ATM_GIBZE
ID ATM_GIBZE Reviewed; 2935 AA.
AC Q4IB89; A0A098E3B7; A0A0E0SQA2; V6RHT9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=FGRRES_16493, FGSG_05519;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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=ESU11490.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231665; ESU11490.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HG970334; CEF88615.1; -; Genomic_DNA.
DR RefSeq; XP_011324066.1; XM_011325764.1.
DR SMR; Q4IB89; -.
DR STRING; 5518.FGSG_05519P0; -.
DR EnsemblFungi; ESU11490; ESU11490; FGSG_05519.
DR GeneID; 23552698; -.
DR KEGG; fgr:FGSG_05519; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G18115; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_8_2_1; -.
DR InParanoid; Q4IB89; -.
DR PHI-base; PHI:1224; -.
DR Proteomes; UP000070720; Chromosome 3.
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: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; 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; 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..2935
FT /note="Serine/threonine-protein kinase TEL1"
FT /id="PRO_0000227703"
FT DOMAIN 1866..2468
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2573..2884
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2903..2935
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 191..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2579..2585
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2751..2759
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2771..2795
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2857..2889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2935 AA; 327890 MW; 18DC4B74BEFB083D CRC64;
MASHNVMNLA RDVKSAAVRD REKAVDELSH LLNPRNRSTN LSDLGDKSYH EIFEAIFSFV
LREKPVLSDR KKSQATLNST ATRLSKCAEA VRMTVGRGNS KIGRKTLLAI VDHITQVLPG
PNGDDFVTPL LQDYIKALTE VLSRPAHVEI LARKGGQHWE TCVGFFLDVA QYLLPDEADI
STLSLARASP ALTRSSPAPG SGYSRSGGRS TPSTQSQRRA APGEGGLLKD VLEGLHYIVI
GGNAPILRQY KDITLVVLRV LSLKQLSLGS LQTLAFAIIN TVFTTTNADD LAHASSVVQS
ILPLMSYWWR CEKVSQDEVI RALRIEISRS IFLMHLHIEN LVINSSDEKI RSDLEELTEN
IWSEYSRRSE AFRLQMSDIT FALSSLPTYG LQLNMFGLRA HNVYGEGHWA VIQNLAFLEG
IMLLPQSRTP ADDAEQSEQR RKRRRIEQDM SRIRLKLKTV EVGVRGTALQ LIPFLLADNS
LSRDELVDLL PELALLATDK NPVTASWALI ASASCISKPE VCHDQIDVWR QLWHFATRSV
SLPGTSRAAS VLLHAILEAD VLPYHTISQD INNMVTTADV NGPSVLCDTS ISLMFHVLQL
RNARVPSASQ STCHHIIRWV FLRWNPNEST FASYHSMHAQ PIQLVNLIRA CCGTTALELN
SHQAAPGGPL TETWSSFKQT EKFTRYVLLA KDEFHDADPI GCCDLSEQSD PASLVDANSR
