ID A0A1L9P385_ASPVE Unreviewed; 2854 AA.
AC A0A1L9P385;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=ASPVEDRAFT_212464 {ECO:0000313|EMBL:OJI96000.1};
OS Aspergillus versicolor CBS 583.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJI96000.1, ECO:0000313|Proteomes:UP000184073};
RN [1] {ECO:0000313|Proteomes:UP000184073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
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=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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775,
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; KV878125; OJI96000.1; -; Genomic_DNA.
DR STRING; 1036611.A0A1L9P385; -.
DR VEuPathDB; FungiDB:ASPVEDRAFT_212464; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000184073; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
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:SF5; SERINE/THREONINE-PROTEIN KINASE ATM-LIKE ISOFORM X1; 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; 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:UP000184073};
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 1798..2396
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2500..2811
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2822..2854
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 143..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2782..2807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2854 AA; 320561 MW; F4E446861E157610 CRC64;
MGDKACHKIF ESLFRLISTE KSLYTRASSK GAASSRLSAC VSVLRTAVDA LLRNLRTKSV
RAVIDHITDV LANPGTALFE LLSVDYTKCL STILHYPPHV EHLGVEEWEN VMHFCLRIVD
ISDDEESQRR TWSPHTSVMD DYLSASGGRS TPSRMTPSLA LREKPKGSPG AVEEALICIR
ILSGVANAPI QENAESLLPG LAKYVRSSPL AGSGHQSAFS TINTVVMRVI FDNSELTRNT
LLDLVPSIRQ HWATKLIGLK DELLVTAMLI VTTLTDEIRR APAADLETII DGLMNTLQRE
YSKRPEKDIL QVDELVFDSK SSAPHERFHL WPRLEAARSE HNWTVVWVIA RLMEMSEELG
TRLSFPVEGE TPSKKQRLGS KIDDVFRDST GSFGARRVPA LQLIPFLPNH YASIESKVSL
LERLIPNIHD DNSAVSSWTM IAIASIAASP EADALILKRH WQQVWDLTSR ASTSQFTSRA
ACNLQNKILQ FGLLDYSAVV ETMDSMLSFV NLNGPSNLSD ASLELWASVI RMKTQMNPGS
VSNASSQICT WLRDAWSIGT SMDRTQTSQI AAFARPLELL SLIMACTNRP FRQPSVLFKG
PTGIIAKCWF FYHTNKRIWS YLFDIHSLLD VYDMWDAEET VSIQQFSQLD PNDLGVIDLL
QAKSEYFLHS WQALSEDKSR HITSDMVQIL TSFCITVILY SFCLPEQPGS RLQALHSNTH
RLWESICSLL ASRESAFILP SLLLFPSFIP LDSGFSKPVA GVHKALYELV APLSRVLEGY
