RAD53_YEAST
ID RAD53_YEAST Reviewed; 821 AA.
AC P22216; D6W3L5; Q6B1S1;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=Serine/threonine-protein kinase RAD53;
DE EC=2.7.12.1;
DE AltName: Full=CHEK2 homolog;
DE AltName: Full=Serine-protein kinase 1;
GN Name=RAD53; Synonyms=MEC2, SAD1, SPK1; OrderedLocusNames=YPL153C;
GN ORFNames=P2588;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1899289; DOI=10.1128/mcb.11.2.987-1001.1991;
RA Stern D.F., Zheng P., Beidler D.R., Zerillo C.;
RT "Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins
RT on serine, threonine, and tyrosine.";
RL Mol. Cell. Biol. 11:987-1001(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8355715; DOI=10.1128/mcb.13.9.5829-5842.1993;
RA Zheng P., Fay D.S., Burton J., Xiao H., Pinkham J.L., Stern D.F.;
RT "SPK1 is an essential S-phase-specific gene of Saccharomyces cerevisiae
RT that encodes a nuclear serine/threonine/tyrosine kinase.";
RL Mol. Cell. Biol. 13:5829-5842(1993).
RN [7]
RP FUNCTION.
RX PubMed=7958905; DOI=10.1101/gad.8.20.2401;
RA Allen J.B., Zhou Z., Siede W., Friedberg E.C., Elledge S.J.;
RT "The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA
RT damage-induced transcription in yeast.";
RL Genes Dev. 8:2401-2415(1994).
RN [8]
RP PHOSPHORYLATION.
RX PubMed=10562568; DOI=10.1093/emboj/18.22.6561;
RA Pellicioli A., Lucca C., Liberi G., Marini F., Lopes M., Plevani P.,
RA Romano A., Di Fiore P.P., Foiani M.;
RT "Activation of Rad53 kinase in response to DNA damage and its effect in
RT modulating phosphorylation of the lagging strand DNA polymerase.";
RL EMBO J. 18:6561-6572(1999).
RN [9]
RP FUNCTION.
RX PubMed=10550056; DOI=10.1126/science.286.5442.1166;
RA Sanchez Y., Bachant J., Wang H., Hu F., Liu D., Tetzlaff M., Elledge S.J.;
RT "Control of the DNA damage checkpoint by chk1 and rad53 protein kinases
RT through distinct mechanisms.";
RL Science 286:1166-1171(1999).
RN [10]
RP FUNCTION IN PHOSPHORYLATION OF RPH1.
RX PubMed=11809875; DOI=10.1093/nar/30.3.643;
RA Kim E.M., Jang Y.K., Park S.D.;
RT "Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in
RT Saccharomyces cerevisiae, is dependent upon Rad53 kinase.";
RL Nucleic Acids Res. 30:643-648(2002).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH PIN4.
RX PubMed=15024067; DOI=10.1128/mcb.24.7.2779-2788.2004;
RA Pike B.L., Yongkiettrakul S., Tsai M.-D., Heierhorst J.;
RT "Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage
RT tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 24:2779-2788(2004).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-175; SER-547;
RP SER-560; SER-774 AND SER-793, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP STRUCTURE BY NMR OF 573-730.
RX PubMed=10588905; DOI=10.1006/jmbi.1999.3313;
RA Liao H., Byeon I.-J.L., Tsai M.-D.;
RT "Structure and function of a new phosphopeptide-binding domain containing
RT the FHA2 of Rad53.";
RL J. Mol. Biol. 294:1041-1049(1999).
RN [18]
RP STRUCTURE BY NMR OF 2-164.
RX PubMed=11124038; DOI=10.1006/jmbi.2000.4291;
RA Liao H., Yuan C., Su M.I., Yongkiettrakul S., Qin D., Li H., Byeon I.J.,
RA Pei D., Tsai M.D.;
RT "Structure of the FHA1 domain of yeast Rad53 and identification of binding
RT sites for both FHA1 and its target protein Rad9.";
RL J. Mol. Biol. 304:941-951(2000).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 29-155.
