ID FUN30_YEAST Reviewed; 1131 AA. AC P31380; D6VPJ9; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 27-MAR-2024, entry version 193. DE RecName: Full=ATP-dependent helicase FUN30; DE EC=3.6.4.12; GN Name=FUN30; OrderedLocusNames=YAL019W; ORFNames=YAL001; 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]. RC STRAIN=ATCC 204511 / S288c / AB972; RX PubMed=1561836; DOI=10.1002/yea.320080208; RA Clark M.W., Zhong W.-W., Keng T., Storms R.K., Barton A.B., Kaback D.B., RA Bussey H.; RT "Identification of a Saccharomyces cerevisiae homolog of the SNF2 RT transcriptional regulator in the DNA sequence of an 8.6 kb region in the RT LTE1-CYS1 interval on the left arm of chromosome I."; RL Yeast 8:133-145(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX PubMed=8458570; DOI=10.1139/g93-005; RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B., RA Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.; RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 RT kb region between the LTE1 and SPO7 genes."; RL Genome 36:32-42(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX PubMed=8144453; DOI=10.1128/jb.176.7.1872-1880.1994; RA Barton A.B., Kaback D.B.; RT "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae: RT analysis of the genes in the FUN38-MAK16-SPO7 region."; RL J. Bacteriol. 176:1872-1880(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809; RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., RA Storms R.K.; RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995). RN [5] 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 [6] 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 [7] RP IDENTIFICATION BY 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-369, 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 [9] RP FUNCTION. RX PubMed=19956593; DOI=10.1371/journal.pone.0008111; RA Neves-Costa A., Will W.R., Vetter A.T., Miller J.R., Varga-Weisz P.; RT "The SNF2-family member Fun30 promotes gene silencing in heterochromatic RT loci."; RL PLoS ONE 4:E8111-E8111(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, 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 [11] RP FUNCTION, AND SUBUNIT. RX PubMed=20075079; DOI=10.1074/jbc.m109.082149; RA Awad S., Ryan D., Prochasson P., Owen-Hughes T., Hassan A.H.; RT "The Snf2 homolog Fun30 acts as a homodimeric ATP-dependent chromatin- RT remodeling enzyme."; RL J. Biol. Chem. 285:9477-9484(2010). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23007155; DOI=10.1128/mcb.00566-12; RA Eapen V.V., Sugawara N., Tsabar M., Wu W.H., Haber J.E.; RT "The Saccharomyces cerevisiae chromatin remodeler Fun30 regulates DNA end- RT resection and checkpoint deactivation."; RL Mol. Cell. Biol. 32:4727-4740(2012). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=22960743; DOI=10.1038/nature11355; RA Chen X., Cui D., Papusha A., Zhang X., Chu C.D., Tang J., Chen K., Pan X., RA Ira G.; RT "The Fun30 nucleosome remodeller promotes resection of DNA double-strand RT break ends."; RL Nature 489:576-580(2012). RN [14] RP FUNCTION, AND MUTAGENESIS OF LYS-603. RX PubMed=22960744; DOI=10.1038/nature11353; RA Costelloe T., Louge R., Tomimatsu N., Mukherjee B., Martini E., RA Khadaroo B., Dubois K., Wiegant W.W., Thierry A., Burma S., van Attikum H., RA Llorente B.; RT "The yeast Fun30 and human SMARCAD1 chromatin remodellers promote DNA end RT resection."; RL Nature 489:581-584(2012). RN [15] RP FUNCTION. RX PubMed=23028372; DOI=10.1371/journal.pgen.1002974; RA Durand-Dubief M., Will W.R., Petrini E., Theodorou D., Harris R.R., RA Crawford M.R., Paszkiewicz K., Krueger F., Correra R.M., Vetter A.T., RA Miller J.R., Kent N.A., Varga-Weisz P.; RT "SWI/SNF-Like chromatin remodeling factor Fun30 supports point centromere RT function in S. cerevisiae."; RL PLoS Genet. 8:E1002974-E1002974(2012). CC -!