RQSHKEISAS NEREGDMDLD DPFLASTDQI EEVSNIVSGN RTDLPLFQDT ASFQRYMTIR
LSLFQRMSAK VDSSQKQPGD ALDEYFTSLD QVDFLAAHEL LPFVYESCAE MDREFLLGIV
EDLGEKCLQS YELERCENSH LICIRMMDSV VKSWTSGIQD NLSDSAADIY TWFTEVFLKR
GRASPSVLVA FAHLLGNVLS LNPTYLSDSS SPSPRTTLFR IIGEGGVLVK FNAGKLIPQL
FGQFLLKDHD VIFNDVLDCL PRDPDWQEGI AVRLFLLAQL ASQWHTLLRR SIYHIFETPA
QVHHSLWYAE KCLQQVSAAL GLPDAKEIFR LFSSQIIYTW TETQSVMSMP FSIFGYASLE
DMLSDAQDEI VGQIMMRASE TDAVELSKFM CRPFVELLAD SFYKAEAYTI ASDISTPPGQ
GSQPKGVENR LKKILGSDQF MKLIEVQFPQ IIATFFGVLD LYEQVEKAFS RRENFRGALN
AFKQISGKDT ARTVLPANQQ PSFRARFLLD ELEFLCKRSG YELETIWTPT LASYVCRTLL
ESIHPALGSL HACSVIRKIK ILVCVAGPVM LSDYPFEMII HALQPFLVDI FCSEDALSIF
WYLLEAGKPY LTDNPGLMAG IAVSTSLSLK RFLKSPPTNP RHEHQLQIVV GNIQTFYGWF
EEYLNSYRSP VLDDYSSERF QRFTGSLQAT VGQEPGSTSV SETDLLLEVL KDRESKSSLL
SKQISDHVIS LLCTTSDGAT GYQLAAIEQD EDAIANAITV CQTLRDFNPG PEYRSWAARV
VGKAFAATGK INDSLLREQD LEFFQPLSPQ SDVDILCRSK ANILQLLCSM LLNSNQTGPI
ERTLQLIVTN LAKFPDFELC AADIPPSLMK ALTWSPYQCP GISLRALEAK ERDRVRGWDV
GLSPSCWARN VGLLLSKTAS DDPVIGPLNS ILYLIPDLAA RLLPYILHDA LLAEYRGEVE
IRDNMSQIFN EVLQNNEDKV VPHSRLIINC ILYLHNQPRP DEHTIVERES WLDIDYAVAS
SAASRCRMPK TALMFLEIHA SRSASGSRRS SVAKYEPPAA LLHDIFKNID DPDIFYGIQQ
TSSLDSVMET LEHESSGFKN LLFQSAHYDS QMQMTGSGNT YGVLNALNST NLQGIANSML
GVLGNSNDAV IPFSSMLMAA TNLRQWDIPV SPLNSSPSAT IFRAFQNLNT YGTLTDMHTS
IDESLTNSLG LIDSDSRSAM SLRTAMRVLG ILTEIEEVLN SKSAEEVSQA WQKVSKRTSW
LKTTDVHEVG EILNSHETLF SSIKQNDYLK SAFNLGDHDA QLLEVKVIRQ SIHIARNHGI
AQASLKSAVY LSKLSDQSAS LGLNVEGVAK FDLANVLWDQ GEMAPSIQIL QHLKDRNDLH
KQAIPMSRAE LLVTLGHHIA EARLEKPEAI IQNYLTPAVK ELKGRSEAED AGRVYHGFAM
FCDQQLQNSD GLEDFSRVEQ LRNRKEKEVL ALDAMLKTAE GKERDNLKFH RAKTKQWFDL
DDREYQRLKR SREAFLQQCL ENYLICLKES EAYNNDVLRF CALWLDQSYS DIANRAVSKY
LADVPSRKFA PLMNQLTSRL LDLSDDFQRL LSALVFRICS EHPFHGMYQI FSSSKSKGGK
DESALSRNRA ATHLADVLRS DRRIGPLWVT VHNANINYVR FAVDRLDDKA KSGAKIQLKR
LQTGVRLEQD AATQRLPPPT MKIEIRIDCD YSDVPKLIRY NPEFTIASGV SAPKIVTAVA
SNGVRYKQLF KGGNDDLRQD AIMEQVFEQV SSLLKDHQAT RQRNLGIRAY KVLPLTSNSG
IIEFVPHTIP LNEYLMPAHQ RYYPKDMKPS ACRKHVADVQ TRSFEQRVRT YRNVTDHFHP
VLRYFFMEKF NNPDDWFGRR LSYTQSTAAI SMLGHVLGLG DRHGHNILLD ERTGEVVHID
LGVAFEQGRV LPVPEVVPFR LTRDLVDGMG VAKTEGVFRR CCEFTLEALR QESYSIMTIL
DVLRYDPLYS WTVSPLRMKK IQEHEPGDGP PALPGSTVDQ RPTNEPSEAN RALTVVAKKL
SKTLSVTATV NELIQQATDD KNLAVLYCGW AAYA
//