ID A0A1L9RR69_ASPWE Unreviewed; 2895 AA.
AC A0A1L9RR69;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 43.
DE RecName: Full=Serine/threonine-protein kinase Tel1 {ECO:0000256|ARBA:ARBA00014619, ECO:0000256|RuleBase:RU365027};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|RuleBase:RU365027};
GN ORFNames=ASPWEDRAFT_58885 {ECO:0000313|EMBL:OJJ37318.1};
OS Aspergillus wentii DTO 134E9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Cremei.
OX NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ37318.1, ECO:0000313|Proteomes:UP000184383};
RN [1] {ECO:0000313|Proteomes:UP000184383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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. {ECO:0000256|ARBA:ARBA00025079,
CC ECO:0000256|RuleBase:RU365027}.
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 Evidence={ECO:0000256|ARBA:ARBA00048679};
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 Evidence={ECO:0000256|ARBA:ARBA00047899,
CC ECO:0000256|RuleBase:RU365027};
CC -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574, ECO:0000256|RuleBase:RU365027}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365027}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769, ECO:0000256|RuleBase:RU365027}.
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DR EMBL; KV878211; OJJ37318.1; -; Genomic_DNA.
DR RefSeq; XP_040690994.1; XM_040838413.1.
DR STRING; 1073089.A0A1L9RR69; -.
DR GeneID; 63754261; -.
DR VEuPathDB; FungiDB:ASPWEDRAFT_58885; -.
DR OrthoDB; 381190at2759; -.
DR Proteomes; UP000184383; Unassembled WGS sequence.
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:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProtKB-ARBA.
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; 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; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365027};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365027};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU365027};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365027};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365027};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365027};
KW Reference proteome {ECO:0000313|Proteomes:UP000184383};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU365027};
KW Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU365027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365027}.
FT DOMAIN 1840..2438
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2542..2853
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2863..2895
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2824..2849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2895 AA; 325273 MW; A6443A3DECA099AB CRC64;
MAEITVDKAI ALLSSDKQRD RSDGLADLKH ILQKNKQSSK LNTLNDKACH KIFESLFRFI
SVEKSAYKRA NSKGPSASRL SACASVLRTA VDVFLQNLRI KSVRAIIDHI TETIPDPGEG
PWEPLSVDYT KCLSALLHYP PHVEHLGIGE WEKLISFCLR GLGVQEDEDS QVSVRNSHRF
TLDGYLDTPS RSTPSRATPV LAIREKHTGD KSALGEIVVC IQLLTASPTA PVQMSAEKIF
