLND KACHKIFESL
FRFISSEKSL YNRGNSKGPS ASRLSTCASV LRLAVDALLH NLRAKSVRAV VDHITETLQD
TGGSLFELLG VDYTKCLTAL LNYPPHVEHL GASEWEKLMG FCLKIMNTQD YEDDRSHTGS
DSRSTLDDFL GTGGTPTPSR SMPTLTAREK PKRDKGAISE AVVCIQLLTA SVNAPVQEPA
AKILHGLVGY VKSSHITGSG HQSAFNSINS VIMRVLSDQS ELVQSILLDL IPVICHLWAT
KLVGLKDELL VTIMLCIVLL TAATRQEPSE LLSRYTEDLL GALYKEYIKR PEKDILQVDE
LVFHQKTSAA VDKILIWPRL ESGKSEHNWT VIWAIANLVD LSEEITARSS SPRTSTETLN
KRQRLTSMVD EIHRDCASSS GARRVCALQL IPLIPRHHAS VDSKSSLLLR LLPNILDENG
ILASWTMITI ASLAGSPNAD SPSLRAIWQQ AWELTCRAST SQATSRASCI LMNSILEYNL
LEYSIVAEAT SSMLTSVNLN GPSTMSDASL TLWATTTRMT ARVNPGSLPN ASKQICAWLR
EVWVIGTVTD RTQLAQLAAF ARPLDLLNLL LACTNRHYIP PKPQFRGATS LIAKGWHFLH
RSKQLLNYLF QLGGILDFDM WDTDDTIHLE TFPRQDPNDN MVLDLLQVKS EMFLQAFQSL
YEDKSHHVTV EIVQIVTSFC ILVALYTECL PHLSASKFHN LQQNCERLWE IICTFLASHE
LEFIQGCLVV LSPFLNPEQF SYNPESTISK ALLRLVIPLV SLLEAYRRSQ RDNLALHNDE
PMDLDDTLFN SKDRLAEVTS IVKSNREALP LFQEFSSFQR CITIQLSVLQ KTNAFLRNHD
QHSSRALVEY LIDLDEVDIL AASNSLPYVY RAISGMDRTS LLDILEDLAE KCLQTYELER
CEASHLLCIH MMHSFVKAWV SSEADSLSGS ASDIYTWFRD VLLAKDMASP SVLVVFSELL
VDVINTNASY SSGESNTSPR TSLLKILEKG SIPVKFDVGN LIPRLFGHYS LNDHDAIFND
VLRHLPKESD WVEGIALRLF ILGQLASRWH TLLRRSIYHM FETPAHVPHS LQYAEKCICD
VANKLGLKDA KELFRLFSSQ ILYTWTEQES ITAMPFSIFS YASIKDMLGD VQDELVGQII
MRAREDEEIE MSKYMGKPFV DLLATSFYKA EAYSIARDIS TPPGQGSQPK GVETRLKKIL
GTEQFMELID QQFPQTIAAF FGSLDQYEQV ERALSKRAKF HDALDGLRCI LGKSASKIVL
PANQQPSFRA RYLIDELEFL CKRSGYELET IWTPTLASYV CRTLLESIHP ALGSFHACSV
IRKIRVLLCV AGSVMLRDYP FEMTLHAMLP FLVDIYCSED ALGIFWYLLE AGQPYLAETP
GLMAGVAVST LLSLKKFLAS PPVDTAQQGQ SKIVTANIER FLQWFGEYIN TYESSLDAET
QESFRRVVKS SQATSTVESH SDDSNERDVI LEILDDRSSE RSLLSKTVSD HVIALLCADS
EEPLGNYHKL NESDRDATAN IVAIYQTLQS FNTGSGYRLW AAKVIGRAFA TTGKVCDALL
REQDLSLFKS QLSDLRLEVH CYSKASILQE LCNMLQNNSH LEVGLVERTL QLIISNLARY
PDFEQCAGVV PLYLMKAFTW DPYQCPPIPT LAPETERDDA KVNWQTSNSL SQWARGIALF
LSKSAAEDPV IGSLSHIIYV IPELAVRILP YMLHDVLLAE LKGEANIRQK VSQIFKQALC
DVHDTTISHA RLAIDCILYL RNQPKPNEAT IVERDEWLEI DFAEASLAAS RCRLPKTALI
FLEIHASRVI FGSRRSSLAK YEAPPDMLHD IFKDIDDPDF FYGIQQSPSL DSVMERLQHE
SSGFKNLLFQ SAQYDSEIQM SADQNAYGVL KALNSTNLQG IANSIFSASG GGFVDTSSSF
DSMLQAATNL RQWDIPVSPL NPSPPATVFR AFQSLNTSGS LAEASKSINE CLLTTLESLT
SASRSAMSLR TAMRVLGVIT EVSDVLDARS TEEIDHEWQK IAARDSWLKT TSVHEIGEIL
NSHEALFSSI NRKSYLRSST NISDHDAQLL EVKAIRQSLH ITRTQGIQQA SLKSAVYLSK
LAHQCSALGI NIEGAAKFDL ANVLWDQGEM TASIRMLHQL KDQNDLHKQA VPISRAELLV
TLVSSLHIDS LRTKPCSFRT NSTSCKGHHV AEARLEKPET IIQDYLLTAV KELKGRSGGE
EAGRVYHGFA TFCDQQLQNP DGLEDFTRVE QLRNRKEKEV RALEDMMKAA EGREREALKF
HRGRTKQWFD LDDREYQRLR RSREAFLQQC LENYLLCLRE SETYNNDVLR FCALWLDKSD
SDIANAAVSK HLGQVPSRKF APLMNQLTSR LLDVPDEFQK MLFSLITRIC VEHPFHGMYQ
IFASSKSKGG KDETALSRNR AAGRLVEGLK NDKRIGPTWV AVHNTNINYV RFAIDRPDEK
LKSGARVPLR KLQTGGRLEQ DAATQKLPPP TMNIEIRVDC DYRDVPKLVK YHPEFTIASG
VSAPKIVSAF ASNGLRYKQL FKGGNDDLRQ DAIMEQVFEQ VSNLLKDHQA TRQRNLGIRT
YKVLPLTSNA GIIEFVPHTI PLHDYLMPAH QKYYPKDMKP NVCRKHISDV QTRSFEQRVR
TYRQVTEHFH PVMKYFFMEK FNNPDDWFSK RLSYTRSTAA ISILGHVLGL GDRHGHNILL
DERTGEVVHI DLGVAFEQGR VLPVPEVVPF RLTRDLVDGM GVTKTEGVFR RCCEFTLETL
RRESYSIMTI LDVLRYDPLY SWTVSPLRMK KMQDASEAGG GPPMLPGAAD QRPSNEPSEA
DRALTVVAKK LGKTLSVTAT VNELIQQATD EKNLAVLYCG WAAYA
