ATM_NEUCR
ID ATM_NEUCR Reviewed; 2939 AA.
AC Q7RZT9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
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=mus-21; Synonyms=tel1; ORFNames=NCU00274;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002238; EAA28509.3; -; Genomic_DNA.
DR RefSeq; XP_957745.3; XM_952652.3.
DR SMR; Q7RZT9; -.
DR STRING; 5141.EFNCRP00000000181; -.
DR PRIDE; Q7RZT9; -.
DR EnsemblFungi; EAA28509; EAA28509; NCU00274.
DR GeneID; 3873915; -.
DR KEGG; ncr:NCU00274; -.
DR VEuPathDB; FungiDB:NCU00274; -.
DR HOGENOM; CLU_000178_8_2_1; -.
DR InParanoid; Q7RZT9; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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..2939
FT /note="Serine/threonine-protein kinase tel1"
FT /id="PRO_0000227705"
FT DOMAIN 1869..2471
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2577..2890
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2907..2939
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 193..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2583..2589
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2755..2763
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2775..2799
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2869..2894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2939 AA; 328696 MW; A20726A7FE66C920 CRC64;
MAPATETVDF KKLIVTLNGK TITGRTSALK SLISYFKGDE TGSQAESHSQ KLFDDKTYHY
VYEALFTCAL TEKADYFSCL KSSKSDSVRN SCVKRLEGCA EALRLAVQHG AYKIKRKTAT
AIADHITQTL LDSDDNFFEP LLKGYVKVLS AFLNIQVNVE NLAAFGGEKW ESSIDLCLNA
ISRFLEAAEH DSGTSVRASP APGTPATSRA GSVGPLSASV QVNGQLAIEF LACVKALTSA
SNAPVLRRAK RISQLVLRLL TLRHIKLGEL QRDSFSILNN ILVRVQTESI ALTNTITTAL
VPVLSHCWQP RSLSRDAMST SLKDEMLKTL YGIHLYLESL LREATDDKLL QDTEDLLDSL
WSEYSRRDDK TRLQLGDVTF SAMQLHPDHP LTMVFGLRPY HLAGEQNWAL LENIALLEIV
YAKNSQRDRQ HLEDEPDKPR KRRRVIGSSN RIHQKLMSQD PAVQLTALQL IPFLSALKHP
SLEEVKGALV DLSQFISAKQ GLVASWAMIA CSSLAAHKTS RDPSLSAMWK QAWHIGIRSL
SLPSTSRSAC VLLNWILKAK LLSDHEIAGD VNQIITTADI SGPAMLVDSA PVLMLTLLRI
RNAIFPNASQ STSSHVIRWV FLKWNPCESA YASVHGVHAA PVDLINLLRA CYEMPPLRMN
TSLTVFDGPV AQFRAVQKQR HAMLRYLLLL EDEAPPEDSH KATSTDQPKR EEIRAADSSS
SHSAKRLILE LLFPKLDELL QMVELWHKRG ESDSAAPVST DRLVSVASTC IVGAFIMPEL
VGLNSSMSRD LEKTVFGIVE GMIKAIAESP QSEDFFNLVL EVSAPYIPTL GEAELTHFKR