RX PubMed=11106755; DOI=10.1016/s1097-2765(00)00114-3;
RA Durocher D., Taylor I.A., Sarbassova D., Haire L.F., Westcott S.L.,
RA Jackson S.P., Smerdon S.J., Yaffe M.B.;
RT "The molecular basis of FHA domain:phosphopeptide binding specificity and
RT implications for phospho-dependent signaling mechanisms.";
RL Mol. Cell 6:1169-1182(2000).
CC -!- FUNCTION: Controls S-phase checkpoint as well as G1 and G2 DNA damage
CC checkpoints. Phosphorylates proteins on serine, threonine, and
CC tyrosine. Prevents entry into anaphase and mitotic exit after DNA
CC damage via regulation of the Polo kinase CDC5. Seems to be involved in
CC the phosphorylation of RPH1. {ECO:0000269|PubMed:10550056,
CC ECO:0000269|PubMed:11809875, ECO:0000269|PubMed:15024067,
CC ECO:0000269|PubMed:7958905, ECO:0000269|PubMed:8355715}.
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=2.7.12.1;
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=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- SUBUNIT: Interacts with PIN4. {ECO:0000269|PubMed:15024067}.
CC -!- INTERACTION:
CC P22216; P32447: ASF1; NbExp=10; IntAct=EBI-17843, EBI-3003;
CC P22216; P34730: BMH2; NbExp=2; IntAct=EBI-17843, EBI-3672;
CC P22216; P32562: CDC5; NbExp=3; IntAct=EBI-17843, EBI-4440;
CC P22216; P40969: CEP3; NbExp=2; IntAct=EBI-17843, EBI-4077;
CC P22216; P39009: DUN1; NbExp=3; IntAct=EBI-17843, EBI-6194;
CC P22216; P34217: PIN4; NbExp=3; IntAct=EBI-17843, EBI-21256;
CC P22216; P40164: PSY2; NbExp=3; IntAct=EBI-17843, EBI-29107;
CC P22216; P14737: RAD9; NbExp=12; IntAct=EBI-17843, EBI-14788;
CC P22216; P35187: SGS1; NbExp=3; IntAct=EBI-17843, EBI-17059;
CC P22216; P53135: SLD3; NbExp=3; IntAct=EBI-17843, EBI-23925;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8355715}.
CC -!- DOMAIN: FHA domains are phosphothreonine recognition modules, FHA 1
CC strongly selects for Asp at position +3 relative to phosphothreonine,
CC whereas FHA 2 selects for Ile in this position.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:10562568}.
CC -!- MISCELLANEOUS: Present with 6900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHEK2 subfamily. {ECO:0000305}.
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DR EMBL; M55623; AAA35070.1; -; Genomic_DNA.
DR EMBL; X96770; CAA65568.1; -; Genomic_DNA.
DR EMBL; Z73509; CAA97858.1; -; Genomic_DNA.
DR EMBL; AY693009; AAT93028.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11281.1; -; Genomic_DNA.
DR PIR; A39616; A39616.
DR RefSeq; NP_015172.1; NM_001183967.1.
DR PDB; 1DMZ; NMR; -; A=573-730.
DR PDB; 1FHQ; NMR; -; A=573-730.
DR PDB; 1FHR; NMR; -; A=573-730.
DR PDB; 1G3G; NMR; -; A=1-164.
DR PDB; 1G6G; X-ray; 1.60 A; A/B=29-155.
DR PDB; 1J4K; NMR; -; A=573-730.
DR PDB; 1J4L; NMR; -; A=573-730.
DR PDB; 1J4O; NMR; -; A=14-164.
DR PDB; 1J4P; NMR; -; A=14-164.
DR PDB; 1J4Q; NMR; -; A=14-164.
DR PDB; 1K2M; NMR; -; A=573-730.
DR PDB; 1K2N; NMR; -; A=573-730.
DR PDB; 1K3J; NMR; -; A=14-164.
DR PDB; 1K3N; NMR; -; A=14-164.
