ID   STH1_YEAST              Reviewed;        1359 AA.
AC   P32597; D6VVG1; Q45U09;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 228.
DE   RecName: Full=Nuclear protein STH1/NPS1;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase STH1;
DE   AltName: Full=Chromatin structure-remodeling complex protein STH1;
DE   AltName: Full=SNF2 homolog;
GN   Name=STH1; Synonyms=NPS1; OrderedLocusNames=YIL126W;
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=1396591; DOI=10.1002/j.1460-2075.1992.tb05495.x;
RA   Tsuchiya E., Uno M., Kiguchi A., Masuoka K., Kanemori Y., Okabe S.,
RA   Miyakawa T.;
RT   "The Saccharomyces cerevisiae NPS1 gene, a novel CDC gene which encodes a
RT   160 kDa nuclear protein involved in G2 phase control.";
RL   EMBO J. 11:4017-4026(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1549132; DOI=10.1128/mcb.12.4.1893-1902.1992;
RA   Laurent B.C., Yang X., Carlson M.;
RT   "An essential Saccharomyces cerevisiae gene homologous to SNF2 encodes a
RT   helicase-related protein in a new family.";
RL   Mol. Cell. Biol. 12:1893-1902(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SK1;
RX   PubMed=16273108; DOI=10.1038/ng1674;
RA   Deutschbauer A.M., Davis R.W.;
RT   "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL   Nat. Genet. 37:1333-1340(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
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   PROTEIN SEQUENCE OF 961-987 AND 993-1002, IDENTIFICATION IN THE RSC
RP   COMPLEX, AND FUNCTION OF THE RSC COMPLEX.
RX   PubMed=8980231; DOI=10.1016/s0092-8674(00)81820-6;
RA   Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L., Erdjument-Bromage H.,
RA   Tempst P., Du J., Laurent B.C., Kornberg R.D.;
RT   "RSC, an essential, abundant chromatin-remodeling complex.";
RL   Cell 87:1249-1260(1996).
RN   [7]
RP   INTERACTION WITH RSC8.
RX   PubMed=9121424; DOI=10.1128/mcb.17.4.1768;
RA   Treich I., Carlson M.;
RT   "Interaction of a Swi3 homolog with Sth1 provides evidence for a Swi/Snf-
RT   related complex with an essential function in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 17:1768-1775(1997).
RN   [8]
RP   INTERACTION WITH SFH1.
RX   PubMed=9154831; DOI=10.1128/mcb.17.6.3323;
RA   Cao Y., Cairns B.R., Kornberg R.D., Laurent B.C.;
RT   "Sfh1p, a component of a novel chromatin-remodeling complex, is required
RT   for cell cycle progression.";
RL   Mol. Cell. Biol. 17:3323-3334(1997).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF SER-505; PRO-646; SER-806 AND THR-881.
RX   PubMed=9799253; DOI=10.1093/genetics/150.3.987;
RA   Du J., Nasir I., Benton B.K., Kladde M.P., Laurent B.C.;
RT   "Sth1p, a Saccharomyces cerevisiae Snf2p/Swi2p homolog, is an essential
RT   ATPase in RSC and differs from Snf/Swi in its interactions with histones
RT   and chromatin-associated proteins.";
RL   Genetics 150:987-1005(1998).
RN   [10]
RP   FUNCTION OF THE RSC COMPLEX.
RX   PubMed=10025404; DOI=10.1016/s0092-8674(00)80551-6;
RA   Lorch Y., Zhang M., Kornberg R.D.;
RT   "Histone octamer transfer by a chromatin-remodeling complex.";
RL   Cell 96:389-392(1999).
RN   [11]
RP   FUNCTION.
RX   PubMed=10329629; DOI=10.1093/emboj/18.10.2836;
RA   Moreira J.M.A., Holmberg S.;
RT   "Transcriptional repression of the yeast CHA1 gene requires the chromatin-
RT   remodeling complex RSC.";
RL   EMBO J. 18:2836-2844(1999).
RN   [12]
RP   FUNCTION, AND MUTAGENESIS OF CYS-763.
RX   PubMed=10320476; DOI=10.1046/j.1365-2443.1999.00242.x;
RA   Yukawa M., Katoh S., Miyakawa T., Tsuchiya E.;
RT   "Nps1/Sth1p, a component of an essential chromatin-remodeling complex of
RT   Saccharomyces cerevisiae, is required for the maximal expression of early
RT   meiotic genes.";
RL   Genes Cells 4:99-110(1999).
RN   [13]
RP   COMPOSITION OF THE RSC COMPLEX.
RX   PubMed=10619019; DOI=10.1016/s1097-2765(00)80382-2;
RA   Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D.,
RA   Winston F.;
RT   "Two functionally distinct forms of the RSC nucleosome-remodeling complex,
RT   containing essential AT hook, BAH, and bromodomains.";
RL   Mol. Cell 4:715-723(1999).
RN   [14]
RP   FUNCTION.