- FUNCTION: DNA helicase that possesses intrinsic ATP-dependent CC nucleosome-remodeling activity and is both required for DNA repair and CC heterochromatin organization. Promotes DNA end resection of double- CC strand breaks (DSBs) following DNA damage: probably acts by weakening CC histone DNA interactions in nucleosomes flanking DSBs, facilitating CC single-stranded DNA (ssDNA) production by the EXO1 and SGS1 machinery. CC Promotes gene silencing at heterochromatin by regulating the chromatin CC structure within or around silent loci. Also required for CC heterochromatin organization at centromeres. CC {ECO:0000269|PubMed:19956593, ECO:0000269|PubMed:20075079, CC ECO:0000269|PubMed:22960743, ECO:0000269|PubMed:22960744, CC ECO:0000269|PubMed:23007155, ECO:0000269|PubMed:23028372}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20075079}. CC -!- INTERACTION: CC P31380; P31380: FUN30; NbExp=5; IntAct=EBI-20621, EBI-20621; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Recruited to double- CC strand breaks (DSBs) sites of DNA damage. CC -!- DISRUPTION PHENOTYPE: Impaired ability to repair double-strand breaks CC (DSBs). {ECO:0000269|PubMed:22960743}. CC -!- MISCELLANEOUS: Present with 6800 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}. CC -!- CAUTION: Was initially reported to contain a CUE domain CC (PubMed:19956593). However, no CUE domain is predicted by prediction CC tools and the CUE-like region does not show no affinity for CC ubiquitinated histones (PubMed:20075079). {ECO:0000305|PubMed:19956593, CC ECO:0000305|PubMed:20075079}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L05146; AAC04938.1; -; Genomic_DNA. DR EMBL; BK006935; DAA06969.1; -; Genomic_DNA. DR PIR; S22266; S22266. DR RefSeq; NP_009383.1; NM_001178164.1. DR PDB; 5GN1; X-ray; 1.95 A; A/B/C/D=780-1122. DR PDBsum; 5GN1; -. DR AlphaFoldDB; P31380; -. DR SMR; P31380; -. DR BioGRID; 31747; 221. DR ComplexPortal; CPX-3297; FUN30 complex. DR DIP; DIP-2541N; -. DR IntAct; P31380; 10. DR MINT; P31380; -. DR STRING; 4932.YAL019W; -. DR iPTMnet; P31380; -. DR MaxQB; P31380; -. DR PaxDb; 4932-YAL019W; -. DR PeptideAtlas; P31380; -. DR EnsemblFungi; YAL019W_mRNA; YAL019W; YAL019W. DR GeneID; 851214; -. DR KEGG; sce:YAL019W; -. DR AGR; SGD:S000000017; -. DR SGD; S000000017; FUN30. DR VEuPathDB; FungiDB:YAL019W; -. DR eggNOG; KOG0389; Eukaryota. DR GeneTree; ENSGT00910000144252; -. DR HOGENOM; CLU_000315_16_2_1; -. DR InParanoid; P31380; -. DR OMA; ELQAYND; -. DR OrthoDB; 5482994at2759; -. DR BioCyc; YEAST:G3O-28831-MONOMER; -. DR BRENDA; 3.6.4.12; 984. DR BioGRID-ORCS; 851214; 5 hits in 10 CRISPR screens. DR PRO; PR:P31380; -. DR Proteomes; UP000002311; Chromosome I. DR RNAct; P31380; Protein. DR GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC. DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central. DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:SGD. DR GO; GO:0003682; F:chromatin binding; IDA:SGD. DR GO; GO:0003677; F:DNA binding; IDA:SGD. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal. DR GO; GO:0000729; P:DNA double-strand break processing; IMP:SGD. DR GO; GO:0031507; P:heterochromatin formation; IMP:SGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0033120; P:positive regulation of RNA splicing; IMP:SGD. DR GO; GO:0000183; P:rDNA heterochromatin formation; IMP:SGD. DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IMP:SGD. DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD. DR CDD; cd17998; DEXHc_SMARCAD1; 1. DR CDD; cd18793; SF2_C_SNF; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR038718; SNF2-like_sf. DR InterPro; IPR049730; SNF2/RAD54-like_C. DR InterPro; IPR000330; SNF2_N. DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1. DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00176; SNF2-rel_dom; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Chromatin regulator; Chromosome; DNA damage; KW DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome. FT CHAIN 1..1131 FT /note="ATP-dependent helicase FUN30" FT /id="PRO_0000074384" FT DOMAIN 584..752 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 953..1108 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 1..70 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 76..111 FT /note="CUE-like region" FT REGION 114..141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 242..273 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 327..350 