HGLAEFVKSS HIAGSGQQAA FNSINTVVTK VLFDQSELVR TFLLDLIPVI RRLWATKLTG
LKDELLVTIM LCMTILGDAI RKEPSEILSH SIQGLVKTLH SEYTRRAEKE MLQIDDLIFY
RPESTRTDKL ITGPRLGNAK SEHNWTLIWA IASLLELSEE IAARLSTPHN LEEAASKRQR
FTSEIEEVFR DSFSSSGTKR LCALQLIPVL VKSQMNVESK ASLLHRLMPN ILDDNGAVSS
WTMVAISSIA SSPGADTPSL KGYWQQVWDL TSRASTSQVT SRAACNLMSS IMQFDLLEYS
AVAETTRSML SSVNLSGPST ISDTSLSLWA ILTRMNAQIN PGSVLNASKQ ICTWLREVWT
IGTVTDRIQT AQVAMFARPM DLLNLLLACT NRPFVLPDCQ FRGPTGTITR SWHFSHRNRR
LLRYLFHLEG IRDSVNPWDT EEKLYLEPFT RQDPNDAVVL DLLYAKSEMF LQAWRSLSED
KSHHVTVEII QILASFCIAI ALYTECLPQQ LASRVADLQQ NSQRLWSNVC SFLASREGDF
IQPCLEMFSP ILDSAPCLFD PENIVSRGLR NIVPPLAEIL EKKRRIQNEF SNDEDAMDLD
DPLSANVDQM TVNKSIINLN REALPFFPDT ATFQRRMTIQ LSILQSTLVD TYQVEEQNNR
SLIEYLTALE EPDILSAQYF LPQVYRSCSS MDRPFLLDIL EDLGGKCLES YGLERCESSQ
RLCISMLTNF VNAWTSGKED HLSESAADLY SWFTDVLLAK GKASCGVLIG LSELLGGIIS
SNASYKSGQA NPSPRTTLFM ILEEGDILVK FSVANLIPRL FGRFSLQDHD AILNDVLESL
PRDPDWSEGI ALRLFILSQL ASQWHTLLRR SIYHMFETPA QVPHSLWYAE KCMRDVANTL
GLDNAKELFR LFSSQILYTW TESQSITLMP FSIFGYSDLR DMLDDVQDEL VGQIIMRGNE
QETAELSNFM NVSFVELLKK SFYRAEAYSI SRDISTPPSQ GSQPRGVENR LKKMLGTELF
VTLIENQFPQ VIATFFGSLD QYEQIEKAFS KRLNFQGALD SLKRITGKSC SQNALPANQQ
PSFRARYLLD ELKFLCKRSG YDLDTIWTPA LVSFVCRTLL ESVHPALGSL HACSVIRKIR
ILVSVAGPVM LRDYPFEMIL HALRPFLTDV YCSEDALGIF WYLLESGKSY LTESPGFMAG
LTVSTFVSLN KFLASSPEST TQENQFMIVL EKLQGFLLWF GEFLDAYESS ILGTDTYEPF
RRLVRSAQKV SITGDNSGDT NERDLLLEIL GDRNSSRNLL SKPIFDHVVS LLCVDFKRLP
CHQYDNIETD EDAISNTVAL CQTLRNFKPG TEYRLWAATV IGRGFAATGQ ISDVLLREQE
PSLFQAHESR SSDGIVCHSK ARIIQILCDM LQNGSYLEVG LVERTLQLII SNLVNSPEFG
HSGNAIPPSL MKALIWNPYQ CPSISMSAAE ERASNDTVGW DPSLSSADWA RNIALFLSKA
AHKDPVVGPL SKVLSVIPGL AVELLPFILH DVLLMGLEGA VNTRHTVSEI FKQVLQQVKE
STIPHARLVI NCILYLRNQP IPDEVTIVER DEWLDINYGD VSSAANKCRM PKTSLLFLEI
HASRIVSGSR RSSLAKFEPP PEIMHDVFRD IDDPDLFYGI QQSSSLESVM ETLEYESSGL
KNLQFQSAQY DSEIQMSGGA NTYGVLKALN STNLQGIANS MFTAPGHLKD TTSSFDSMLQ
AATSLRQWDI PVPPLNPSSS ATVFRAFQSL NTSGTLFEVS TSIEDSMLTT LDLLASTNRS
AISLRTAMRV LGIMTEINDV VHASSSVELS QGWERIKARN FWLKTTSVHE VGEILNCREA
LFSSIKEKDY LKSALNITDQ DAQLLEVKAI RQSLETTRNH GISQASLKSA ICLSKLAGPC
ASRGINIEGA AKFDLANVLW DQGEMTPSIR MLQQLNDQND LHKQAIPISR AELLVTLGHH
VAEARLEKPE AIIQQYLTPA VKELKGRSEG EEAGRVYHGF AMFCDQQLQN QDGLEDFKRV
EQLRNRKEKE VLAWEEMMGN SSGRDREALK MYRAKAKQWF DLDDREYQRL LRSREAFLQQ
CLENYLLCLK ESDTYNNDAL RFCALWLDKS DNEIANNAVS KHLNQVPSRK FAPLMNQLSS
RLLDVSDDFQ SLLFALIFRI CVEHPFHGMY QIFASSKSKG GKDQSSLARY RAAGRLVDGL
KNDKRIGPTW VSIHNTNINY VRFAADRLDE KLRSGAKVSL KKMLTGQRLE QDAASQKLPP
PTMKIDVRVD CNYSDIPKLV RFNPEFTIAS GVSAPKIVTA IATDGLRYKQ LFKGGNDDLR
QDAIMEQVFE QVSSLLKDHQ VTQQRNLGIR TYKVLPLTSN AGIIEFVPHT IPLHDYLMPA
HQKYFPKDMK PNACRKHIAD VQTRSFEQRV RTYRQVTERF HPVMKYFFME KFNNPDDWFT
KRLSYTRSTA AISILGHVLG LGDRHGHNIL LDERTGEVVH IDLGVAFEQG RVLPVPEVVP
FRLTRDLVDG MGITKTEGVF RRCCEFTLEA LRQESYSIMT ILDVLRYDPL YSWTVSPLRM
KKMQDAPEAG DGPVLPGTTD QRTANEPSEA DRALTVVAKK LSKTLSVTAT VNELIQQATD
EKNLAVLYCG WAAYA
//
