ID A0A177C870_9PLEO Unreviewed; 2988 AA.
AC A0A177C870;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=CC84DRAFT_1125200 {ECO:0000313|EMBL:OAG03052.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG03052.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG03052.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG03052.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441555; OAG03052.1; -; Genomic_DNA.
DR RefSeq; XP_018033417.1; XM_018175714.1.
DR STRING; 1460663.A0A177C870; -.
DR GeneID; 28759200; -.
DR InParanoid; A0A177C870; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000077069; 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; 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:UP000077069};
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 1896..2502
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2615..2926
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2956..2988
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 180..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2894..2944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2894..2916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2928..2942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2988 AA; 334752 MW; 2F2E893C687F31DE CRC64;
MGVTSIQDAK VLIASTKVKE RGAGLKDLIH ILKHNHGKAS LETITNKAYL ALCETLFQCL
RDERSTYQHH LAGRTKSAQT HANLLQLAAV ALRHVINSAL RTIKATTVEL IVETIIELLP
DKNGRFLGPL DELPKALRAL LEYQPHVERM SHDCWHDTVQ FCTESLSTIF AVAEEEPHDS
WETTVSSRAR TPFESTDGAP RPSLRGNDSA PRATPRGTAS RSRRYTDGQT ITAEDLVQCL
HMLAKASNAP ILSCAHAILD ALIAFLQKKT GRGTPAALAA INAILPRVIL SKSQLSEQVI
RELLPLLRSL WSDPVIRDEV MITLTYVEAH LRHLVATDSD GVLSLDAEAL VEAFYSDYRR
RQETTAHQFL EEDYLCFRKA GGVAANVHPL STHTFSMDTE NVRYESLWAT VAYIAKLSAM
LDGRKHKLAR GNDRDDELAT KRHRITHHFD EYLRHVSETR SNAKRSALQV LAFMVQEIPL
DEDQILALLD KLTVIISAEN SVHSSWAMIA LAAIACQQQA TKDALKPYWS SVWQSATRAV
TSLSSCRAAC HLMDVLLKLD VVSFSTVTAS VQNMLFSIEL SGPALLTETS AAFMTTLIRE
RVKENPTSHD VTAERILNWL FGKWTPHLWA ERTSTSLNAH HCDARDILSL LHACLDRSVA
SVRPAVFQIL GPIAQARLRI ANFADLSAYL LLLEPQEKFI RELTLASGAV NSTPSSCAIQ
LEGRIVNFCI SELERTKSRW KDMSQQNPQG ITSNMWRVIT NFCVVTAALS ALLHRNDRPV
AALDAATDSA AQSLSHLLAK PQTEQYKMEA VLETCAASLP DITSITTLSS TVFHEAGVSY
LATHLRRALN SRQETKRSFY AEDEDLMDLD GGMDSQMSNG TSTNEVEVPR HDLQASGEAG