YASRKLTLEL FYPKLSELSD LCTSWNKKPN EGGIQISFDR FQSLLSACLA GTLLLPIFGD
LNSTQSSSVD STLKYILDKA LNSALTSVEP TAFVDSVLRV VRAVMPDMIT SSLNRIQANN
PDLFHLFGRI WKSIGQQKDQ TDPDNNIDLM DIDEDFDSQS SRASSVHAPV AAPRFNIQMK
LDMQTFYIET KARLRFLSIL DSDFGQIGLV PDTYVDHLIK MPDEDLLMCQ SLLLELFGSD
LVITPENALS IIERLGDCIS LSEYQCAEVA LSTCIGVIDG LHSIWLNDKQ HLSERVGDLY
YHFIKVCLTS NIFSPGVQMS MVQLLFTLLR TNTEYGKDQG LDSPRTCLLY ILKNGPMSVK
YTISQKIADI FDLFVLKLHD EVFVDVLDSL PTDPLDTTGI AFRLLVLSNL ACRWSTLLRR
CTYHIFETPG KIPRSTDYAT RCLVNVSRTL NLESPKALFR LFSRQLLYTW LEYDHIEDIP
FSIFGFKTLG DLLKSAQSEA IGLTVMRGQD QTFAEVCHLL GSSESDLVRE NFTTAVAYSM
IFGDSNGGDD KERGEAHVKR LLGRAAYMEL IYINFVDIAA LFFDLIDQEN SFERVFARFK
LDYAGQILSA VKAISHSPAE LPANQQPMFK AKYLINELHR LCQNTEFQFH DLWTPPVVVS
IARKLLNTVH PALGPLHACS VLRKVRVLIS LGGSVALESY PLEMLLNATR TFITDSECAD
DALGISQYLL AEGARHLSNV PSFLAGYALS TLASLRVFLE SSQSSTTQES QFKATMSKAE
KFHVWISKYL EEYESPMFKN LEQRSAFKSI TRSAARIRSS GNAERGTAES KLLLDILADQ
AADHQLLNEP SRQLALGLLC GDFSIPETIK DDVIESDEDA LKYSTAVWKS CDTENLSEEY
LSWAGRVVGR AFSASGEIPT GVLRESNLSQ YQKMAPGSNG SETGILYLLQ DLTSNPDSIT
AGLAEAALRS IVSDANNLDD ELLAVACQKS LTESLLVTSQ WGTHRSPPSD KGLITPTSSP
NQLDVWSTDI TSKDWLLNLS AHLARYVPES IVLSVLAPIL ARVEHFAERA FPFVVHLALF
FTRNQQHSPK RQLSVAIKSW LECTVTEAKE NQKLLINMLL YLRTQQYPKE SSIADRSHWL
EVDSALVAAA ASRCGMYKTS LLFVEYVPPE TSRSSRTSSA ATKEVDMSET LLAIFENIDD
PDAYYGLPEE PSLSKILARV EYENDGPMSL AFRGAEYDSN VHLGNPMAQS DGQALVRAFS
TLGLSGPSNW FLQTQDNMET SPPVLEDTFN TARKLGIWNL PAPPSDHHAV TVFKAYQSIH
QATDIANVRA AVHDGFGRTM SSLVVHSLNA TALRKRLGAL ASLTELDDVL GVSDSSEMNL
LIEKFKNRSG WMRSGLYESV GQILSCRSTT MSMVSQQETL RTNIKLSAAT ARQMEVESMI
TASQIYRYHQ ATQESLKIST ILTKLIPSCT ALDLHVDAAV TIEAANSAWD YGQMSTSIRM
LQDIDKDSVL EKQTLPVSRS DLLSKIGYQV SVARLEKPHD IQKNYLEPAL KELKGKGQGR
QAGSVFHQFA MFCDQQLQDP DGLEDLARLQ SLKKAKSDEV SELKTLISGT RDTQLKTRYS
HVLNKEKQWL NLDEQELRRV EQTRSEFVRL SLENYLLSLI ASDEHNNDAL RFTALWLERS
EEESTNQAVM RHLSEVPTRK FAGLTNQLTS RLQDNNTTFQ KLLLELVYKI CVDHPYHGMY
QIWSGTKAKA QQKDDVAVLR VRATDRVAKS LAETQSVANI WLSIDKTSKY YHALAMDRNP
NKYKSGVKIP LRDSTPGHNL VNCLAKYRIP SPTMHIELSA TKDYSKVPII SKLEPTMTIA
SGVSAPKIIT AVGSDGVRYK QLVKGGHDDL RQDAIMEQVF SAVSSLLKLH RITQQRNLSI
RTYKVLPLTA SSGLIEFVPN TIPLHEFLMP AHERYYPKDL KGSQCRKEIF GVQGRAVATR
ISTYRRMTEK FHPVMRYFFM ENFMDPDEWF LKRLAYTRST AAISMLGHVL GLGDRHGHNI
LLDHKTGEVV HIDLGVAFEA GRILPVPEMV PFRLTRDIVD GMGITKTEGV FRRCCEFTLD
ALREEQYSIM TILDVLRFDP LYTWSISPLR LAKLQKARHN DDSPMDDEQS EAETKKGKKA
AGHVNEPSEA DRALEVVRKK LSKTLSVTAT VNDLINQATD ERNLAVLYSG WAAYA