EEPYALRLFA TVSNSLLEKT RRESPTDSDP ASMDLDDEFD SQETRKSTTA GKRFLSRRDI
TLKHTPEAFY LDTSLRLHLL RIIRADDGEL GRVPDPIVDH LLELSDEDLL SCRLFMQELF
ASDVVTPVDL AIRMIERIAA TISNNQYTCC EAAMCTVMDI MEGFITMWTD EELEISNLVG
DIYDHLIKRA LPNNSLSSTA QIWFSRLLFR LLEVNPMFAS QVLKLPSTRS TLLTILRDAP
MDVKFFIGIN LPRIFGMHVL QTHDDIIVEI LEVLPGEGME GIAFRLFVLA ELACKWPTLL
RRCAYHIFET PGKNQTSASH ATSCLKRVSR CLNLSSPQEL FTIFAPQILY TWLAIDSIDE
IPYSIFGFSN LAELLSKSQS EAVGIMIMRG HETDARELAK TLKLSIQELV TQNFSKIVAY
SIAQDSSLPN EVTGESRVRR IIGAEPYSSN IILNFADILA IFFEICDQEY PIEDSFRKDA
ANFAYAADIM DKIKAFGHLD TMLPPNQQPS YKAKFLKRQI LHLVKRTNYE LHDIWTPALV
VFVARKLLNT IHPALGPLHA CSVLRKIRVL ICLAGDTALY GYPLEMLLHS LRAFVVDPEC
ADDALGITQY LITEGSDHLI RFPSFLAGYA LSCLADLRVF LESSQSSTTQ ESQFKATKSK
AQLFHAWFSK YLANYTTNAW KDKTQKEAFE AITQSAANIR VMGNAEKGTH ESKLLLEILK
DWGRQHQLLN GPARSVALSI LCGSFNVPPP SRLDVIQSDE EALAHGAAVW MSCGSKKLSS
EYLAWAGRVI GRSYAASGDV PPELLRESRL QEYRKKSPVN FDFMESEEAL LSLIEALTAS
SDGFRAGLAE AALRVAVSDA LHENDRPLIT ACQKSLSESL LVASEWGELR IPRSDRFSVE
HPNETEIFSA EFLESPEWAQ QLTTLLAQSV PGSVALRVLP PILTKVKGFA EQAFPFIVHN
VLEYELDQTQ GMKQKLSEAL KEWLTSTSPA ARDNQKLLIN TILYLRTQAN PNETSIADRL
HWLEVNFSIA AAAATRCGMY KVALLFAELA STEITRQSRR SSAIQGLGDT SEILLDIFEN
IDDPDAYYGL TQDASLSTVL ARLEYENDGT KSLAFRGAQY DSHLRRRDVA SQQDGQALIK
ALSSLGLAGL SNSLLQTQQS LDGSSTSLDS TFITARRLEI WNLPAPAATE NWAVTVYKAY
QSMHQASDIN MVRSAVHDGL TKTLKHLTGK SLNTLTLRHQ LGALATLAEL DDVLNTGDLS
ELNGIIEDFQ ARSKWMMSGQ YDDVSRILSC RETTLSLWSQ RHNLRPARLT PANARLAQIR
GMLVSSDIYR FHRATQETLN LSTTLTDLIR PSEQMGLAVD AAIRMETANS LWDQGEMISS
IRMLQNIDKE SPLEKQTVPV SRSDLLSKIG YQVSVARLES PDTIQKNYLE PALKELKGKS
EGKEAGRVYH QFAMFCDEQL QNPDGLEDLA RLQNLERGKN DEVTQLKALI ASTRDSQLKN
KYSSHLSKAK QWLDLDQQEL RRVEQTRSEF VRLSLQNYLL SLAASDEYNN DALRFTALWL
ECSEDDMVNE VVKRYLSKVP TRKFAPLINQ LSSRLQHQEG LFQITLIGLV YSICLDHPYH
GMYQIWSGVK ARSIKNDEVA LSRQKATDKI ARAIKKSGAS AAKIYLAINA TSKVYHNLAM
DRDAKKYKAG HKMNIKDSKA GLEFLAAFAE FPIPPPTMQM PLLASCDYSQ VPMIVKFEPQ
MSIASGVSAP KIITAIGSDG RQYKQLVKGG NDDLRQDAIM EQVFAAVSEL LKHHRATRQR
NLGIRTYKVL PLTETTGVIE FVSNTIPLHE YLMPAHEIYY PKDLKGSHCR KEIMNAQSKS
VDTRVAVYRK VTERFHPVMR YFFMEWFPDP DEWFARRTAY TRTTAAISML GHVLGLGDRH
GHNILLDTKT GEVVHIDLGV AFELGRILPV PELVPFRLTR DIVDGMGITK TEGVFRRCCE
FTLDALREET YSIMTILDVL RYDPLYSWSM SPLRMARLQN VRVGAGEDDV VEAEDERRAG
DKKSTKNLNE PSEADRALEV VRKKLSKTLS VMATVNDLIN QATDERNLAV LFCGWAAYA
