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ATR1_DICDI
ID   ATR1_DICDI              Reviewed;        3157 AA.
AC   Q54ER4;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable serine/threonine-protein kinase atr1;
DE            EC=2.7.11.1;
DE   AltName: Full=Ataxia telangiectasia and rad3 related protein 1;
GN   Name=atr1; ORFNames=DDB_G0291380;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16596165; DOI=10.1371/journal.pgen.0020038;
RA   Goldberg J.M., Manning G., Liu A., Fey P., Pilcher K.E., Xu Y., Smith J.L.;
RT   "The dictyostelium kinome -- analysis of the protein kinases from a simple
RT   model organism.";
RL   PLoS Genet. 2:E38-E38(2006).
CC   -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC       signaling upon genotoxic stresses such as ionizing radiation (IR),
CC       ultraviolet light (UV), or DNA replication stalling, thereby acting as
CC       a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000177; EAL61674.1; -; Genomic_DNA.
DR   RefSeq; XP_635176.1; XM_630084.1.
DR   STRING; 44689.DDB0229332; -.
DR   PaxDb; Q54ER4; -.
DR   PRIDE; Q54ER4; -.
DR   EnsemblProtists; EAL61674; EAL61674; DDB_G0291380.
DR   GeneID; 8628122; -.
DR   KEGG; ddi:DDB_G0291380; -.
DR   dictyBase; DDB_G0291380; atr1.
DR   eggNOG; KOG0890; Eukaryota.
DR   HOGENOM; CLU_225616_0_0_1; -.
DR   InParanoid; Q54ER4; -.
DR   OMA; ASRICHK; -.
DR   PhylomeDB; Q54ER4; -.
DR   Reactome; R-DDI-3371453; Regulation of HSF1-mediated heat shock response.
DR   PRO; PR:Q54ER4; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; ISS:dictyBase.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR   GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR   Gene3D; 1.10.1070.11; -; 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; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR012993; UME.
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; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; DNA damage; DNA repair; Kinase;
KW   Nucleotide-binding; Nucleus; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..3157
FT                   /note="Probable serine/threonine-protein kinase atr1"
FT                   /id="PRO_0000376001"
FT   DOMAIN          2042..2714
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   DOMAIN          2817..3121
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          3125..3157
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT                   ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1283..1319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2823..2829
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2989..2997
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          3009..3033
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   COILED          3..50
FT                   /evidence="ECO:0000255"
FT   COILED          989..1020
FT                   /evidence="ECO:0000255"
FT   COILED          2073..2102
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3157 AA;  360794 MW;  D2B32B1B280AAF82 CRC64;
     MPSEQFQEQQ RQQQQQYQQQ LERERQEKEQ NEKESLISNL VSLIIEIQQL GGNEYNSQNH
     PINLSKDSIV DDKNNKKDLD TTSVTNNNKQ QQQQNKTTHK IQQKYELYIS RIRSILPELI
     NSHLVSTASI SDINQIVKLI SYLIEKIPNS SLAIGDSSGD ICFFLFKLIP FLSHKSSTNI
     CSQQHQQLDE NEEFTENLIT AIKAMLNFLN DDANVLLLFF KETICLFKDC IDFIKCLNSS
     NNQQEQEKSI FPMVLKTYCE LSSSVIINSN TTGNTSSYSK HYQSLDLLVQ TEMAFNQYSK
