ID A0A0F4GTN3_9PEZI Unreviewed; 2965 AA.
AC A0A0F4GTN3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=TI39_contig312g00006 {ECO:0000313|EMBL:KJY00805.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY00805.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJY00805.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJY00805.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJY00805.1}.
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DR EMBL; LAFY01000304; KJY00805.1; -; Genomic_DNA.
DR STRING; 1047168.A0A0F4GTN3; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000033647; 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: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; 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 Reference proteome {ECO:0000313|Proteomes:UP000033647};
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 1900..2507
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2610..2923
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2933..2965
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 424..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2892..2923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2892..2920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2965 AA; 329514 MW; 4E5A3457341AC1CA CRC64;
MSEVTLFGAL ECIRSSLAKT RSKGFSDLKY ILRHNQNSSK VTGLDDASFH SIFETLFHAA
VGEQSTVAKA KTNATQKSAV TRLSDLASAL RHAVEAGAPF IRAKTARAVL DHVADTIQVP
NGSFCEPIAL DYAKCMRAVL SHQPHVEHMN RPSSTDPNQK DWERIAEFCT RCIQQAVAES
NEDDFSGDND ATSTIGTLNT LSYRSSRSAL RESDGSQGTQ QTLRMVADEM IGCLRALTAA
PNAPLQRKAE PLLWLLVEHL RVAASTPRSH EDAFTAINQL LCWTRTEDTK VTHDATPHLI
RLVKNYWTAK SPALQPMTAT ILLLRPYIFK AIGQSGGLSL RVELSGLLQA VQGEYSKRQE
RDHQKQLSLD DVRMEINPME NPEAGKVGIA LFTLQSSEAR SNAECNWTLV YLLASLTNAL
MSTNHSNHQL NSDDEPDDGS EHRPAKRRRR DDHEHGDDFA TLLKATNTGP DQARICALQT
LFFLVQQRAI DPIQMVRAVD SVMVSCTDDG NGVASWAYLA LAGCASQISA TSPKLADRWT
AVWQIASRAL SSVSACRSAS FALYIMLQLR LVPHSSIHDL LQTTTNAMDL NGPAQMSDAV
TLLLRAVLQY CQQTNPEAAS STAESILGWL SRTFVPSKID DKQYTSSTTT YGVSDVVLLI
GATLNRRGHP LRSTNFPTYH AVARTWLFCD GQKELLSYLL LEEDTNLGTN SELHDSLHQL
ASASVEAPRT SCEALALTHL TAELTRANEA WTTSVTERAR QPSQDSFAML CKACCIATCV
SSCFEFSDTR RASQLRYQSN NLLHALGEYV ARPGSDQTKA DCFLTTFSAV MSGIASNDHS
CGSRRTKCEA VICRTIKKTL DTIQEAANFG EEDDAMDLYD GAADSQDSRH ARPTIETVDL