ALHACSATYL HLISSVGDQL EDERDTIPAE FIEHLVSKSQ SDLLRSRQLL KGILCGHFHM
SAADCLKLLE KLMEALIDPT AREYNSSEVA NCMMVETLVG MTKVWNSEPI DQESEEVQEQ
TQALYEYYTR DMEKSGVRAS PSLQTRVADF LHGLLSCYNI SNDAKSPSVR TRLFQLLSKG
EMTVKYHIAK KLPTVFEVWS LSTHDDILQD VDSHLPGDGE DLEGIAIRLL VLSKLASRWH
TLLRQCVYRI FATAGVVSTA ALHASHCISE VARAKKLGDS TSLFRLFAPQ VIFTWLDRKR
KYAEIPYTIF GYDSLAHLLR DVESEAVGQA IMLGMESEVD YIAQELGVKV SELLSRNISK
AAAYTISWDT CRGSGRNKDL PSNEQLLCKL ISKTDHEQKV GGDRGNMKNG HATGPKHLSL
DQKYFALALG HLFQTVDYEE RIKKSLEKRN SSDPALHALT RMLNNSQSSG DFNVGIEPSF
SAFYLPDQVD RLCRRAFGGI TNFWNPATYT LVLRMLLDRI HPALGSLYAR SMIRKIRIVV
AFAGSVAYQG YPLQMTLQSL RPFLTDIQCA EDTIGIIQYL FENGMQYLSD NLSFVTGIGL
SILISLRSFL GSSQEIMTQQ SQYLASMDSA KVFHTWLTAK LKGYSEGLTV NDPSSVNAFK
LITTAASQVR LQGNSIRDSE ESKLLLEILE DVRSGRKLLN TTSRDVALNL LCQDFQPAST
AAEDILGNDI DAAGYAPFVW DSCRRGNVGH GYLRWAARVL GRAFSAFGGV ERSSAHSHPW
SSQDPNIRDI VGRASREAVV QDIIDMLYSD DRNNVSLAED ALRVIVSRLS RLRRDEADEV
VRNIPSHLVE ALKGDLSPST IPVLPNESLE DAVAPTSHTK AAAEWIKDLA IALCNAASQD
HVLGALPKLL DGMSHMADKL FPYILHLVLL KDAEGDRKVR QTMSAAIMDW FSKHEPSHVP
YVRSLLQAIL YLRSQPIPRE MTRVDRDRWL EIDWLRASEA ATNCGMFRTA LMFAETYSGT
PTVKSVSRRS SIMQEAPKLP VKLQLSIYKN LDEPDSFYGV DQGSSLSSAI ERFDYEGDGL
SSMLFRGARF GSQMRRSNVV NATDSRGFLN SLIKLNMDSV ANALLSTDQL RDIGDEAVEY
TLHTARKLGK WDIKAPELNH SESSTLYKAF QGLHYATGEA SAKLSIDNQL LATMEFLFGR
QDSTSLTKIR LRTLAALTEA DELISCGSPD QLLDSWDRVK GREKWMQTGE FEDVRQLLSC
RETLLSVMGS NNALLDAIHT RAGTLRSMEV EALVSTSTIC RRHGALQESL TSVTYLSDIV
QDCKAFGLDV EASAKYEEAN VLWDHGEQEK SIGIRQELVD YGNFDSQDKQ ISLPVLLAKL
GHHLAEARSA TPEKIIQNYL KPAIRELKGQ IQGPDPGQVF HEFALFCDKQ LQSPEAAADR
DRAKSIMDRR AQEIQDFERL IRQEQSKQTR ETYKRSHHKA HVWYKLDHAE YERLRKGREE
LLRQCLENYL LSLQASDEYN SDALRVFSLW LEHSETMLAN SAVHAHIDKV PSGKFALLMN
QLSSRLQHDR SDFQKLLTNL VFRICIEHPY HGMHQIFAMQ MKTANVTRED VIRSKDEAAK
SRQKAAASLA AELAKDKRSS IIWSCLFRSN EIYHALAMFK DDKEQRQGRD ISLDRYPESK
ALMHKVPTYK VPPATLQIEV RADMDYSHLP RIVRFKSRMS IANGLSAPKI ITAIGSDGHT
YKQLYKSGND DLRQDAIMEQ VFDQVSRLLK KHTATRLRNL GIRTYKVLPL STRSGLMEFV
QNTIPLHGWL MPAHERYNPH DYKPDKCRKD IGAVQQETLQ ARVKVWNKIA ENFHPVMRYF
FLERFQDPDE WFERRLAYTR STAAISILGH VLGLGDRHCH NILLDEKSGE VVHIDLGVSF
EAGRVLPVPE VVPFRLTRDL VDGMGYTKTE GVFRRCCEFT MDTLREERES IMTLLNVLRY
DPLVNWSVTA TKARRMQEQQ DTNAAQRSNT AGPERTPVPS GISATDLEVQ GDDKKKDEQA
GEAGRALSVV EKKLSTTLST KATVNELIQS ATDERNLAVL YMGWASYA
//
