ID A0A3B6RSU9_WHEAT Unreviewed; 2618 AA.
AC A0A3B6RSU9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 08-OCT-2025, entry version 33.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LOC123149735 {ECO:0000313|EnsemblPlants:TraesCS7A02G543400.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7A02G543400.1};
RN [1] {ECO:0000313|EnsemblPlants:TraesCS7A02G543400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS7A02G543400.1};
RA Rossello M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:TraesCS7A02G543400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
CC -!- FUNCTION: Probable serine/threonine kinase. Seems to play a central
CC role in cell-cycle regulation by transmitting DNA damage signals to
CC downstream effectors of cell-cycle progression. May recognize the
CC substrate consensus sequence [ST]-Q and phosphorylate histone variant
CC H2AX to form H2AXS139ph at sites of DNA damage, thereby regulating DNA
CC damage response mechanism. {ECO:0000256|ARBA:ARBA00054078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769}.
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DR SMR; A0A3B6RSU9; -.
DR EnsemblPlants; TraesCS7A02G543400.1; TraesCS7A02G543400.1; TraesCS7A02G543400.
DR Gramene; TraesCS7A02G543400.1; TraesCS7A02G543400.1; TraesCS7A02G543400.
DR Gramene; TraesCS7A03G1323100.1; TraesCS7A03G1323100.1.CDS; TraesCS7A03G1323100.
DR Gramene; TraesWEE_scaffold_012067_01G000200.1; TraesWEE_scaffold_012067_01G000200.1; TraesWEE_scaffold_012067_01G000200.
DR OMA; ICAWIRW; -.
DR Proteomes; UP000019116; Chromosome 7A.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00892; PIKKc_ATR; 1.
DR FunFam; 1.10.1070.11:FF:000024; Serine/threonine-protein kinase ATR; 1.
DR FunFam; 3.30.1010.10:FF:000020; Serine/threonine-protein kinase ATR; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR056802; ATR-like_M-HEAT.
DR InterPro; IPR050517; DDR_Repair_Kinase.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR057564; HEAT_ATR.
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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR012993; UME.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF69; SERINE_THREONINE-PROTEIN KINASE ATR; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF23593; HEAT_ATR; 1.
DR Pfam; PF25030; M-HEAT_ATR; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF08064; UME; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00802; UME; 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};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1555..2163
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2274..2588
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2586..2618
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2618 AA; 293300 MW; 23279241613D0E24 CRC64;
METKVVLRLL NYTAPRFPGV FSNGRPAEVI RVIGRILPLF AEPDYQSIIF EPVWSLLSLL
