ID G1QY16_NOMLE Unreviewed; 2615 AA.
AC G1QY16;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=ATR {ECO:0000313|Ensembl:ENSNLEP00000005837.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000005837.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000005837.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000005837.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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 EMBL; ADFV01028510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01028511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01028512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01028513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01028514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSNLET00000006145.3; ENSNLEP00000005837.2; ENSNLEG00000004792.3.
DR eggNOG; KOG0890; Eukaryota.
DR GeneTree; ENSGT00940000155714; -.
DR HOGENOM; CLU_000178_2_1_1; -.
DR TreeFam; TF101183; -.
DR Proteomes; UP000001073; Chromosome 8.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048584; P:positive regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0080135; P:regulation of cellular response to stress; IEA:UniProt.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd00892; PIKKc_ATR; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR021133; HEAT_type_2.
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:SF128; SERINE_THREONINE-PROTEIN KINASE ATR; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 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; 2.
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; PS50077; HEAT_REPEAT; 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 DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 800..834
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1614..2159
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2270..2575
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2583..2615
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 413..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2615 AA; 298115 MW; 7F11EB32C7A524E9 CRC64;
LSSWGLQVSF NLYFSATPEE YNTVVQKPRQ ILCQFIDRIL TDVNVVAVEL VKKTDSQPTS
VMLLDFIQHI MKSSPLMFVN VNGSHEAKGS CIEFSNWIIT RLLRIAATPS CHLLHKKICE
VICSLLFLFK SKSPAIFGVL TKELLQLFED LVYLHRRNVM GHAVEWPVLM SRFLSQLDEH
MGYLQSAPLQ LMSMQNLEFI EVTLLTVLTR IIAIVFFRRQ ELLLWQIGCV LLEYGSPKIK
SLAISFLTEL FQLGGLPAQP ASTFFSSFLE LLKHLVEMDT DQLKLYEEPL SKLIKTLFPF
EAEAYRNIEP VYLNMLLEKL CVMFEDGVLM RLKSDLLKAA LCHLLQYFLK FVPAGYESAL
QVRKVYVRNI CKALLDVLGI QVDAEYLLGP LYAALKMESM EIIEEIQCQT QQENLSSNSD
GISPKRRRLS SSLNPSKRAP KQTEEIKHVD MNQKSILWSA LKQKAESLQI SLEYSGLKNP
VIEMLEGIAV VLQLTALCTV HCSHQNMNCH TFKDCQHKSK KKPSVVITWM SLEFYTKVLK
SCRSLLESVQ KPDLEATIDK VVKIYDALIY MQVNSSFEDH ILEDLCGMLS LPWIYSHSDD
GCLKLTTFAT DLLTLSCRIS DSYSPQAQSR CVFLLTLFPR RIFLEWRTAV YNWALQSSHE
VIRASCVSGF FILLQQQNSC NRVPKILIDK VKDDSDIVKK EFASILGQLV CTLHGMFYLT
SSLAEPFSEH GHVDLFCRNL KATSQHECSS SQLKASVCKP FLFLLKKKTP SPVKLAFIDN
LHHLCKHLDF REDETDVKAV LGTLLNLMED PDKDVRVAFS GNIKHILESL DSEDGFIKEI
SICFWDIGDI YVAAKGDLVP FALLHLLHCL LSKSASVSGA AYTEIRALVA AKSVKLQNFF
SQYKKPICQF LVESLHSSQM AALPSTPCQN ADMRKQDVAH QREMALNTLS EIANVFDFPD
LNRFLTRTLQ VLLPDLAAKA SPAASALIRT LGKQLNVNRR EILINNFKYI FSHLVCSCSK
DELERALHYL KNETEIELGS LLRQDFQGLH NELLLRIGEH YQQVFNGLSI LASFASNDDP
YQGPRDTISP ELMADYLQPK LLGILAFFNM QLLSSSVGIE DKKMALNSLM SLMKLMGPKH
VSSVRVKMMT TLRTGLRFKD DFPELCCRAW DCFVRCLDHA CLGSLLSHVI VALLPLIHIQ
PKETAAIFHY LIIENRDAVQ DFLHEIYFLP DHPELKKIKA ILQEYRKETS ESTDLQTTLQ
LSMKAIQHEN VDVRIHALTS LKETLYKNQE KLIKYATDSE TVEPIISQLV TVLLKGCQDA
NSQARLLCGE CLGELGAIDP GRLDFSTTET QGKDFTFVTG VEDSSFAYGL LMELTRAYLA
YADNSRAQDS AAYAIQELLS IYGCREMETN GPGHQLWRRF PEHVREILEP HLNTRYKSSQ
KSTDWSGVKK PIYLSKLGSN FAEWSASWAG YLITKVRHDL ASKIFTCCNI MMKHDFKVTI
YLLPHILVYV LLGCNQEDQQ EVYAEIMAVL KHDDQHTINT QDIASDLCQL STQTVFSMLD
HLTQWARHKF QALKAEKCPH SKSNRNKVDS MVSTVDYEDH QSVTRFLDLI PQDTLAVASF
RSKAYTRAVM HFESFITEKK QNIQEHLGFL QKLYAAMHEP DGVAGVSAIR KAEPSLKEQI
LEHESLGLLR DATACYDRAI QLEPDQIIHY HGVVKSMLGL GQLSTVITQV NGVHANRSEW
TDELNTYRVE AAWKLSQWDL VENYLAADGK STTWSVRLGQ LLLSAKKRDI TAFYDTLKVV
RAEQIVPLSA ASFERGSYQR GYEYIVRLHM LCELEHSIKP LFQHSPGDSS QEDSLNWVAR
LEMTQNSYRA KEPILALRRA LLSLNKRPDY NEMVGECWLQ SARVARKAGH HQTAYNALLN
AGESRLAELY VERAKWLWSK GDVHQALIVL QKGVELCFPE NETPPEGKNM LIHGRAMLLV
GRFMEETANF ESNAIMKKYK DVTACLPEWE DGHFYLAKYY DKLMPMVTDN KMEKQGDLIR
YIVLHFGRSL QYGNQFIYQS MPRMLTLWLD YGTKAYEWEK AGRSDRVQMR NDLGKINKVI
TEHTNYLAPY QFLTAFSQLI SRICHSHDEV FVVLMEIIAK VFLAYPQQAM WMMTAVSKSS
YPVRVNRCKE ILNKAIHMKK SLEKFVGDAT RLTDKLLELC NKPVDGSSST LSMSTHFKML
KKLVEEATFS EILIPLQSVM IPTLPSILGT HANHASHEPF PGHWAYIAGF DDMVEILASL
QKPKKISLKG SDGKFYIMMC KPKDDLRKDC RLMEFNSLIN KCLRKDAESR RRELHIRTYA
VIPLNDECGI IEWVNNTAGL RPILTKLYKE KGVYMTGKEL RQCMLPKSAS LSEKLKVFLE
FLLPRHPPIF HEWFLRTFPD PTSCRSAYCR STALMSMVGY ILGLGDRHGE NILFDSLTGE
CVHVDFNCLF NKGETFEVPE IVPFRLTHNM VNGMGPMGTE GLFRRACEVT MRLMRDQREP
LMSVLKTFLH DPLVEWSKPV KGHSKAPLNE TGEVVNEKAK THVLDIEQRL QGVIKTRNRV
TGLPLSIEGH VHYLIQEATD ENLLCQMYLG WTPYM
//