ID A0A6P5Z7H8_DURZI Unreviewed; 2745 AA.
AC A0A6P5Z7H8;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LOC111298112 {ECO:0000313|RefSeq:XP_022748507.1};
OS Durio zibethinus (Durian).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Helicteroideae; Durio.
OX NCBI_TaxID=66656 {ECO:0000313|Proteomes:UP000515121, ECO:0000313|RefSeq:XP_022748507.1};
RN [1] {ECO:0000313|RefSeq:XP_022748507.1}
RP IDENTIFICATION.
RC TISSUE=Fruit stalk {ECO:0000313|RefSeq:XP_022748507.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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 RefSeq; XP_022748507.1; XM_022892772.1.
DR GeneID; 111298112; -.
DR KEGG; dzi:111298112; -.
DR OrthoDB; 381190at2759; -.
DR Proteomes; UP000515121; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:TreeGrafter.
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:0000077; P:DNA damage checkpoint signaling; IEA:TreeGrafter.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:TreeGrafter.
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:000036; 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 SUPFAM; SSF48452; TPR-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:UP000515121};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1678..2291
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2402..2715
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2713..2745
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2745 AA; 307381 MW; F0358AA35596B812 CRC64;
MASNSNSKNL SSLVHELRER IAASSSTPPN NNINNNDDVL ETRFRAVLPN LLHAYVVPSS
SANEREVIAV LKLISHTARN FPGVFYHGKA SAILPVIGRI LPFFAEPAFR SRHGVIFDTI
GPLLSLLRTG SRDAYRMLFI DAMSVIEDIC YMGSHSVENS RIAEATELTL KCFHRSFSGN
LSDSTCLCDL PTSNKPIDGP GILINLLGRN RWQLFATWII KLVSKCLTEG TLYVEGLINT
SFVCAACSLL CYGDADLHMA CFDFARVIGS AMSFDIVPHE NLIQSITSIL SEDKEGLPVF
RNLEYDSSIG GCLRALHTSC PDDVVKLTAE NLVYVFPNSM WRTKSTELKV ALCTAYIRIS
RTCPPHIWRP EFLIHVLCCP EPCILLVDCF QVALSILGPN RVGGGTTELS NLGLSTSSDI
SIASPKVGEK RQIIDVGPFK IKRQKVDGEV KFSNTNVQGD IKLTGLVSYE REEGYADSMH
DSLLLFVETL NTPSVKHDAL RPDVALTALS LLSIAFCRYP QTNMSLCIFR QMQTWIPWIC
EQVHVLQAKQ GSPITLDISI YLEGIHSMLL IQGSLFFEDN LFKNENNEVD INVVLKLPWT
HTLVVPKSHL PWKAKLISVQ VVSKLGPRFS TGRGFEVLDL ALHDEIEEVR KEALVSMPVI
VVWSGLDTLA NMFRRLEFLE IDKHEKVKKV IPYCLGFLSC LYGSYHGVGG IEICSCKLFL
