FUN30_YEAST
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 03-AUG-2022, entry version 186.
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}.
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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; 209.
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; P31380; -.
DR PRIDE; P31380; -.
DR EnsemblFungi; YAL019W_mRNA; YAL019W; YAL019W.
DR GeneID; 851214; -.
DR KEGG; sce:YAL019W; -.
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; GTIQDKW; -.
DR BioCyc; YEAST:G3O-28831-MON; -.
DR BRENDA; 3.6.4.12; 984.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006338; P:chromatin remodeling; IMP:SGD.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:SGD.
DR GO; GO:0031507; P:heterochromatin assembly; 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 assembly; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR000330; SNF2_N.
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; SSF52540; 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
