ID U4LEJ8_PYROM Unreviewed; 2891 AA.
AC U4LEJ8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=PCON_07796 {ECO:0000313|EMBL:CCX29977.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX29977.1};
RN [1] {ECO:0000313|EMBL:CCX29977.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX29977.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX29977.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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-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|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; HF935395; CCX29977.1; -; Genomic_DNA.
DR STRING; 1076935.U4LEJ8; -.
DR eggNOG; KOG0892; Eukaryota.
DR OMA; HACSVIR; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000018144; 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; 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 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}; Chromosome {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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU365027}; Telomere {ECO:0000256|RuleBase:RU365027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365027}.
FT DOMAIN 1806..2426
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2537..2848
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2859..2891
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 86..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2821..2843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2891 AA; 325311 MW; EEBF733C156C09A4 CRC64;
MVGSVLRLAV QCGVATIKAK TVPTIWKHIL ETLPSGDTLC EPIKVDYIKA LKVLFQHMPH
TEHLRRKEWE KIATFCLENV QSQLGAAGEG SQREPSSTPA GSRGRATARK QTTRIAKETR
EFLLCLRYLL AAPNAPILEN RVQLCETLMQ FLRTQQKIDQ AHQHVFYSLN CVLNVIAGND
LTLTYKVCDE LVPIITRLWD TNTAGTKDQM IISLIHCRLH IKAQLRSHDS QRLRDNVGYL
YEMLYNEYNT RATLTRDDRE ILQMDDVIFP SPTEKPDPEI PFRLKAIALR PGSVNDHKEE
IWMVPQLIAM FVELLDASGN SDRIPHKKST GGGDSPTRKR PRMYSRFGET MRYIRSIDVS
RKLCALQVFT FLADLKAVDE DDFPSLVQDL IEASKHENPT ITGWALAAIG SCAFLTCASE
PVHSGLWHQV WQLCARYASN QHVCRIASHI MRIIATKDLV AYSTISSSVE SMVRNDDGNG
PSIVTDSSLA LWSYLLRKRN TMPQSVTFNA NEQIFAWFNT HWHPEREGLS SNNVKAQSYS
QKILPGDVID FLAVCCGVKP SAIERRTPRI CGPIGQACIR ASRCRSLYVT LLNEDDDESD
KTDSKYMDSS LSSGTENINA ELQELIVNMF EMRTKSVKDA WAAISSQHGG VTVAVLQNLV
GYLLIAGTTL SMISGPGLIK ARQVDVKLRE GLLQDFFTYV ESKNCSLGQV TGIYLAIEGI
LPKNISEILD QNSVFHDFLR GTAGQFLAGI SRVSGDKVTS QSLTREPERD DDGMDLDFPE