DR PDB; 1K3Q; NMR; -; A=14-164.
DR PDB; 1QU5; NMR; -; A=549-730.
DR PDB; 2A0T; NMR; -; A=14-164.
DR PDB; 2JQI; NMR; -; A=14-164, B=3-12.
DR PDB; 2JQL; NMR; -; B=3-12.
DR PDB; 2YGV; X-ray; 2.94 A; E/F/G/H=800-821.
DR PDB; 4PDP; X-ray; 2.59 A; A/B=170-512.
DR PDB; 4PDS; X-ray; 2.90 A; A/B=170-512.
DR PDB; 5T2F; X-ray; 2.66 A; A/B/C/D=22-162.
DR PDB; 5T2S; X-ray; 2.40 A; A/C=22-162.
DR PDB; 5XZV; X-ray; 3.10 A; A/B=1-466.
DR PDB; 5XZW; X-ray; 2.80 A; A/B=1-466.
DR PDB; 6C4U; X-ray; 2.60 A; A/B/C/D/E/F=29-162.
DR PDBsum; 1DMZ; -.
DR PDBsum; 1FHQ; -.
DR PDBsum; 1FHR; -.
DR PDBsum; 1G3G; -.
DR PDBsum; 1G6G; -.
DR PDBsum; 1J4K; -.
DR PDBsum; 1J4L; -.
DR PDBsum; 1J4O; -.
DR PDBsum; 1J4P; -.
DR PDBsum; 1J4Q; -.
DR PDBsum; 1K2M; -.
DR PDBsum; 1K2N; -.
DR PDBsum; 1K3J; -.
DR PDBsum; 1K3N; -.
DR PDBsum; 1K3Q; -.
DR PDBsum; 1QU5; -.
DR PDBsum; 2A0T; -.
DR PDBsum; 2JQI; -.
DR PDBsum; 2JQL; -.
DR PDBsum; 2YGV; -.
DR PDBsum; 4PDP; -.
DR PDBsum; 4PDS; -.
DR PDBsum; 5T2F; -.
DR PDBsum; 5T2S; -.
DR PDBsum; 5XZV; -.
DR PDBsum; 5XZW; -.
DR PDBsum; 6C4U; -.
DR AlphaFoldDB; P22216; -.
DR SMR; P22216; -.
DR BioGRID; 36030; 621.
DR ComplexPortal; CPX-1322; RAD53-ASF1 complex.
DR DIP; DIP-2322N; -.
DR IntAct; P22216; 40.
DR MINT; P22216; -.
DR STRING; 4932.YPL153C; -.
DR iPTMnet; P22216; -.
DR MaxQB; P22216; -.
DR PaxDb; P22216; -.
DR PRIDE; P22216; -.
DR EnsemblFungi; YPL153C_mRNA; YPL153C; YPL153C.
DR GeneID; 855950; -.
DR KEGG; sce:YPL153C; -.
DR SGD; S000006074; RAD53.
DR VEuPathDB; FungiDB:YPL153C; -.
DR eggNOG; KOG0615; Eukaryota.
DR HOGENOM; CLU_379543_0_0_1; -.
DR InParanoid; P22216; -.
DR OMA; CRLICTT; -.
DR BioCyc; YEAST:G3O-34050-MON; -.
DR BRENDA; 2.7.12.1; 984.
DR EvolutionaryTrace; P22216; -.
DR PRO; PR:P22216; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P22216; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:SGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009202; P:deoxyribonucleoside triphosphate biosynthetic process; IMP:SGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IGI:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IC:ComplexPortal.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IMP:SGD.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IMP:SGD.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR CDD; cd00060; FHA; 2.
DR DisProt; DP01182; -.
DR IDEAL; IID50168; -.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016256; Ser/Thr_kinase_Rad53.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000661; Ser/Thr_PK_RAD53; 1.
