ID A0A5N4EIQ6_CAMDR Unreviewed; 2441 AA.
AC A0A5N4EIQ6;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Ataxia telangiectasia and Rad3-related protein {ECO:0000256|ARBA:ARBA00084048};
GN ORFNames=Cadr_000000204 {ECO:0000313|EMBL:KAB1283312.1};
OS Camelus dromedarius (Dromedary) (Arabian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9838 {ECO:0000313|EMBL:KAB1283312.1, ECO:0000313|Proteomes:UP000299084};
RN [1] {ECO:0000313|EMBL:KAB1283312.1, ECO:0000313|Proteomes:UP000299084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Drom800 {ECO:0000313|EMBL:KAB1283312.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAB1283312.1};
RX PubMed=30972949; DOI=.1111/1755-0998.13020;
RA Elbers J.P., Rogers M.F., Perelman P.L., Proskuryakova A.A.,
RA Serdyukova N.A., Johnson W.E., Horin P., Corander J., Murphy D.,
RA Burger P.A.;
RT "Improving Illumina assemblies with Hi-C and long reads: an example with
RT the North African dromedary.";
RL Mol. Ecol. Resour. 19:1015-1026(2019).
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:ARBA00048977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000256|ARBA:ARBA00048977};
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:ARBA00048659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000256|ARBA:ARBA00048659};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus envelope {ECO:0000256|ARBA:ARBA00004259}.
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:KAB1283312.1}.
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DR EMBL; JWIN03000001; KAB1283312.1; -; Genomic_DNA.
DR Proteomes; UP000299084; Unassembled WGS sequence.
DR GO; GO:0070310; C:ATR-ATRIP complex; IEA:UniProtKB-ARBA.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA 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:0006260; P:DNA replication; IEA:UniProtKB-ARBA.
DR GO; GO:0000723; P:telomere maintenance; IEA:TreeGrafter.
DR CDD; cd00892; PIKKc_ATR; 1.
DR FunFam; 1.10.1070.11:FF:000009; Putative serine/threonine-protein kinase ATR; 1.
DR FunFam; 1.25.10.10:FF:000149; Serine/threonine-protein kinase ATR; 1.
DR FunFam; 1.25.40.10:FF:000142; Serine/threonine-protein kinase ATR; 1.
DR FunFam; 3.30.1010.10:FF:000011; serine/threonine-protein kinase 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; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR056802; ATR-like_M-HEAT.
DR InterPro; IPR056803; ATR-like_N-HEAT.
DR InterPro; IPR050517; DDR_Repair_Kinase.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR057564; HEAT_ATR.
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: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; PF25032; N-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; 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 Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KAB1283312.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000299084};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 656..690
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1457..1985
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2093..2401
