ID A0A162EDE1_9CRUS Unreviewed; 2568 AA.
AC A0A162EDE1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=APZ42_026490 {ECO:0000313|EMBL:KZS09380.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS09380.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS09380.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS09380.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS09380.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZS09380.1}.
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DR EMBL; LRGB01002076; KZS09380.1; -; Genomic_DNA.
DR STRING; 35525.A0A162EDE1; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
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-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00892; PIKKc_ATR; 1.
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; IPR016024; ARM-type_fold.
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; 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; 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 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:UP000076858};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2568
FT /note="Serine/threonine-protein kinase ATR"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007833633"
FT DOMAIN 1536..2113
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2221..2536
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2536..2568
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1450..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2568 AA; 291872 MW; 2569812C68CC0672 CRC64;
MHGVCKHPLF VILASGMATV LLNDEAEQSR KLSMDVQDTK NTTLSAVSNH RKMMALPALK
ILADLDHSEK SFDVLMSVMD RCCREPNNQS VFLGCGDDEL DHKLAFAYTK WFLGRFSIIF
TRKSYMKAFN SFIELNVKIL NLFRDKEPNQ FRSLVNEFVN LLKELAVIVS QRSNEEVHTH
QSFKLHSFVP KEPVALATDC LLKMDGLELN SLQECSLLQS NVTKIIAMSA DGILQYDPQL
CSKLVCILLD QLNYGEICTF KSTLNCLGQI LVHDCSTRVL EIFLHYAYRL VNLMMDENNR
VWNENSENSS SEIGVALIEC LSRLSNPFGS CSMTNHQYLR LISFILLREQ FHQPIVLNNL
LQSMLGALQR FTCQETTSLC RFTPDLWIKL LKHSYAAIPP MLIILQSEMA PGDSPIEISE
PLAKRLKIDF LPTLTSVTLW EQLKSRWTLI LDQQVTDQPV EMADITALVR IAISGVKLKL
KWREMNSVMD DADFENLNGK ICQILLTGEI NSENMDNVIA IICEYLTSCI PLTYAGIDKN
VALAWFALSA LPWLSSVSES CDLEVKWIQV SRKFRPSFLK HQSSFASCFV KFPVGFFKPW
AVEIGLKIFD IEFLQADAGT LIPSLPWIVR HSKSFREAIS QCLTTILASG SKEEIRELTK
TGTDLVCALS GKTNVVNNPE DGLSLRCTHN LENLATSMKI SIVPENMALF FLEFVFDEND
HSVLHRVELF RSVLYHSART EALRLSVTKK LHKAAQMSVE KNFAYLQSTV LKCTTILVQF
WKETVMSDCF HVVFKILLLS SYGAPVMCWT SSTVKEIASK LNVTPEMLFQ RHVTIVCDVL
LSNPDLEWRN SLLSLAPEIF MSSSHMVSNV HQWLLLLIPT LIPRLVVERA KAPSPFFEEI
CNQMNKNPSE LIVKYFSDIY VHILLYCDAN EQSAVTSYVE RITKLKLPLL RAPNFQSVHN
DLVIQLHSQR DRVLKALKVF ADEDKSAAVS ASTSTAKNRC QTKSLNSLGD YLRPRFLGIL
VHLDSVLLSK VLSDHIKIEA LSSLSDLLHL MGTENIVAVR LKVLATLRTA LQLTEEPFPQ
LNASAWDAFV RILGVQDLGP LVSQIAVSIL PLHSSCAEQI RSILYYIVVE NAETLKEHLK
DLHFLPELPG LEDVVYSLKK TCSTNTSIPE QLSFLMRNIS HEDFEVRMQS LSHLKSIVQK
NFDIIQQLIM GTNDTSEAVL TRLISALLKG CSVREDELLL LYGKCFGYLG AVDPGRLTFS
DQHNGDSTVY TATLIDDDFT FHLLGLLARS FLAPRNSQNL SILSFTIQQI LKIYNSEDDS
SKLFESALWN RLPEQLRVAF SPLTSSRYAL KQQTESGPAP FPLYRSTAGK SYGNWLYNWT
AGLIKKVTHP LAQQIFNACL PTVRRDLNIN RYLLPYVVIT ALWSSPVEES ARIGEEIMAV
LTDRGLQRSP RRMMKRYSSS ASATDVSSQG SSPKDSADAN LHQSSMQGIF HLLDHLKKWL
KQKSNSHRSN RKDRSITLDK EYKVVQELVD RIPNDLLARA AYQCQAYARA ILHLEAHLKA
NPIQLRGQLG FLQKLYVAMD EPDGVAGVCA IRDQEPSLEE NITAYEATGR LQDAFSCYER
ISQREDCSLE FYQGMLRCLL NLDLPQGSLT MANGLLQNCP EWRRNLDDYR AECGWRLGQW
DLLEDVVKPY DLTSANNDAA VGWGVGLGQA LLATKTNDLP KMEKCLRSVR LKQMRVISAI
NLERNSYPRA YENFVRLHIL SEMESAVSLL DPALIAKETA FRARFSELLK NWNQRLDGVQ
ASVRYTEPVL IVRRVVLKLI GQQVETKHPQ LMEEIEAEIG NSWLVSARLA RKAAHFQRAH
ILQLVASTSP CPPPAIYMEQ AKLHWAKGEQ DQAITVLKRG VEKRFPDLQA VQIEAAGLEP
DKFTSDILEC LKAKLLLARY YDETGHADMN TIIRYYKEVT EISKVWEEGF FRLAGYYDVL
WNNLEGTKEN HLDMARYIVT NLGRSMIYGS QFIYQAMPRM LSLWMELGTA EAENPKIYKN
SSSRVKMTDV TRAIDIAQEK IPAYKFLTAF PQLISRICHP HPEVAALLRR IIAKTLVSHM
QQCMWMMISV LKSSYSVRAK RCREIIDMVA SNQPSVRKFF GDATNLADRL VELANKPVED
GVMVLSVEKA FRALPSLLSQ SHFSKIMVPL QWLMTVTLPT TPGENVEHNP FPKDSVYIVG
VEDTVEVMHS LQKPKKISIR GSDGKLYVFL CKPQDDLRKD FRLMEFNQLI NRYLLRDPDS
RKRNLHIRTY GVIPLNEDCG LIEWIPNLIG LRLVLNRIYR EKGCLMSNTE LRKRTPHLRD
TLLRKRELFE KEILPRYPSV FSEWFLSTFP DPQDWFLARL SYVRTTAVMS MVGFIVGLGD
RHGENILFDA VCGDAVHVDF SCLFNKGLSF EWPEQVPFRL THNMIEAMGA TGVEGSFRKC
CEVTLHVLRK EIDTLLSVLK PFVHDPLVEW SKKSVNKGRA DLPEIKNEQA LEHVENIKMR
LQGYFQQPNS KNKMKYRLSV EGQVNQLIAE ATNVDNLCQM YIGWAAYM
//