RX   PubMed=12183366; DOI=10.1101/gad.995002;
RA   Saha A., Wittmeyer J., Cairns B.R.;
RT   "Chromatin remodeling by RSC involves ATP-dependent DNA translocation.";
RL   Genes Dev. 16:2120-2134(2002).
RN   [15]
RP   FUNCTION OF THE RSC COMPLEX.
RX   PubMed=12072455; DOI=10.1093/genetics/161.2.575;
RA   Chai B., Hsu J.-M., Du J., Laurent B.C.;
RT   "Yeast RSC function is required for organization of the cellular
RT   cytoskeleton via an alternative PKC1 pathway.";
RL   Genetics 161:575-584(2002).
RN   [16]
RP   FUNCTION OF THE RSC COMPLEX, INTERACTION WITH CSE4 AND HISTONES H3; H4 AND
RP   H2B, AND SUBCELLULAR LOCATION.
RX   PubMed=12697820; DOI=10.1128/mcb.23.9.3202-3215.2003;
RA   Hsu J.-M., Huang J., Meluh P.B., Laurent B.C.;
RT   "The yeast RSC chromatin-remodeling complex is required for kinetochore
RT   function in chromosome segregation.";
RL   Mol. Cell. Biol. 23:3202-3215(2003).
RN   [17]
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   [18]
RP   INTERACTION WITH RTT102.
RX   PubMed=15506919; DOI=10.1042/bst0320899;
RA   Lee K.K., Prochasson P., Florens L., Swanson S.K., Washburn M.P.,
RA   Workman J.L.;
RT   "Proteomic analysis of chromatin-modifying complexes in Saccharomyces
RT   cerevisiae identifies novel subunits.";
RL   Biochem. Soc. Trans. 32:899-903(2004).
RN   [19]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [20]
RP   INTERACTION WITH LDB7 AND NPL6.
RX   PubMed=16204215; DOI=10.1534/genetics.105.047589;
RA   Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R.;
RT   "The RSC chromatin remodeling complex bears an essential fungal-specific
RT   protein module with broad functional roles.";
RL   Genetics 172:795-809(2006).
RN   [21]
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   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, 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   [23]
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: Catalytic component of the chromatin structure-remodeling
CC       complex (RSC), which is involved in transcription regulation and
CC       nucleosome positioning. RSC is responsible for the transfer of a
CC       histone octamer from a nucleosome core particle to naked DNA. The
CC       reaction requires ATP and involves an activated RSC-nucleosome
CC       intermediate. Remodeling reaction also involves DNA translocation, DNA
CC       twist and conformational change. As a reconfigurer of centromeric and
CC       flanking nucleosomes, RSC complex is required both for proper
CC       kinetochore function in chromosome segregation and, via a PKC1-
CC       dependent signaling pathway, for organization of the cellular
CC       cytoskeleton. This subunit is the essential ATPase of the complex. It
CC       is a DNA translocase capable of nucleosome remodeling. Required for
CC       full expression of early meiotic genes. Essential for mitotic growth
CC       and repression of CHA1 expression. Also involved in G2 phase control.
CC       {ECO:0000269|PubMed:10025404, ECO:0000269|PubMed:10320476,
CC       ECO:0000269|PubMed:10329629, ECO:0000269|PubMed:12072455,
CC       ECO:0000269|PubMed:12183366, ECO:0000269|PubMed:12697820,
CC       ECO:0000269|PubMed:8980231, ECO:0000269|PubMed:9799253}.
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: Interacts directly with SFH1, CSE4, histones H3, H4 and H2B,
CC       and via its N-terminus, with RSC8. Interacts with LDB7, NPL6 and
CC       RTT102. Component of the two forms of the RSC complex composed of at
CC       least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30,
CC       RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102.
CC       The complexes interact with histone and histone variant components of
CC       centromeric chromatin. {ECO:0000269|PubMed:12697820,
CC       ECO:0000269|PubMed:15506919, ECO:0000269|PubMed:16204215,
CC       ECO:0000269|PubMed:8980231, ECO:0000269|PubMed:9121424,
CC       ECO:0000269|PubMed:9154831}.
CC   -!- INTERACTION:
CC       P32597; P02309: HHF2; NbExp=4; IntAct=EBI-18410, EBI-8113;
CC       P32597; P61830: HHT2; NbExp=4; IntAct=EBI-18410, EBI-8098;
CC       P32597; P02293: HTB1; NbExp=3; IntAct=EBI-18410, EBI-8088;
CC       P32597; Q9URQ5: HTL1; NbExp=3; IntAct=EBI-18410, EBI-8717;
CC       P32597; P38210: LDB7; NbExp=2; IntAct=EBI-18410, EBI-21189;
CC       P32597; P11632: NHP6A; NbExp=3; IntAct=EBI-18410, EBI-12019;
CC       P32597; P38181: NUP170; NbExp=3; IntAct=EBI-18410, EBI-11756;
CC       P32597; Q07979: RSC58; NbExp=6; IntAct=EBI-18410, EBI-36549;
CC       P32597; P53330: RTT102; NbExp=5; IntAct=EBI-18410, EBI-23637;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549,
CC       ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and
CC       flanking chromatin. Association of the RSC complex with these loci is
CC       dependent on this subunit.