DSKEEEKVES TTKNREQLEV FCSKEASWLT TSLLITLCSL AQGDTTREDI CAVFVDSCLL
KLTSDKTPLV GPLIRDFIIT AGEDLPMDLT IDLFMQAAED LIGKYNVEAS EIGMTTGLDI
LTALAPRWVP ANSDPDLREN CEIFFHTIIP LVKQGDDISY SVRVALGRLC EQILLIDPVY
GKPTAPENEA SQPPSSRPPA SSARNRRTQE EEPKKQDWWP RTLLIDLIED PDLRVAYSAA
HRMHVIFEVF GESQHLALTD MISQKLNSDP DWLEGLIIRV HAFGLMSHMS PTMVSRAIYR
IFETGKIEEM GEYCARVLKT VARSAGLQNQ RGLFRLFKDN LIYLFLKHYS SLNEVPYYVF
GYKNFEDMCK DIPGDLVAHC FAHRKREDAE AVAQINGIPL QTLISDNFAN VAAYALVWDA
AVPAPRVQEG EAPQATLYSQ LRKMFKDEKF AELIQTNFPQ IIAIMFEMTQ HEGTEAKFFD
KEPDFGEARM HMEDIKAHGH LKHKVRITEP PVFPVKGIFG AIKFASNQIT VDYREIWNPA
MVVIVARRCF DSLHPARGPV HTLSVIRHIR LLISLAGRKV YEGYPLEMLI HGLKDYITDT
MCAEDTIGIL QYLLENGKEY LCKKPPFLIG VFLSLLAAIR KSRQIPSTQM QSQEPQLIDA
NSAIHMFSGW LKDHLAKCVF PRNQNEILHS IVRTALEFKQ QGNAVHNSKE SKLLKLLIDE
DMKGSRSLLD PASRKLAFNL ICSDFERPES YRDDIFGADK NSFTRANSLL RISRNSNVND
GFLLWSARVL GRAYASTGQL HIDWTKEMEF HFPKRDPVLT AQIDKAPKVE IMKRLKELLL
SDDKKVVSLA EKALSWIIDG EAQIQEENSM SVLTDEESKA LYWGERPVEK PPTKQSITHA
GELKGSFITW VNDLAIAMCT NVPGVPVLNC IRDVLKNVDG VAEELFPYIT HILLAMDINQ
NPIAPPGLRD ELSALFQHCF NNCEEKTVPH NTVLIKTVLY LRSQQVVEGE ASKAERDNWL
ALDYLDAAKA AATCKMFKTA LLFAEIYSYE EKPAEIVNTS QRSRRESFQT KASEIIRLEV
PTDLQLAIFE NIDDPDAFYG IKQTFDLQTM MRNFEYEGDG LNMLWMQSAS QQSKVSLGAP
SSGSGLGLIN AFNTLGMNDV SHSLLQTGAS GSSSSPESAD NAYLSAWKLE QWDLPCPEVF
DTRSAQIYRA LQSVNKTVGS RSVALRMDPH ILSVMKQIKD GTRTGHALGD RMKTLAMLTE
MEEVFISQSH EQLEEVCENM KRRTAWMETG TYSDVEEMLA LRQVAFGSLS KRDHLRIHAN
LEPKQARLFE AEALVSSCKM ARKHIALHHA LSAAVKLSDI VQPCKEIGLD ISGVATLQAA
NVFWEKGQLV PSIRMLASLE NDKASASQTM AVGRAKLLAK LGNRISEARL EQPDTIMSTY
LERAIRALRG NEHGSEPGRV FHEFAKFCDQ QLNDRSNTED LERRTKLLDE SRGDVDELMS
LNSKVPSTAR TPKTNQALQR ELFKAKAWLA LGEQEYVRLK AARDAFVEKS IFNYLKCLIA
CDDYDEDAVR FCSLWFEYYL MDRANDAASI LDQVPSRKLA PLINQLSSRL LKEESKFQEL
LRKLMVRVCA DHPFHAVYQL VAIAKTKAQD DAAVSRSKAA KLVLHTLKEN NKGKMVSTVI
VPAILTTASE YEILAHARTD KKKDGSRVSL AKLLSTQKRD SKMWETGIPD LGIPPPTMDI
PIRADCDYSL VPRIRRFDQY ATIADGLSAP KIIKCEADNG MVYKQLVKGG NDDLRQDAIM
EQVFEQVSSV LQKGRTSRQR DLKIRRYKVI PLSATSGIIE FVANTIPLHD WLAPAHRKYH
PNDLEFMTCR KIISDAAKKT RRDREKAFET VMRGFNPVMH YFFMHEFSGP DAWYTSRLAY
TRSTAAISML GHVLGLGDRH LNNILLDKGT GEVVHIDLGI AFEQARILPV PEVIPFRLSR
DIVDGMGING TEGTFRRCCE FTLEVLRNES YRVTTILDVL RYDPLYNWTV SPHRMKRIQE
SHLERSDVSR KGEQGSKSDG EGELEAKRAL AVVADKLSKT LSVEATVNGL IQTAMDPRNL
AVLYCGWSAY C
//
