ID A0A1D2NE23_ORCCI Unreviewed; 2846 AA.
AC A0A1D2NE23;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=Ocin01_03204 {ECO:0000313|EMBL:ODN03482.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN03482.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODN03482.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODN03482.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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:ODN03482.1}.
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DR EMBL; LJIJ01000072; ODN03482.1; -; Genomic_DNA.
DR STRING; 48709.A0A1D2NE23; -.
DR OMA; TERRENH; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000094527; 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 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 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, ECO:0000313|EMBL:ODN03482.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1781..2390
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2496..2805
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2814..2846
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2297..2316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2846 AA; 324964 MW; F2E18612477C4332 CRC64;
MSKRKRSSES NDLNTSNRAS KAASHKNPSV HNNHGRNRRG GVESDDLHEV VDLEADDDEP
EAAANIGVGV SASKKKRMEK AKESRTMKKD IKLDNRQPST SLTPPLSAEP VSEREPEVFC
SAASNIRSTK NGDGNSNSQY LTPSDSEPLE FKRPGVPLFK KPYPPVLPGP SSSSHQTVVV
GEKMGPTEKQ LQATQKSREM RKAIIDVLQA TLEDASKCSI ASVPDLLENF LPCIKRMSFI
FASRRYPGQR DVDDLSGEDE ISDLARWWLF GMTALLFSTP ADGVKKMKEA VKYMIRTVCQ
FLCNGHPKVV DSIIPLLINV IRDLTVRGDN DQMRVLKLDL PSLECSSSGP NSQKSIYNIQ
LTVDNEWAIP HFMQSISAVL PRIFFYHFHL RHVLVELLNR FLSRQSCESV ETAVTSYSSP
AMPAIAYLTE DCIVSLIQRL VESPSLPGIN LHQLSLLVGQ HGTTFDAISE DIGMNLLPLV
LPEYLHSKNF SLLYHNENTV IIADAFRSLM DTVPIHHSQI ISCESIKFSK LVSLAGLNVI
LNPLLEKILL AELENESTGS GPNFQANWSL QHPLRIVKVW EVSQLWSKIM HQWESSLYTV
SSHGTPNHEG AVNFMKRSSV FIKLAKNLWN GVYPLLTTKR VRFIFFELKH LQRWFSSRDG
YEIHLAILET MESFHACNWL GIKLSPKVLT NLISIPGWPW IANFDAFLPQ KYKPLHSFTR
LDVSNIIGSK VLVAKSIRVL GSEVFRPWTH FVTEVYSYII NAESTLANSV LVIELLDMIA
DVRWPFKQMP IKIIFTFVAQ IVNREEWKVN SGLRTSLANA IVALPCLCCS VNLGGMNPGN
EFSIIKSGCH ICSRKQENLA NMAQPSIPDY LTQRIASLAS PLLRSKFLLV KFQLSDLIVR
FASHSEKSST QVTLPFMHVV VTGKVDLSEN VFQKIGVLLT QVGNLNNPCE YRLGLAQQIF
TSLRRLMVNS TSNRKISTNK LSKVLKGFFQ LATYPLSLSV FVELVKCIVF FLSQTDKSEV
TILCQKIVAK YASVYQCQPF DLIVRIRQDL SREIIKVATK AFFVPPESRD YYVNVQQCAD
FLARLFLLGE FRYGKMFISY YYPAMLEKMV PKLPTRYGYR FLLSAMASHS KQIEQAVLQD
WVMLYYPTLL LDHNSETVST CLQFLKNHYG FVAIFAAKQQ EQRILNEALC RLSDQREKLL
RCLPHLCKFD EDSSQMMYNA GTSKAMSILE IQELLSKRLL GFFLHLDTKL QSRIETVESK
KKILRSFTSL LDLMKEKKIT PLRSKVYKTL SSMTKEGPEY FKELFDAWKV FADNLDAEHF
GPMASQILAA VLPLRNSPLR NDVDCLISHF VVFKKKLTEP HYHELYFLIE HLKKGDNEDT
RTKSEKAKVI NAVGGKINEM KNNWLEYFMM IVKESSHENV HIRYQAFSKL LDVFRHESSN
FENKVLTRGQ MHVSQVISAL LAGLRGDSSN EKLKTLIIEC LGNVGALDPV RFRSEDDDLR
TKSRCTTYSG QMTTFAVLYL QELIREFQEA KDTTSFDYCA CLIQQVLQEF KVFPTNEDPI
WSCISPASQH HIMHLLTTKY QMDTTSPPPT VYSPIYLSEH GLTFDSWLLN WLTVLISCIT
TEELRAHSLF NKNKYLLRRN PRIAAFIIPY VTMYAIFCGN AEQREEIVRE IITVLERWTV
LDAMKVKAHS TVPIKDSQTE FGVKEELSVE NESVFHFRCT QVIFSVLDHL LRSFKLAKRK
WGLKLASERS RGPSSKTIHP PMSEVNMKNI EAVLEKIPAN LISQVAFDCG SYTIALYYLE
QELRTNPSNE KLQRNLGYLQ RIYVSLNDMD SVIGIAAVRD SDPSLCEIVL ENIAKWKMED
CVRNLEKMTA NDPSDLIAHN ALVQAYLNLD EPRKADTLIR GTIQKRSEWE LAFQDVQLES
LVKLKNWPEL NTLVGRVEMT PSSCILDDTS FTWNTDLVRT ISKIQQMLFN DATEIVERIK
SKMIAPLVAA SEEMYPYKRA YHNVVQLHIL TEMEDAIKLL QTHLNYIASG KGQSTQGKLF
HDVKRMMTRW DARFRNVSKS MTVIDQILNV RKCLFEIMKT TFHTNGSVCE VLNSAIRECW
LDVARDASKC GNFIRADNCL MEAKKFMSPK VLIEEAKILS RKGEKEHAIS VLQKGIALYF
PQKDTWKEQS SSDHASSYET LDARILCSKA LLLLAKLCEE EKLLNMEDYI AKYKEASDVY
RDSEKNYFTL GSYHDRLWSS TERRENHFHI QATVVRYYSQ SLLYGCKYVY QSLPRLLSIW
FDFAAALQSG EYSKVNSSSS KSASSSSSNQ SNDNIPIMKP EDVLEIMAAA IKRMVAGIPA
YILITAFSQL ISRLCHSHRK TWTDLREIIV SIICAHPHQT LWMIMAVTKS LNSQRKKRCL
EIYTSVEKTK SELKPLIRSY TELTAKFLAV SDYPIERNKG SLTSVCPSLP NMIRNSAFGK
VSIPFQIFLN PSLPRVGNNH KEHEPFPESL VYIEDIEDNI DVMPSLIRPK KLTLRASNGK
SCGLMCKPKD DLRKDSKVME VNNVVNWYLN QITESSQRRL HVRTFSVVPL NEECGLLEWV
PNLQGLRPIL LSLYKEKNIT PNNRDLRCTI ELHDTLEVKM EKFVEKMVKP HPPVFHEWFF
NNFNDHQSWY EARMAYIRTT AVMSVVGYIM GLGDRHGENI LVDSATGETV HVDFNCLFNK
GETFEWVERV PFRLTQNMID AMGPLGYEGV FRRSCEIVMN MFREHKSVFL SVLRPFVFDP
LVEWNRNRDD RRGCSSAAGQ HGGELTNEKA VETMKYIRNR LNGTARNLMR DINTELSVEA
QVKYLIDEAT SIENLCQMYI GWAAFF
//
