ID   RAD2_YEAST              Reviewed;        1031 AA.
AC   P07276; D6VV38; E9P8X9;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   27-MAR-2024, entry version 214.
DE   RecName: Full=DNA repair protein RAD2;
DE            EC=3.1.-.-;
GN   Name=RAD2; OrderedLocusNames=YGR258C;
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=3000874; DOI=10.1016/0378-1119(85)90177-5;
RA   Nicolet C.M., Chenevert J.M., Friedberg E.C.;
RT   "The RAD2 gene of Saccharomyces cerevisiae: nucleotide sequence and
RT   transcript mapping.";
RL   Gene 36:225-234(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX   PubMed=3011752; DOI=10.1128/jb.166.3.914-923.1986;
RA   Madura K., Prakash S.;
RT   "Nucleotide sequence, transcript mapping, and regulation of the RAD2 gene
RT   of Saccharomyces cerevisiae.";
RL   J. Bacteriol. 166:914-923(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9090059;
RX   DOI=10.1002/(sici)1097-0061(19970315)13:3<287::aid-yea75>3.0.co;2-5;
RA   Clemente M.L., Sartori G., Cardazzo B., Carignani G.;
RT   "Analysis of an 11.6 kb region from the right arm of chromosome VII of
RT   Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals the
RT   presence of three new genes.";
RL   Yeast 13:287-290(1997).
RN   [7]
RP   FUNCTION.
RX   PubMed=8247134; DOI=10.1038/366365a0;
RA   Habraken Y., Sung P., Prakash L., Prakash S.;
RT   "Yeast excision repair gene RAD2 encodes a single-stranded DNA
RT   endonuclease.";
RL   Nature 366:365-368(1993).
RN   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-367, AND
RP   IDENTIFICATION BY 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).
CC   -!- FUNCTION: Single-stranded DNA endonuclease involved in excision repair
CC       of DNA damaged with UV light, bulky adducts, or cross-linking agents.
CC       Essential for the incision step of excision-repair.
CC       {ECO:0000269|PubMed:8247134}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate in
CC       the reaction catalyzed by the enzyme. May bind an additional third
CC       magnesium ion after substrate binding. {ECO:0000250};
CC   -!- INTERACTION:
CC       P07276; P19882: HSP60; NbExp=2; IntAct=EBI-14757, EBI-8586;
CC       P07276; Q00416: SEN1; NbExp=3; IntAct=EBI-14757, EBI-16945;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M10275; AAA66928.1; -; Genomic_DNA.
DR   EMBL; Y07777; CAA69080.1; -; Genomic_DNA.
DR   EMBL; Z73043; CAA97287.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08349.1; -; Genomic_DNA.
DR   EMBL; AY692857; AAT92876.1; -; Genomic_DNA.
DR   PIR; A29839; A29839.
DR   RefSeq; NP_011774.1; NM_001181387.1.
DR   PDB; 2LOX; NMR; -; B=642-690.
DR   PDB; 4Q0R; X-ray; 2.75 A; A/B=1-111, A/B=732-986.
DR   PDB; 4Q0W; X-ray; 2.10 A; A/B=2-111, A/B=732-986.
DR   PDB; 4Q0Z; X-ray; 2.40 A; A/B/E/F=2-111, A/B/E/F=732-986.
DR   PDB; 4Q10; X-ray; 2.70 A; A/B=2-111, A/B=732-986.
DR   PDBsum; 2LOX; -.
DR   PDBsum; 4Q0R; -.
DR   PDBsum; 4Q0W; -.
DR   PDBsum; 4Q0Z; -.
DR   PDBsum; 4Q10; -.
DR   AlphaFoldDB; P07276; -.
DR   SMR; P07276; -.
DR   BioGRID; 33510; 75.
DR   DIP; DIP-5869N; -.
DR   ELM; P07276; -.
DR   IntAct; P07276; 7.
DR   STRING; 4932.YGR258C; -.
DR   iPTMnet; P07276; -.
DR   MaxQB; P07276; -.
DR   PaxDb; 4932-YGR258C; -.
DR   PeptideAtlas; P07276; -.
DR   EnsemblFungi; YGR258C_mRNA; YGR258C; YGR258C.
DR   GeneID; 853174; -.
DR   KEGG; sce:YGR258C; -.
DR   AGR; SGD:S000003490; -.
DR   SGD; S000003490; RAD2.
DR   VEuPathDB; FungiDB:YGR258C; -.
DR   eggNOG; KOG2520; Eukaryota.
DR   GeneTree; ENSGT00940000163631; -.