VNDLDVAYSK LALRSCAALY ATTIVALETD AEVIGGPSTA SEEVVSFILL QSEATVIASR
GVIIQFTQLG LALSLRDTQR LLEFFVETII PSYIYGRSEV AIGTVLDVMD NLRDLWTDPS
NVDLYNLGLD VYDWCTGTAL SNGVLSPSVQ KRLASLLLQL CRLTVDYPSS DDDGSSGQDS
SARTSLFGLL KQGTVSVQFH LAAHISKVFG RTVLSQHEAM FDDLVESLPE DIDHMEGIAM
RLLFFAKLGS EWHSLLRQCV YYMFETAGTG SVPHAARCIA TLASMLPLKT PRKLFALFAP
QLLFTWLASS KSLRDIPFAA FQYASLNEIL VDNRIEVCAQ AVMHGSQEGI DTLSRALKIL
PQGVIKLSYA KSVAYAISCD IKTGSAQGSS GDTALTEHHL KSYLNNRAEH VPTLAEQWPA
IIGHFFLTSQ QDDPEDKWLE AKQDNKRANE PDNAPALEAM RRMKAFGHSS RKLPQSQEPS
FPSRNLWKEI GRLCRRLDID PSCLWNSSTF SLTVRMILDA MDSSLGSLHS CLMIRRLRLL
VCMAGEVAFS GFPLKMLIHS LRPFLNDSEC ADDTLGILQY LFNSSREYLR EHLTFLAGTV
VLLVLRLRKH AKSSHSSTTQ ESQHSATVQK MLGFQRWLVD YLSRLASDVS SPAFDRLTES
LNSLQLPGNA RKDTPESNLL LFLLGQWSAE QALCPRTDCL EAIAILAEYF EPAESISDDC
IGTDSDAVLY SQALWDIIQQ AAVSREFVQW SARVLGRAYA ATGQRPDVGA DGPGADLERH
PRTTANDQIT VNSQVIVARR WSELLYSRSR IEAGLAEHSL RKLVQRLSNS ATELRVFVQV
LPEEIDVAVA DGFFSYEPPS IDQRAFTDVQ DDALHRALHA TAARSMEAWT KELAVTVCRW
ASNVAVVACL APLVYSVSGL AAELLPSMLH ILLVDEMDRE KTLHSELSTA ITACLVETDP
ALKTKQQFFL KLLLYLRSQQ YPTELTRSDR TKWLQVDPVL AAAAAARCAM PHCGLLLAES
IPPVAQSSRR TSGRASTSQI MTIPPLENDL LLSIYRQLEE PDSFYGVQQS ASLDTVLSRL
DHEAIGLRSL MFRSAQMDSH MRHSHRLAEE DAVGMVHSLS NLNFNSLAFA LLNQGVGGNV
MTSGSMLEAA KALQQWDISL PETRVGDAFT AFGVLQELTR ATEPRQIQGK VCMAMTEHTL
RGITAGKYSR PSPSWCGVLA SLTEVEAIVS SPELEEMTAR WHAIREGSNW MRMARYEDVK
SLLSNRETMF GVVSQNLELQ RSLHVGQPDA RTFEVQALLD QSRLAREHGR LQEALTAVAT
LSDLVELCTN NNLRVEAAVK LETASVLWDA GEASASVKML QDVLGMTDLG KQTIPVGRAG
LRAQLAHQLA EARLEKPEDI MRHYLKPAIS DMKSVRTGTE AGRVFHEFAK FCDDELQNPG
NIENFTRVVK LRQAKQEEVD AFKAALRTKK SAGDRADLTR SLNLETKWLE MDIEEETRLK
DSRNNYVQQS LQNYLLTLQA SDAHDICVLR FFALWLEHSE DPGANAVVQK YLPDVPSWKF
VLLMNQLMSR VSKESSTFQM ALGELLIRIF KQHPYHSLHH LFTNARNQPK SDETATKSRH
SGSTAFVDRL YQGPVQKDLL TRLFYCNKLY RDIADSSPEA NKSGKFNVRS IPSAKKLMEN
IVRAKMPPIT INLPLRADAH YEIVPLIAKF KPEGTILGGI SAPKLVTVVD TNGKEYKQIF
KNGRDDLRQD AIMEQVFEEV SKMLRNHKST RQRDLKVRTY KVIPLSNTTG VIEFVANSIP
LMDYLRPAHQ RYHPNDYKEN KAREIINNAK DSAQSHRIGE YRRVCEHMHP VLRHFFLERY
DNPDEWFSKR TAYTRTTASV SILGHIIGLG DRHCSNILLD EVTGEVVHID LGVSFEAGRV
LPIPELVPFR LTRDIIDGMG ITKTEGVFRR CCEFTLDAVR EDKDSIMTLL NVLRYDPLYN
WTVSPLKAKR MQQAQDNNGL KGAQESEPSV RQQNQDGGES ERPLQVVENK LSKTLSTAAT
VNELIQQATD ESHLACLFSG WGAYY
//
