ID A0A0C3JNQ9_PISTI Unreviewed; 3042 AA.
AC A0A0C3JNQ9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=M404DRAFT_995273 {ECO:0000313|EMBL:KIO10808.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO10808.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIO10808.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIO10808.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-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}.
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DR EMBL; KN831951; KIO10808.1; -; Genomic_DNA.
DR STRING; 870435.A0A0C3JNQ9; -.
DR HOGENOM; CLU_000178_11_0_1; -.
DR InParanoid; A0A0C3JNQ9; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000054217; 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; IPR003151; PIK-rel_kinase_FAT.
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; PF02259; FAT; 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; 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:UP000054217};
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 1963..2567
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2682..2998
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 3010..3042
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 170..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2973..2993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3042 AA; 342543 MW; C09A7B5FD946BFE5 CRC64;
MSNLKTVVDR LRSEKVKERQ EGIAALRSTF AREDAVYSIE DGRGWLVLYQ ALFTTVKVEK
LDTAKKSGKA GTAGAAAQRR LVEAAAAVRW LVERSVRCLS KRALTPLLEH LTQMLVHRHE
LFSPIALDYL KTIRVLLSWT PHMDHVNLET WLKLVEICFN VVLDEPMDKE LVPSEEDNLS
GENSMYQSDS NDDDAGSSSI PAQTRKRHLA ERATPGSTDS SHRFRRSARR TVSLEQVECT
ALLALLFRHP AAPFLATVDR SDPDRKGNLI PVPIASALFK RMKRFLECYP TDTSLHHDYL
LALRSFLSQV SLNCKDEVDD LARSSWDALV GLWGTKNKQL KENLVGIFRI LFPFITAAQS
APSYGWADAV QNLLVLLNGE AESKWGIDGL FIDSLRLDVS PAEVGAGEIF VSHTFRAGWN
FDTNQALAWT LLELQADCIE KLFKHSESVH VGTPSFSSTT KRMKREDPIC ALLQSIRSTS
TTNVRVYNLQ ILLFLIDRHW AEFHNALQND IINVLLQLIS VDDVSIQSWI FLSLAAVARW
DGVDGVCHSG TVFATAVRTD RRGPTTWDPI WTHAVRRANV PVVCRAACHT AYLLIGHAKH
LLTSHRVLAE IETFAKDLDL QGPNFPYDAV CMFLAQCLRV ASQDVRLYRM QLEEKVLSWL
LDNWGIGVVT SNVSGKARLP PHTINDFLNL LGSICGYRQH TDLICASPLP DCEIAEVMEE
QRKTKIIRDY LLFAKLPQVP HCKGTVEDVA LVSSDELPSS RLDQELVSPR GRERRVSIFL
HKAIESLVVG WEVAKVNNFT HAAAEEIRQS LDVAITAIIF DSLQASNGTR SNRRVVQLAG
KVVVLLAPLL TDSRWTTEER VLILKAFDPL ILDGDSGNDD EEWEAMVVPS VDSGIRSHIL
