ID A0A067NI82_PLEOS Unreviewed; 3062 AA.
AC A0A067NI82;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=PLEOSDRAFT_1105591 {ECO:0000313|EMBL:KDQ26690.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ26690.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL198009; KDQ26690.1; -; Genomic_DNA.
DR STRING; 1137138.A0A067NI82; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1105591; -.
DR HOGENOM; CLU_000178_11_0_1; -.
DR InParanoid; A0A067NI82; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000027073; 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 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|RuleBase:RU365027};
KW 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 Reference proteome {ECO:0000313|Proteomes:UP000027073};
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 1998..2581
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2692..3016
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 3030..3062
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 191..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2979..3000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2983..3000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3062 AA; 344549 MW; 396457EC0B1A6111 CRC64;
MSGLREVLEG LSSAKIKDRQ ESFSTLRRVF SDDTLVATFH ITSKGETDTR AWLAVFQAVF
AAVKLEKILY KKKEHTSTVA TVTRRLEEAA AFFRWLVERS VTVLNKRATF AILDHIRDYI
EDHGALFTPL SADYVKALRC LLEYRPHLDH VEAGKWTEWV ALAFNVVLGE DLSRGLTLVP
AGESIVDEAM SVDDPDDEDE LPMHGLSPLK KRKRGQSAGP SQQGSAMKKT PKASSQHAHR
GSQVSTEQIE FMAILPILLG SQNVLPPPPK KPAPKKSTSA KSTSKDQSGD TNPIAPLETP
FSPFSAEPEA ILQRLRRFLK LYPTDGSLHN DYLIVLSITL DRLALNRRKE VMEFARDAWP
SLAGLWGAKS KALKEGLASV LTTLLPFYTK NDSSVWGVGL KKLWNSLDGD SQNRWSVDSL
ALENLRLEIS GDKDSPFATQ TFKAGFGFES GQALSWVILQ LQSDVLAKLY HLSESVGFRT
GGKRQKTDNP LSSLLSAITR QPLPSMRAHR LQLLLFFISR HWSRLHRTFQ CDVFNTLTQY
ISFDDVDIQS WVYLCLAAIA YTEGCSAAPV KEEMYSGGDD REIHWDPIWT HAMRRASVPL
VCRAACHIAY ILIIHSVNSP ATTPPDMPPS KRQLLSSQRV LGEIEVLVKD IDVQGPSLPY
DSVCRFCAEC LKVASQDVRL YRMHLEDKVL NWLVDCWKPG GISGAGSSGR RTSSKQSRVP
LHALSDVMML LEAICGLTKK SDFLCSLPLP QCWAAATLVD QVETSVIRDF LLEAKLPPFR
TLGNLREGDK ISIGDGSNPQ STPDVDDAEL VQPRSRDRKL SAFFVKFLEP LVAEWELSIE
ENGYVPADAA RRSIDFATVS ICYEFLLNYN GVRPNRRVVQ LACRVCRIAS SLLITTKWSE
DEKADILRGL EPLWDSGFNV SSRHRMEAML LPGFDSGINS QVLRSLTSRS TKRRTRVSVF