DR   HOGENOM; CLU_003018_2_0_1; -.
DR   InParanoid; P07276; -.
DR   OMA; PNSMDFS; -.
DR   OrthoDB; 5479162at2759; -.
DR   BioCyc; YEAST:G3O-30928-MONOMER; -.
DR   BioGRID-ORCS; 853174; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P07276; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P07276; Protein.
DR   GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004520; F:DNA endonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:SGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; IDA:SGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IGI:SGD.
DR   CDD; cd09904; H3TH_XPG; 1.
DR   CDD; cd09868; PIN_XPG_RAD2; 2.
DR   DisProt; DP01631; -.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR   IDEAL; IID50166; -.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   NCBIfam; TIGR00600; rad2; 1.
DR   PANTHER; PTHR16171:SF7; DNA EXCISION REPAIR PROTEIN ERCC-5; 1.
DR   PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   PRINTS; PR00066; XRODRMPGMNTG.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1031
FT                   /note="DNA repair protein RAD2"
FT                   /id="PRO_0000154035"
FT   REGION          1..95
FT                   /note="N-domain"
FT   REGION          342..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..884
FT                   /note="I-domain"
FT   COMPBIAS        459..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         792
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         794
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         813
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         815
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         864
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         583
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        782
FT                   /note="F -> L (in Ref. 5; AAT92876)"
FT                   /evidence="ECO:0000305"
FT   STRAND          667..669
FT                   /evidence="ECO:0007829|PDB:2LOX"
FT   HELIX           769..781
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   STRAND          786..788
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           793..802
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   STRAND          807..810
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           815..818
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   STRAND          823..827
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   STRAND          830..839
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           840..847
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           851..861
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           874..884
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           887..899
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           901..904
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           909..920
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           932..939
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           957..968
FT                   /evidence="ECO:0007829|PDB:4Q0W"
FT   HELIX           972..982
FT                   /evidence="ECO:0007829|PDB:4Q0W"
SQ   SEQUENCE   1031 AA;  117838 MW;  682D4AECFBD7F0F3 CRC64;
     MGVHSFWDIA GPTARPVRLE SLEDKRMAVD ASIWIYQFLK AVRDQEGNAV KNSHITGFFR
     RICKLLYFGI RPVFVFDGGV PVLKRETIRQ RKERRQGKRE SAKSTARKLL ALQLQNGSND
     NVKNSTPSSG SSVQIFKPQD EWDLPDIPGF KYDKEDARVN SNKTFEKLMN SINGDGLEDI
     DLDTINPASA EFEELPKATQ YLILSSLRLK SRLRMGYSKE QLETIFPNSM DFSRFQIDMV
     KRRNFFTQKL INTTGFQDGG ASKLNEEVIN RISGQKSKEY KLTKTNNGWI LGLGANDGSD
     AQKAIVIDDK DAGALVKQLD SNAEDGDVLR WDDLEDNSLK IVRHESSNAT TAPQKRSNRS
     EDEGCDSDEC EWEEVELKPK NVKFVEDFSL KAARLPYMGQ SLNNAGSKSF LDKRHDQASP
     SKTTPTMRIS RISVEDDDED YLKQIEEIEM MEAVQLSKME KKPEADDKSK IAKPVTSKGT
     EARPPIVQYG LLGAQPDSKQ PYHVTNLNSK SESVIKRTSK TVLSEFRPPS QQEDKGAILT
     EGEQNLNFIS HKIPQFDFNN ENSLLFQKNT ESNVSQEATK EKSPIPEMPS WFSSTASQQL
     YNPYNTTNFV EDKNVRNEQE SGAETTNKGS SYELLTGLNA TEILERESEK ESSNDENKDD
     DLEVLSEELF EDVPTKSQIS KEAEDNDSRK VESINKEHRK PLIFDYDFSE DEEDNIVENM
     IKEQEEFDTF KNTTLSTSAE RNVAENAFVE DELFEQQMKD KRDSDEVTMD MIKEVQELLS
     RFGIPYITAP MEAEAQCAEL LQLNLVDGII TDDSDVFLFG GTKIYKNMFH EKNYVEFYDA
     ESILKLLGLD RKNMIELAQL LGSDYTNGLK GMGPVSSIEV IAEFGNLKNF KDWYNNGQFD
     KRKQETENKF EKDLRKKLVN NEIILDDDFP SVMVYDAYMR PEVDHDTTPF VWGVPDLDML
     RSFMKTQLGW PHEKSDEILI PLIRDVNKRK KKGKQKRINE FFPREYISGD KKLNTSKRIS
     TATGKLKKRK M
//