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Database: UniProt
Entry: A0A1L9P385_ASPVE
LinkDB: A0A1L9P385_ASPVE
Original site: A0A1L9P385_ASPVE 
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
//
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