RTGDREAYRQ FFLDAMVAVE DLQYVASKHT ESGCLLKCFC GSFSDILEST AIFSDLPERF
QPKNGPGVLI DLSGDMRWCS FATSLIRLIN KCLTDGTLHV EGIVTMPFVS AACSILCYGD
ESLHKVCFDF ARIVATVMTV EILPTETIIR SITSILSQDV NELSSIRDPD YDLSIVQTSR
SSELQAAMCN AYMRIVEVCS PQVWKPEILL KLLYLPKPYD KVTECIRLVV DKLGQSLVSV
DANDDRGSFQ EKSEVFELPK VGQKRVAQNQ ENTLYKRQKM SESRSTIGSF MAKLSPAGIG
HELAKDYAYD LQLSLNSRIK FLSPDNHNAY PLEPDIAIQV LSLLSLSFCV NPKTSLFISI
SKQVLSWIPW ICKQATEKCF FSFDMLLYFK ALQTVMLLRS FHPGDSKQFE DEAQLICVHS
EDLDYPLYVD LISLLKRVWS DGHVSTQTCL DKLKCLVVQV IAKIGNRLNI DCDLELLELA
IHSESVEVQN EALMSLPIIV LYSGPTMLGV MFKKLELCGD LGSDKVWKCV AFSLGFLSCL
NGTTDVTDKA GNSCKLFMDK DSKQPVSTLD LLLKGFWCPH CDNRTVNTKE QISIVDMAVL
ETENVALKHN ILKAHILFFK FLYAQTSKEC IISMVEVLPR VLRHSSKEVL LEMKIKWVNC
IDFLLLNGMK DVRDAFSLVV CCFLETRVMD ILFSDELGME GGTKELKFMD KIKQAFAEAE
DSHVLLTLLE STATIMQASD TQGEVFFCSF VLLIAQLDNH DPIVRKTASR LLHRCCTYSF
KGGIELFLSN NFRVRDDLYD YLSSRLLNHP VVINEFAEAV LGIKTEELIR RMVPSVIPKL
IVSHPDNDQA VITLHELANH LNTELVPLIV NSLPKVLSFA LFYEDGQHLP SVLQFYHTET
GSDSKEIFAA ALPTLLDEII CFPGESDHTE TDRRTTRISP TIQNIARILT GNDTLPEFLK
NDFVRLLNSI DKKMLHSDDL KLQKQALQRI RKLVEMMGPY LSTHAPKIMV LLIFATDKEA
LQMDGLDVLH FFIKQLAEVS STSIKYVMSQ VVAAFIPSLE KCRECPSVHL KKIVEILEEL
VVKNSKLLKQ HIRELPLLPS LPSLSEVNKV IQEARGSMTL QDHLKDAVDG LNHESLNVRY
MVACELSKLF KAKREDVTAL IIGEDTSDLD VISALIMALL KGCAEESRTM VGQRLKLVCA
DCLGALGAVD PAKFKVISCE RFKIECSDDD LIFELIHKHL ARAFRAASDT TVQDSAALAI
QELLKLAGCQ SLPKEDNGED SSSCEMSRRG QKLWGRFSSY VKEIIAPCLT SRFHLPSVND
AALLGPIYRP TMSFRRWIYY WIRKLTSHAT GSRYGIFSAC RGIVRHDMPT ALYLLPYLVL
NAVCYGTPEA RQSITDEILS VLNAAASESS GAIVQGVTGG QSEVCVQAIF TLLDNLGQWV
DDLKQEIALS QSNNAMAGRQ AGKLNDENCS NNGQDQLLVQ CSNVAELLAA IPKVTLAKTS
FRCQAHARAL AYFESHVREK SGSSNPAAEC SGTFSDEDIS FLMEIYGGLD EPDGLLGLAN
LRNSSSLQDQ LIINEKAGNW AEVLTLCEHA LQMEPDSVHR HCDVLNCSLN MCHLQAMIAH
VDGLVGRIPQ YKKTWCMQGV QAAWRLGRWD LMDEYLPEAD KGLVYSSTEN NASFDIGLAK
IFKAMTTKDQ FMVAEKIAQS KQALLVPLAA AGMDSYMRAY PYIVKLHMLC ELEDFNSLLG
DESFLDKSFN ADDPSFLKLT KDWDNRLKCT QSSLWAREPL LAFRRMVYNL SHMNSQVGNC
WLQYAKLCRL AGHYETAHRA ILEADASGAP NVHMEKAKHL WNIRKSDSAI AELQQTLLNM
PAEVLGNAVL SSLSSLSLAL PNAPISATQA SKENPDVSKT LLLYTRWIHN TGQKQSEEIK
TLYSRVTELR PKWEKGFFCM AKFLDDLLVD ARKRQEDKKF TGGVGSVTPG SAGSASAPAK
ERPWWELVPT VLLCYAKGLH KGHKNLFQAL PRLLTLWFEF GNIYIREGPS AEMKVVHDRM
LAVVRGCSKD LPTYQWLTVL SQLISRICHQ NGELVRVVRY IIQVVLQAYP QQALWMMAAV
SKSTVSARRE AAGQILKLAK KGVGKRSDYV ALFNQFPSLI EHLIKLCFHP GQPKARSINI
STEFSSLKRM MPLGIILPVQ LALTVTLPSY DSNMSGQSTF HPFSISEHPT IAGIADDAEI
LSSLQKPKKV VFLGSDGVAR PFLCKPKDDL RKDARMMEFN AVINRLLSKV PESRRRKLYI
RTFAVVPLTE DCGLVEWVPN TRGLRHILQD IYITCGKYDR MKTNSQMKRI YDVCHASKIP
EDEMMKTKIL PLFPPVFHKW FLTTFSEPAA WFRARVAYAH TAAVWSMVGH IVGLGDRHGE
NILIDATTGD CVHVDFSCLF DKGLQLEKPE VVPFRLTQNM IDGLGIAGYE GVFLKVCEIT
LLVLRGHKEA LMTVLETFIH DPLVEWTKAH KSSGGEVQNP QAQRAIANIT ARLQGVVVGV
NAAPSLPLSV EGQARRLIAE AVSHKNLGKM YIWWMPWF
//