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 400..533 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 703..706 FT /note="DEGH box" FT COMPBIAS 1..51 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 114..128 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 253..269 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 331..349 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 400..416 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 417..431 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 432..446 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 464..481 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 482..533 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 597..604 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 369 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 451 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MUTAGEN 603 FT /note="K->R: Abolishes both the silencing function and the FT ability to promote DNA end resection of double-strand FT breaks (DSBs)." FT /evidence="ECO:0000269|PubMed:22960744" FT STRAND 813..820 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 824..846 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 853..858 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 859..861 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 864..874 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 878..880 FT /evidence="ECO:0007829|PDB:5GN1" FT STRAND 883..885 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 887..897 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 901..904 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 909..917 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 921..930 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 932..935 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 936..938 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 944..946 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 949..962 FT /evidence="ECO:0007829|PDB:5GN1" FT STRAND 969..974 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 976..988 FT /evidence="ECO:0007829|PDB:5GN1" FT STRAND 993..996 FT /evidence="ECO:0007829|PDB:5GN1" FT TURN 1002..1004 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 1005..1014 FT /evidence="ECO:0007829|PDB:5GN1" FT STRAND 1020..1024 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 1025..1029 FT /evidence="ECO:0007829|PDB:5GN1" FT STRAND 1039..1044 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 1049..1056 FT /evidence="ECO:0007829|PDB:5GN1" FT TURN 1057..1059 FT /evidence="ECO:0007829|PDB:5GN1" FT STRAND 1068..1075 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 1079..1086 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 1094..1096 FT /evidence="ECO:0007829|PDB:5GN1" FT HELIX 1109..1122 FT /evidence="ECO:0007829|PDB:5GN1" SQ SEQUENCE 1131 AA; 128507 MW; 7E61B9ABB3A42ED2 CRC64; MSGSHSNDED DVVQVPETSS PTKVASSSPL KPTSPTVPDA SVASLRSRFT FKPSDPSEGA HTSKPLPSGS PEVALVNLAR EFPDFSQTLV QAVFKSNSFN LQSARERLTR LRQQRQNWTW NKNASPKKSE TPPPVKKSLP LANTGRLSSI HGNINNKSSK ITVAKQKTSI FDRYSNVINQ KQYTFELPTN LNIDSEALSK LPVNYNKKRR LVRADQHPIG KSYESSATQL GSAREKLLAN RKYGRHANDN DEEEEESMMT DDDDASGDDY TESTPQINLD EQVLQFINDS DIVDLSDLSD TTMHKAQLIA SHRPYSSLNA FVNTNFNDKD TEENASNKRK RRAAASANES ERLLDKITQS IRGYNAIESV IKKCSSYGDL VTSQMKKWGV QVEGDNSELD LMNLGEDDDD DNDDGNNDNN NSNNNNTAGA DATSKEKEDT KAVVEGFDET SAEPTPAPAP APVERETKRI RNTTKPKVVE DEDDDVDLEA IDDELPQSEH EDDDYEEEDE DYNDEEEDVE YDDGDDDDDD DDEFVATRKN THVISTTSRN GRKPIVKFFK GKPRLLSPEI SLKDYQQTGI NWLNLLYQNK MSCILADDMG LGKTCQVISF FAYLKQINEP GPHLVVVPSS TLENWLREFQ KFAPALKIEP YYGSLQEREE LRDILERNAG KYDVIVTTYN LAAGNKYDVS FLKNRNFNVV VYDEGHMLKN STSERFAKLM KIRANFRLLL TGTPLQNNLK ELMSLLEFIM PNLFISKKES FDAIFKQRAK TTDDNKNHNP LLAQEAITRA KTMMKPFILR RRKDQVLKHL PPKHTHIQYC ELNAIQKKIY DKEIQIVLEH KRMIKDGELP KDAKEKSKLQ SSSSKNLIMA LRKASLHPLL FRNIYNDKII TKMSDAILDE PAYAENGNKE YIKEDMSYMT DFELHKLCCN FPNTLSKYQL HNDEWMQSGK IDALKKLLKT IIVDKQEKVL IFSLFTQVLD ILEMVLSTLD YKFLRLDGST QVNDRQLLID KFYEDKDIPI FILSTKAGGF GINLVCANNV IIFDQSFNPH DDRQAADRAH RVGQTKEVNI TTLITKDSIE EKIHQLAKNK LALDSYISED KKSQDVLESK VSDMLEDIIY DENSKPKGTK E //