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2409..2441
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 422..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..448
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2441 AA; 277987 MW; 5872AFA92E607046 CRC64;
MGEHGLELAS MIPALRELGS ASPEEYNTIV QKPRQILCQF IDRILTDVNV VALELVKKTD
SQPTSVMLLD FIQHIMKSSP LMFVNVNGSH GQNEAKGSCI EFSNWIVTRL LRIAATPSCH
MLHEKICEVI CSLLFLFKSK SPAIFGVLTK ELLHLFEDLI YLHERDAEGH SVEWPVVVSR
FLSQLDEHVG YLQPAPLQFM NMQNLELIEV TLLTVLIRII AVVFFRRQEL LLWRIGCGLL
EYGSPKVKSL AISLLTELFE LGGLPAQPAS TFFSSFLGLL KHLGEMDADQ LKLYEEPLSK
LIKTLFPSEA EAYRNIEPVY LSMLLEKLCV MFEDGVLMQL KSDLLKAALC HLLQYFLKYV
PAGYESALQV RKVYVRNICR ALVDVLGVQI NAEYLLGPLY AALKMESMEI IEEVQCQIQQ
EDLSSDSDGL SPKRRRLSSS LKSSKKAPKQ TEETKHVDMN NKSILWSALK QKLESLQIFL
ELNSLKNPVI ETLEGIAVIL QLTALCTVHC SHQNMDCHNF KDCQQKCKKK PSVVITWMSL
DFYTKVIKSC RTLLESIQKL DLEAVIDKVV KIYDALIYIQ VNTSFEDHIL EDLCGMLSLP
WIYSHSDDDS LKFTTFATNL LTLSQKISDS YSFIDNLCHL CKHLDFREDE TDVKTVLGTL
LNLMEDPDKN VRVAFSGNIK HILESLDAED GFIKELFVLR MKEAYTHAQI SRNNELKDTL
ILTTGDIGRY IWQLWAAKGD LVPFALLHLL HCLLSKSASV SGAAYTEIRA LVAAKSVKLQ
NFFSQYKKPI CQFLVESLHS SQMTALPSTP CQNAEMRKQD VAHQREMALN TLSEIANVFD
FPDLNRFLTR TLQVLLPDLA AKASPAASAL IRTLGKQLNV NRREILINNF KYIFSHLVCS
CSKDELERAL HYLKNETEIE LGSLLRQDFQ GLHNELLLRI GEHYQQVFNG LSILASFASS
DDPYQGPRDI TSPELMADYL QPKLLGILAF FNMQLLSSSV GIEDKKMALN SLMSLMKLMG
PKHVSSVRVK MMTTLRTGLR FKDDFPELCC RAWDCFVRCL DHAYLGSLLS HVIVALLPLI
HIQPKETAAI FHYLIIENRY WVIAETSEST DLQTTLQLSM KAIQHENVDV RIHALTSLKE
TLYKNQEKLI KYATDSETVE PVISQLVTVL LKGCQDANSQ ARLLCGECLG ELGAIDPGRL
DFSTTETQGK DFTFVTGVED SNFAYGLLME LTRAYLAYAD NSRAQDSAAY AIQELLSIYD
CREMQTDGSG HQLWRRFPEH VREILEPHLN TRYKSSQKST DWSGVKKPIY LSKLGNNFAE
WSASWAGYLI TKVRHDLASK IFTCCSIMMK HDFKVTIYLL PHILVYVLLG CNQEDQQEVY
AEIMAVLKHD DQHTIGTQDS ASDLCQLSTQ TVFSMLDHLT QWARHKFQAL NAEKFPQNKS
NRNKVDSVVV QEEYERAMNQ GKQAITIHMR NAGLSLGKLY AAMHEPDGVA GVSAIRKAEP
SLKEQILEHE SIGLLRDATA CYDRAIQLEP DQIIHYHGVV KSMLGLGQLS TVITQVNGVH
ANRSEWTDEL NTYRVEAAWK LSQWDLVENY LAADGKSTTW SVRLGQLLLS AKKRDMTTFY
DTLKLVRTEQ IVPLSAASFE RGSYQRGYEY IVRLHMLCEL EHSIKPLFHQ SAGDNSQEDS
LNWIARLEMT QNSYRAKEPI LALRRALLSL NKRPDYNEMV GECWLQSARV ARKAGHHQTA
YNALLNAGES RLAELYVERA KWLWSKGDVH QALIVLQKGV ELCFPENKTP TESKNMLIHG
RAMLLVGRFM EETANFESNA VMKKYKDVTL FLPEWEDGHF YLAKYYDKLM PMVTDNKMEK
QGDLIRYIVL HFGRSLQYGN QFIYQSMPRM LSLWLDFGAK AYEWEKAGRS DRAQMRNDLA
KINKVITEHT NHLAPYQFLT AFSQLISRIC HSHDEVFVVL MEIIAKVFLA YPQQAMWMMT
AVSKSSYPMR VNRCKEILNK AIHMKKSLEK FVGDATRLTD KLLELCNKSV DGSSSTLSMS
THFKMLKRLV EDATFSEILI PLQSVMIPTL PSIPGAHANH EPFPGHWAYI AGFDDTVEIL
ASLQKPKKIS LKGSDGKFYI MMCKPKDDLR KDCRLMEFNS LINKCLRKDA ESRRRELHIR
TYAVIPLNDE CGIIEWVNNT AGLRPILTKL YKEKGVYMTG KELRQCMLPK SAALSEKLKV
FREFLLPRHP PVFHEWFLRT FPDPTSWYSS RSAYCRSTAV MSMVGYILGL GDRHGENILF
DSLTGECVHV DFNCLFNKGE TFEVPEIVPF RLTHNMVNGM GPMGTEGLFR RACEVTMRLM
RDQREPLMSV LKTFLHDPLV EWSKPVKGHS KASLNETGEV VNEKAKTHVL DIEQRLQGVI
KTRNRVTGLP LSIEGHVHYL IQEATDENLL CQMYLGWTPY M
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