DR SMART; SM00240; FHA; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49879; SSF49879; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; DNA damage; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..821
FT /note="Serine/threonine-protein kinase RAD53"
FT /id="PRO_0000086595"
FT DOMAIN 66..116
FT /note="FHA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 198..466
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 601..664
FT /note="FHA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 735..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT BINDING 204..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 204
FT /note="V -> A (in Ref. 5; AAT93028)"
FT /evidence="ECO:0000305"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:5XZW"
FT STRAND 31..43
FT /evidence="ECO:0007829|PDB:1G6G"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1G6G"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:1G6G"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1G3G"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1G6G"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1G6G"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5XZV"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1G6G"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5T2F"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1G6G"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:5XZW"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5XZV"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1G6G"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1G6G"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1G6G"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:1G6G"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5XZW"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:4PDP"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:4PDP"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:4PDP"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4PDP"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:5XZW"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:4PDP"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:4PDP"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 293..312
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4PDP"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:4PDP"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:4PDP"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:4PDP"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 387..403
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 413..421
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 437..446
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 457..461
FT /evidence="ECO:0007829|PDB:4PDP"
FT TURN 464..467
FT /evidence="ECO:0007829|PDB:4PDP"
FT HELIX 484..493
FT /evidence="ECO:0007829|PDB:4PDP"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:1QU5"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:1QU5"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:1QU5"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:1QU5"
FT STRAND 592..597
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 601..606
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 620..629
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 636..638
FT /evidence="ECO:0007829|PDB:1FHQ"
FT STRAND 645..651
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 653..655
FT /evidence="ECO:0007829|PDB:1QU5"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:1FHQ"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:1FHQ"
FT STRAND 666..671
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 678..680
FT /evidence="ECO:0007829|PDB:1DMZ"
FT TURN 684..687
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:1QU5"
FT STRAND 692..695
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 703..707
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 710..712
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:1DMZ"
FT HELIX 721..728
FT /evidence="ECO:0007829|PDB:1DMZ"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:2YGV"
FT HELIX 811..813
FT /evidence="ECO:0007829|PDB:2YGV"
SQ SEQUENCE 821 AA; 91962 MW; 84A9612229CA72D1 CRC64;
MENITQPTQQ STQATQRFLI EKFSQEQIGE NIVCRVICTT GQIPIRDLSA DISQVLKEKR
SIKKVWTFGR NPACDYHLGN ISRLSNKHFQ ILLGEDGNLL LNDISTNGTW LNGQKVEKNS
NQLLSQGDEI TVGVGVESDI LSLVIFINDK FKQCLEQNKV DRIRSNLKNT SKIASPGLTS
STASSMVANK TGIFKDFSII DEVVGQGAFA TVKKAIERTT GKTFAVKIIS KRKVIGNMDG
VTRELEVLQK LNHPRIVRLK GFYEDTESYY MVMEFVSGGD LMDFVAAHGA VGEDAGREIS
RQILTAIKYI HSMGISHRDL KPDNILIEQD DPVLVKITDF GLAKVQGNGS FMKTFCGTLA
YVAPEVIRGK DTSVSPDEYE ERNEYSSLVD MWSMGCLVYV ILTGHLPFSG STQDQLYKQI
GRGSYHEGPL KDFRISEEAR DFIDSLLQVD PNNRSTAAKA LNHPWIKMSP LGSQSYGDFS
QISLSQSLSQ QKLLENMDDA QYEFVKAQRK LQMEQQLQEQ DQEDQDGKIQ GFKIPAHAPI
RYTQPKSIEA ETREQKLLHS NNTENVKSSK KKGNGRFLTL KPLPDSIIQE SLEIQQGVNP
FFIGRSEDCN CKIEDNRLSR VHCFIFKKRH AVGKSMYESP AQGLDDIWYC HTGTNVSYLN
NNRMIQGTKF LLQDGDEIKI IWDKNNKFVI GFKVEINDTT GLFNEGLGML QEQRVVLKQT
AEEKDLVKKL TQMMAAQRAN QPSASSSSMS AKKPPVSDTN NNGNNSVLND LVESPINANT
GNILKRIHSV SLSQSQIDPS KKVKRAKLDQ TSKGPENLQF S