KDQYRRLIWR SADVQDAFGH VSNSIRTILR TLCGELGPDG QSLDQDDVSD LAQPNVLKVT
NMRFPPVLPS STEHITKMCI SFLAFVPILQ SASAEATRDK DLTDLVLACA TSSHPENFLQ
VCPALLDHVR CGAITLSPST LEAYLAGVGH ISPMYAYAKN DILQGLVIRI LDSTCHIWLD
PSDLLEGIRD KVSQLCQWLC TTTSQRLLGS WRVRDSAACF LDRYLDCDPT QVSWTELNGR
ELTRPADLLS MMIADEDIRV RFRTATLAPR LLALVRLGAR RPELQYNSIR LKLSTDLKHY
EHILTRSLCL GNIMIVSSAV RRGPYWHMLE TCLHCNDYSP HIRAILVQVA QRLGLGSPSV
LFQLYASQIA FSVREHNPLS IPSDVLGYQN LSEYAEAAFR PFTPTNLIAR PKDLGTSLFK
SHCSALSKRP QNGIRECFGD LIGIRVAQCF AEDEDTDGVE DILRETVQMG TDVMDDEEFR
DLLEQNADSI ITSILHTLGD QDFTQAGPLH HGLQVLAGSK AAEEFAILNR YRDDRYFATH
EPHFPINPAS SLLRSIIWLC SKFSEYRHPA VTFHVMQALL MEIHKSPLVN EQVRLINALT
LWVALRNEHF KEFTLLHTLA QGATSFMVQS DLARDSQSIL EWCFECYRND LQDDPCLPDI
LIRLCFQADD YAKDTGKGGF AKLGDTLTDW IDGQAMLFHR SPIHCKQVSR ALPAWSHRLA
PELAELYETI PTGTLSEIIG DPRISSNKFR LVRRLRELAS DDDTGGEQFG RADFWRLKEC
IPPPGQIQEE DIHAFAGLLV SHRGQVDGIG MDHPNPFSVR TKHLSSKRGP NEEGSPQNAI
LFSLVTMLDS GDPFEVQSAY TTLRLVASCS PMTIHPSSWP IQISQTLGHF HLCLPPPRPG
VKRNLSELES EAFLDALSSF PRWVTQLAVL ICEVLSSQNS FYSQLTPMLT SNHDFAEQLL
PVLVHTILQD NTDKSSKELL SQYFLTTIKA ADVAIRCLSC VIDVVLHLRQ FERQATGAGK
KRTNPLGHNE WLSLDFALLA QSCITCGAYT TALLFLELAA EYNQFSLPLS AEQILFEIYS
HIDEPDGFYG IKTNDLGQFL IRRFHHEGQW EKAFHFHGAA MEAQQHDQTT MDGLLRSYHS
FGFNQLAIHT LQSSPNGTSS PSMSYRLGWR TEAWDLPDVT EGGEGSSVYA ALRAMHRERD
FGIIRNIVRK SMLQEINKLR GLGIENHAEI HSVIQNLMCL DQVRLWEEPE TQRSLALQRI
DDALTRSFTS IDTDMEFSDL ENIMSTRVSL IRSVRYKEER SQIGNMRTPF LSSLLDFERA
CLLRLSEAAR QSHQGQIALN AITRAQRLET TTRFPVLKEF AQVIWLQKEE NAAVRLLREL
WENKESSDLL QEAMLLAHLG TWTSDACLEK PVAILEKYFT PAVKLIQKMD FGPSDPVRAD
VYYRCAMFAE RQYRTICASP DGEERRARVE QKRREVETRR NLTSKSLALQ NELGKAIKLL
AADEMLLEEY NSSKDIFLTR ALDMYSHCLA CSNDFDDDAA LRLCSLWFAN FEVDNLQNTI
ASSLRRVPAI KFMFLAHQIT ARLSKSPNPS KCQTILSNLV LRMCKEHPYH SLYQVLCLQP
SILPPETRRT SGRPAPAPPT STQSERGAAA YAIIDLLRND QDQLQRLKPI QILFDASLQW
AMHKVTKDCK NFAIPSHYSI RKISNLRAPV LTSHLPLDPT TRYESCVWVS KFDTQFTLAG
GIHLPKITDC YGDDGERYKQ LFKGDDDLRQ DAVMEQVFEL VNVVLKRDRE TKRRALSVRG
YKVVPLGPQA GVLEFVGNTT SLQQWLSRAH QKYRKEGEPS WIQVKDQIAN VQAADRRPPG
WRPEMVVPVY RSAMEPFKPV MRHWFTEQHK IPTSWFAVRL RYIRSVATTS IVGHILGLGD
RHASNILILK TTGELVHIDL GIAFEQGKLL AIPERVPFRM TPDMVDGMGI AGTQGVFQRC
AEETLRVLRE GSQVIMTVLE VFKHDPLYSW TASEEKLRNA QRETNKSGAG AEQDASEGSS
IQPVLVANSG NVTQELADRT LSSVARKLDK SLSVEFTVNE LLAEAMDPNN LGAMFVGWSP
YF
//