NIKDEKQIET LDFLLQGFWC SKCDRCVLHD DEPNSRIMHL PAAQILESGY NFDFVYLQSL
YFNLLYDESS EEVQLACVGV IRRILLHGPQ DVLLKMRTKW LRCIDFLLLN RKKYVREAFC
TQISSFLQGP ILSFLFSDGT ASCKSGEENF LNMIKHALAA TENPQIIETL LESTAEIMMA
VDVYSQLFLF SLILLVDQLD NLHLTVRMSA SRLIHRSCCF HFKGGFELLL SKAVHIRNEL
FDYLSISLAG RPKMVKEFAE AVLGVETEEL LKKIIPVVLP KLVVSQQDNN QAVDTLHELA
KCLNTDVVPL IVNWLPKVLA FALRQADEKE LISALQFYHA QIGSNNREIF AAALPALLDE
LICFLDGGDL NEINKRLERV PQMIKNVARV LTDAEDLPGF LRNHFVGLLN SIDRKMLHSE
DFSLQKQALK RIEMLIKMMG SHLSTYVPKL MVLLMHAIGK ESLQSEGLSV LHYFIVQLAM
VSPSSTKHVI SQVFAALIPL LEKATENSSA HLHKVVQILE LVLKNRVILK EHIHEFPLLP
SIPALTEVNK AIQEARGAMT FKNQLRDVVA GLNHENLNVR YMVVSELNKL LKSRKEDVAA
LVNGEGGSDM DILSSLITSL LRGCAEESRT AVGQRLKLMC ADCLGALGAV DPAKVRNISC
QRFKIQCSDD DLIFELIHKH LARAFRAAPD TVVQDSAALA IQELLKIAGC EASMDENVSP
MSQTNVDNEP SEATALGIRT SDSSSGNNSR GQKLWDRFSN YVKEIIAPCL TSRFQLPNVA
DSTSAGPIYR PSMSFRRWIF SWIKKLTAHA IGSRASIFNA CRGIVRHDMQ TAIYLLPYLV
LNAICHGTEE ARHGIAEEIQ SVLNAAASEN SGAAVYGVTG GQSEVCIQAV FTLLDNLGQW
VDDVKQELAL SQSFQSPASR QQASKSKDQN SVLSESQDQL ILQCKYVSEL LSVIPKITLA
RASFRCQAYA RSLMYFESYV QGKSGSFNLA AERSGIFEDE DISYLMEIYS CLDEPDGLSG
LACLRKSLSL QDQLLINKKA GNWAEVLTAC EQALQMEPTS VQRHSDVLNC LLNMCHLQAM
VTHVDGLISR VPKYKKTWCM QGVQAAWRLG RWDLMNEYLS GADEEGLLCS SSESNASFDL
DVAKILQAMI KKDQFSVAEK IALSRQALIA PLAAAGMDSY TRAYPMIVKL HLLRELEDFH
TLLIDESFLE KSFHLDDCGF SKVMENWENR LRFTQPSLWA REPLLAFRRL VFGASSLGAQ
VGSCWLQYAK LCRLAGHYET ANQAILEAQA SGAPNVHMEK AKLLWSTRRS DGAIAELQQS
LLNMPVEVVG SAAISSITSL SLVPLNPQPL PGDTQAMNEN QEIAKTLLLY SRWIHYTGQK
QKEDVICLYS RVRELQPKWE KGYFYTAKYC DEVLVDARKR QEENFELGPR IVPSASALTA
SSNSNTEKHW WSYLPDVLLF YAKGLHRGHK NLVQALPRLL TLWFDFGSIY QRSAAASSKD
LKNVQVKVTS IMRGCLKDLP TYQWLTVLPQ LVSRICHQNE EIVKLVKNII ISVVRQYPQQ
ALWIMAAVSK STVPSRRAAA AEIIQAARKG FSQGNSGNNL FAQVASLIDH LIKLCFHAGQ
PKSRTINIST EFSALKRMMP LGIIMPIQQS LTVTLPTYDM NLSESLSSDI FSGMELPTIS
GIADEAEILS SLQRPKKIVL LGSDGIERPF LCKPKDDLRK DARMMEFTAM INRLLSKYPE
SRRRKLYIRT FAVIPLTEDC GMVEWVPHTR GLRHILQDIY ITCGKFDRQK TNPQIKRMYD
QCQGKIPEDE VLKNKILPMF PPVFHQWFLT TFSEPAAWFR ARVAYAHTTA VWSMVGHIVG
LGDRHGENIL FDSTTGDCVH VDFSCLFDKG LQLEKPELVP FRLTQNMIDG LGITGYEGIF
LRICEITLSV LRTHRETLMS ILETFIHDPL VEWTKSHKSS DVEVQNPHAK RAISNIEARL
QGVVVGVGAA PSLPLAVEGQ ARRLIAEAVS HKNLGKMYIW WMPWF
//