     NNNNNNNNNN NSEKDKNIEK EKSNSNDDNS KSIDEGVIIV ISSINRLINL QYGLLVSISS
     VIDNFSPILY SVSIDLWDVL SQYLFLLNDL KLSSFKYMAN FIYSLLVLFE KLLKLSSNQI
     PALLYNNIVG QFFNVLLPMS MLLNDKDCSK RREEIDIKLT SIIPLLFSNV PSSTLFDFSS
     IILPNILFII NNTNLTELKV SILDIYLNIL KLSELQFKSI YNLVPLFGDE GIHDKLYQCF
     DYVINQSYLI DTDDDDDDTD IDISLEILNT LIDYSNCLNI SNIYESISTV TNSVKDKNID
     NNTENIEKDD GDGGAGGTSE NVNNKQIENQ KSITEDSKQQ QQQQQQQPTI EQQKSIRIYL
     KALHLIFKIC KNHHNRVSVK ELVNLFINNL NFIYDLIIQQ KELDNLFLEV LMDLLKLSST
     VEIEYLHRIS TLKSNEQLLE SLFKLSTIVT NHSTIFNLTK YAEIINSIKV ISFSLVCWLP
     CSYYVNERVD IVLSTLSLNK SLVNSTTTTT TTTTTTTTTT TTTATTNTTT TTATTTDKSS
     SQQNVGESNK NNPTIVSSSP ILVNISSDTS SSMGDSQAIS ASQQQQRNNN NNNKGEKYLS
     KLDQNYLINV IKLLPVFISN MSPVNSLATI STNHQYQIMC NDIIKRLESI IDLNVTSLIL
     DMVGVIGGSL YCLKEGYCFF ENLNRCTYLN NNNNNNNNNN NNNNNNNNNN NNIQEQNNLI
     IINNSILLQR FTDTKNNRIK IDPLLSNYNN LVGCGIFEGV WLPLCSCKCV TVSSVLNTNI
     VDLNLKPYRP IHKSPPSNNN NNNNEKDETI MDIDKTNNNE QILILESKYK ENILFSKLFL
     EYHDGQNSDL DNDTSMMTSG GGDGDHDSSI KYFYLGFTFK NILIHNSPLP STSIEGFFKF
     YLNLLSANRN DIIRKSVIKI IISMLKFNYQ TNPDVLTNFF YQLHPLYSNK SEREDILFSI
     LYLLKKIANL IIQSQKDQYI LNNSLNNNNN NNNNNNVQQL SSSSSSHNNQ LNNNNTTTTN
     NDSITWQDKI YSNDFILIIF CTLIENLSRQ TTIKVNSIET IEFIAKKLNQ TPKTLMMTNM
     AQYINPRIIE NLYTNRQSLV ELCRYFLGIG LNQFLISSLP TVIPVLIFKS SNNILNCLKD
     ELKDLKELCG QDYLMGLIFE YIFIHATSVE NLTSCIICFC RFADFNQDAV VSNLPKSFIN
     SLILNLANGD GQQAKKALDY VSQFVGGDMT FDKFLIKEFL GSMNFFTMIM TNKQKSTQEK
     LTMMTSFHRL LGLMGQSVDL FRPKIMAFLR LAIKTPMEEI AIDAWFTFIQ LLKLDSIGPI
     LNQIVFSILP FVQSYPEKSL LIFDYLIIKN RTILKPYFKT IPFLPKEYTV LKPYIQELES
     SSANLTTQIK QLMELFSNES IEVKLMSTNK LKELLSANKS IIHEMIQLDS DPILINDLVK
     SLLIGCRDPY LKLSVNFLTC LGELGAIDPV KLDFSLRNQS TAEKDKVQIA AELIEKYLAK
     FVLSPSNPTP QDRAGYAIQE ILKCCQDTKL SEKLSNECND IIKPYYSSEY MLPLFSKKNN
     NLVGGGGGNG NGGGNGVSSS GSSSCFYGSN MTYKKWITSW LSDLLFKTKG SPGSANNDLD
     SIFMACRGII KDDLKICHYL LPLVILNIIE YGRESDIQSI KNEILEVLNN NTDLSTDNGQ
     ICTQIIFHVI NSLNNWIDVR KRKYFLTQQQ RTASQKGKSK KLESPPDVVV IERFLNGIPE
     KILAFASYRC GALSTSLSYM ESLIRNETSQ ILKQQQQQHQ LNLQLNMQQQ NLQYQQQLQQ
     QQPQQQQQQQ QQQQQQQVQQ QQIPILNSSQ PASMASAREL ALNNNLQLLQ KIYHEMDDID
     GLIGLSHKRV GSPSNEEKIV ELESQGFWGD ALLYYNTALE RSPINMDLRI GALNCLFNLG
     QHESLLLQIE GLKQEPWLTN KDQSKLGTIK IQSSWRLSHW DKIDETLSQT HEPNFEAYLG
     RILYSLVKKQ EKEFNSNLFQ CRSFLAQLLN GSALDSYQRC YPYLIQAHIL EEIEQSYKLI
     HYNVIPIENV TITNNNNNIG NNNNSNNNNV QKQQMLKKLL SEWDDRLKII QPSFKLRESI
     LSVRREILEI GSFSKEVIDC WMKIGKYARH DKKFELSLNA ILKPTPSQQD KFYFIEHAKL
     MWNQGHSFEA INILTQELKN KWNPIINSNN NSSNNSSSNI NINNGSKLSL LGLPQEDLFI
     ISKTHLLIAR WKQQCGITHH SELTEHYSSA TAFEWEKGFF FLGRYYDSLL SNLKRVNQNS
     PNSPPLDSVS YVDYTRNIIS SYGQAVILGH SYIYQTLTRI IALWCELGVI FSDFKIPEKS
     TKVTSDSLES IKKAMSKLEL DVPASNWLMF LSQVASRICH KNTDTWLILE KIIIRTMIEF
     PKQSIWIMMM QYRSSSSIRK QRARTCLEKA RKTDAIKKNQ DETILLCAQL LAVSNHPKKA
     NKRYSIKMSE IFKKLYEMKD LTVILPLQSS LNVSLPPNGK PDKSYPAFGS LPLIGSFEDQ
     IDIMPSLQGP KKINVNDRQG NRYSFLLKPN DDLRKDQRVM EFNTMVNKLI KKDPACRKRN
     LKIRTYTVIP FNEESGIIEW VSNTATLRSI LGGIYETMDT IGIDRFNQMV NAKKEKHYLD
     LFEDFNRFFP PVLHKHFITN FPEPSAWLDA RDAFARSCAI MSMVGSVLGL GDRHTENILL
     DSITGECVHI DYNCLFWKGE TFTVPERVPF RLTRNMVDVF GVLGVEGTFK TVCENTLRVL
     RSNKEVLLRV LENFIYDPFL ILFDKKNQNS NNNNNTHFGE VENDQAVEIL KRISATLQGI
     PTVGLQLSIE GQVNHLIQEA TNPKHLCNMY VGWCSWY
 
 
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