NALRARLSRD VRSRAQRRSL QRMIWRNADI QDDFAAVFQS LNQLLCVLID QVPHDEDSNA
DEEGDRFEPI RTTRAAMPAD DGSQDHSLAV RRLVEICVTF LSVVPALQNP VGEVTHNKEL
VKVVTNCSEE KLLVLGPPLL TVVCKRLLNL NAHVLDTLLG KCADLLQRYS HAFNAQFHLL
VTDLLKCTMH IWLEKKVAGS VLGDHVLDLC AWISGIARKK VTFWKVRDSV VQFTAMLLAE
DPSQSFWPAE DGEESVSRPL HILLALNADE DIRVRFRAAV KTANLFALRE DDGTRDFGNL
DSFYTSVHES LPRDLAKREH MFTRSLCLGN IMIGSSYVRR GPYWHLLEVA FHSPSYARHI
QVVLNGVSMR LGLSDSHELF EAYASQIAFS IRQNFYDAMR LPPSLLGYDN RRACAEAALR
LCTPANLMVD GGSDAVAHGR TLFNNHCTAI QKTVHEGLLM CVGDLIGLQL VCFMDRPPGN
SGSVTQQLRE VLTSIGLNFP SQEAFVECVR ENVAGIAVAI IRSLGDQDFS ERGAIVTALR
KVTSTDTTGT FLSLNQYRQL GDFRYHPPNL PRFGTGTVLR ALQWCISSSK REDAAAISFH
VLHQLFSELH LTPFVNEQHR LLNGIALLVS VRHCDFGDPT LLHTFVQKSS LLLAQSDLIT
AGQSFLEWGF SIFRKTHQVD QRLPNILAHV CALVGDLQSA STSASATAGK LRSWLDEQAL
SLSQDQKIRP FVLKALPVWS HEPSSELSAL VEDLSADDLS ATLSDHRITS NKFRLVRQLN
RLAEQHAYCR VRFSTSDFWR LKDNIPPKGR LSRGDIDAFA SLLIANAGNI YSFRSEPAFP
QTLRARHCRG TKRQEDEKTE PAPQHAILQT LLAMLDDGDP SEVNLVYLAL RSLISVASPG
ILSFQLWPTE YRTPIEYFQR FPVPPPNARQ ARTIDQLDAI WPQNADFPQW ICSVTTLLAD
ILASKDNFYA QLVPLLQRNT LFAEEVLPVL VHTLLQAERA RAIEVSARKG LSDYFTNVLR
AEEVNRLCLR AIVDVILHLR NFEPSNSTGQ LAHDKWLDVD FHLLARSAVT CGSYTTALLF
LELACEYQQL NMDATGGVEH LLFDIYSHID EPDGFYGIKT TDLRHFLIKR FHHEKQWEKA
FRFHGAALEA DNHGSIDADG LLQSFHAFGF DHLALRALQS SQGGIDSDVG SSTMSYQLGW
RTETWDLPDS GQQDSSTTLY RALRAVHRER NHKVVDATIN QALCDMMERL LTLGNEDITE
IREVGRNFMC LSQITRWRSG KLQEYLDSKT SDARAFSHLV DIDPDFEFLD LERILATRLS
LVRSVRQKEE REQIGELISP FTRTLIDVEK RCLVRLSVAA RKSNQLQVAL NSIVKAQQLE
KTPSYEISQE FANVLWLQRE QKLAVQFLKD LLSQKKAEPG SKPTIEEAMT MARLGSWISE
ACMEKPTDIK QNLFDAAVQV AACAEKRMPT RNDSCASIYH KCAQFAERQY HAILKSPDGV
RWKVYVDRKR QEIKQMETQL RGTQMSSHDY GVLVHEQTKA RALLAEDEDA YERHNGALVT
FLESAIDMYS RCLAASDGFD DDVPIRFSSL WFANFDDERL QKGIMAAVDR IPSRKFVFLS
HQLSARISRP IHGEMPKSQQ ILQRLVLRMC QEHPFHSLYQ VYCIRPEGSV QSGSMRRTSS
RLESPTSQTD RGLAASHIFD VLLADPNHSA RTKAIEQVCN ASLQWAKYPI KELTGKKTNI
ILNVPEGLLI RQLRNIHVPV LTSHPPIDPT LRYDNCVWIS HYDKTFQPAG GVNMPKINTC
YGTDGQRFKQ LFKGEGNDDL RQDAVMEQVF DLVNTVLRHD RETKRRDLKV RGYTVLPLAP
QAGVIEFVGN TSPLASWLQP AHKRYRPNDM DHHQATRYLS QTREKYKGKT EALVAAFSEI
CRRIQPVMRH YFPEKSKTPI AWFAMRLNYT RSVATTSIVG HVLGLGDRHI SNILLDNRSG
EVVHIDLGIA FDQGKRLPVP ERVPFRMTRD MVDGMGYSGT QGVFQRCAEE TLRVLREQSD
VVMTVLEVFK HDPLHSWTAS ELKLKKIQES AVGPPQQLNP LAERPDFDMK SGSAEAAERA
LGSVARKLDK SLSVECTVNE LIAEATDVVN LATIYYGWSP DL
//
