KRE29_YEAST
ID KRE29_YEAST Reviewed; 464 AA.
AC P40026; D3DLT7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=DNA repair protein KRE29;
DE AltName: Full=Killer toxin-resistance protein 29;
GN Name=KRE29; OrderedLocusNames=YER038C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH NSE5.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP SUBUNIT.
RX PubMed=15738391; DOI=10.1073/pnas.0500537102;
RA Zhao X., Blobel G.;
RT "A SUMO ligase is part of a nuclear multiprotein complex that affects DNA
RT repair and chromosomal organization.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4777-4782(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-101, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, 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).
CC -!- FUNCTION: Acts in a DNA repair pathway for removal of UV-induced DNA
CC damage that is distinct from classical nucleotide excision repair and
CC in repair of ionizing radiation damage. Functions in homologous
CC recombination repair of DNA double strand breaks and in recovery of
CC stalled replication forks.
CC -!- SUBUNIT: Component of the Smc5-Smc6 complex which consists of KRE29,
CC MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6. Interacts with NSE5.
CC {ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:15738391}.
CC -!- INTERACTION:
CC P40026; Q03718: NSE5; NbExp=3; IntAct=EBI-22506, EBI-27756;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
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DR EMBL; U18796; AAB64573.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07691.1; -; Genomic_DNA.
DR PIR; S50541; S50541.
DR RefSeq; NP_010955.3; NM_001178929.3.
DR PDB; 6J0W; X-ray; 2.40 A; C/D=13-41.
DR PDB; 7LTO; EM; 3.20 A; B=1-464.
DR PDB; 7OGG; X-ray; 3.29 A; Q=177-464.
DR PDB; 7SDE; EM; 3.20 A; B=1-464.
DR PDBsum; 6J0W; -.
DR PDBsum; 7LTO; -.
DR PDBsum; 7OGG; -.
DR PDBsum; 7SDE; -.
DR AlphaFoldDB; P40026; -.
DR SMR; P40026; -.
DR BioGRID; 36773; 164.
DR ComplexPortal; CPX-1364; SMC5-SMC6 SUMO ligase complex.
DR DIP; DIP-5183N; -.
DR IntAct; P40026; 4.
DR STRING; 4932.YER038C; -.
DR iPTMnet; P40026; -.
DR MaxQB; P40026; -.
DR PaxDb; P40026; -.
DR PRIDE; P40026; -.
DR EnsemblFungi; YER038C_mRNA; YER038C; YER038C.
DR GeneID; 856760; -.
DR KEGG; sce:YER038C; -.
DR SGD; S000000840; KRE29.
DR VEuPathDB; FungiDB:YER038C; -.
DR eggNOG; KOG4599; Eukaryota.
DR HOGENOM; CLU_051886_0_0_1; -.
DR InParanoid; P40026; -.
DR OMA; TEYFKDC; -.
DR BioCyc; YEAST:G3O-30219-MON; -.
DR PRO; PR:P40026; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40026; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR InterPro; IPR014803; DNA_repair_Nse5/Nse6.
DR Pfam; PF08691; Nse5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..464
FT /note="DNA repair protein KRE29"
FT /id="PRO_0000084329"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6J0W"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6J0W"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:6J0W"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:7LTO"
FT TURN 267..272
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 301..316
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 330..335
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 355..365
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:7OGG"
FT HELIX 371..377
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:7OGG"
FT HELIX 389..396
FT /evidence="ECO:0007829|PDB:7LTO"
FT TURN 397..403
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 405..415
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 433..440
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:7OGG"
FT HELIX 449..461
FT /evidence="ECO:0007829|PDB:7LTO"
SQ SEQUENCE 464 AA; 53772 MW; 0E35F6857ECA5BBD CRC64;
MGSVNSSPNE EFETVPDSQI SGFDSPLIPT SVGSYFRDDD DDEKVHPNFI SDPENDSLNS
DEEFSSLENS DLNLSGAKAE SGDDFDPILK RTIISKRKAP SNNEDEEIVK TPRKLVNYVP
LKIFNLGDSF DDTITTTVAK LQDLKKEILD SPRSNKSIVI TSNTVAKSEL QKSIKFSGSI
PEIYLDVVTK ETISDKYKDW HFISKNCHYE QLMDLEMKDT AYSFLFGSSR SQGKVPEFVH
LKCPSITNLL VLFGVNQEKC NSLKINYEKK ENSRYDNLCT IFPVNKMLKF LMYFYSDDDN
DDVREFFLKA FICLILDRKV FNAMESDHRL CFKVLELFNE AHFINSYFEI VDKNDFFLHY
RLLQIFPHLQ SALLRRRFSE KQGRTETIQQ NIIKEFNEFF DCKNYKNLLY FILTMYGSKF
IPFGPKCQVT EYFKDCILDI SNETTNDVEI SILKGILNLF SKIR