CC   -!- MISCELLANEOUS: Present with 1990 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; D10595; BAA01446.1; -; Genomic_DNA.
DR   EMBL; M83755; AAA35120.1; -; Genomic_DNA.
DR   EMBL; DQ115392; AAZ22501.1; -; Genomic_DNA.
DR   EMBL; Z46833; CAA86866.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08427.1; -; Genomic_DNA.
DR   PIR; S49883; S49883.
DR   RefSeq; NP_012140.1; NM_001179474.1.
DR   PDB; 6K15; EM; 3.40 A; J=1-1359.
DR   PDB; 6KMB; X-ray; 2.40 A; A/B/C/D=1248-1359.
DR   PDB; 6KMJ; X-ray; 1.40 A; A=1248-1359.
DR   PDB; 6KW3; EM; 7.13 A; J/W/Y=1-1359.
DR   PDB; 6KW4; EM; 7.55 A; J/V/Y=1-1359.
DR   PDB; 6KW5; EM; 10.13 A; J/P/Q=1-1359.
DR   PDB; 6LQZ; NMR; -; B=1183-1240.
DR   PDB; 6MR4; X-ray; 2.71 A; A/B/C/D/E/F=1250-1359.
DR   PDB; 6TDA; EM; 15.00 A; S=1-1359.
DR   PDB; 6UY1; X-ray; 2.21 A; A/B/C/D/E/F/G/H=1250-1359.
DR   PDB; 6V8O; EM; 3.07 A; R=1-1359.
DR   PDB; 6V92; EM; 20.00 A; R=1-1359.
DR   PDB; 6VZ4; EM; 3.90 A; K=301-1097.
DR   PDB; 6VZG; EM; 4.20 A; K=301-1097.
DR   PDB; 7F3S; X-ray; 1.40 A; A=1248-1359.
DR   PDBsum; 6K15; -.
DR   PDBsum; 6KMB; -.
DR   PDBsum; 6KMJ; -.
DR   PDBsum; 6KW3; -.
DR   PDBsum; 6KW4; -.
DR   PDBsum; 6KW5; -.
DR   PDBsum; 6LQZ; -.
DR   PDBsum; 6MR4; -.
DR   PDBsum; 6TDA; -.
DR   PDBsum; 6UY1; -.
DR   PDBsum; 6V8O; -.
DR   PDBsum; 6V92; -.
DR   PDBsum; 6VZ4; -.
DR   PDBsum; 6VZG; -.
DR   PDBsum; 7F3S; -.
DR   AlphaFoldDB; P32597; -.
DR   EMDB; EMD-0777; -.
DR   EMDB; EMD-0778; -.
DR   EMDB; EMD-0779; -.
DR   EMDB; EMD-10465; -.
DR   EMDB; EMD-21107; -.
DR   EMDB; EMD-21114; -.
DR   EMDB; EMD-21484; -.
DR   EMDB; EMD-21489; -.
DR   EMDB; EMD-9905; -.
DR   SMR; P32597; -.
DR   BioGRID; 34865; 234.
DR   ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR   ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR   DIP; DIP-5889N; -.
DR   IntAct; P32597; 68.
DR   MINT; P32597; -.
DR   STRING; 4932.YIL126W; -.
DR   iPTMnet; P32597; -.
DR   MaxQB; P32597; -.
DR   PaxDb; 4932-YIL126W; -.
DR   PeptideAtlas; P32597; -.
DR   EnsemblFungi; YIL126W_mRNA; YIL126W; YIL126W.
DR   GeneID; 854680; -.
DR   KEGG; sce:YIL126W; -.
DR   AGR; SGD:S000001388; -.
DR   SGD; S000001388; STH1.
DR   VEuPathDB; FungiDB:YIL126W; -.
DR   eggNOG; KOG0386; Eukaryota.
DR   HOGENOM; CLU_000315_15_3_1; -.
DR   InParanoid; P32597; -.
DR   OMA; VNYISHT; -.
DR   OrthoDB; 5482994at2759; -.
DR   BioCyc; YEAST:G3O-31377-MONOMER; -.
DR   BioGRID-ORCS; 854680; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P32597; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P32597; Protein.
DR   GO; GO:0000785; C:chromatin; NAS:ComplexPortal.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
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:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0015616; F:DNA translocase activity; IDA:SGD.
DR   GO; GO:0004386; F:helicase activity; IDA:UniProtKB.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; IDA:SGD.
DR   GO; GO:0006284; P:base-excision repair; IMP:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR   GO; GO:0031055; P:chromatin remodeling at centromere; IMP:SGD.
DR   GO; GO:0007059; P:chromosome segregation; IGI:SGD.
DR   GO; GO:0007010; P:cytoskeleton organization; IMP:SGD.
DR   GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR   GO; GO:0051321; P:meiotic cell cycle; IMP:UniProtKB.
DR   GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:SGD.
DR   CDD; cd04369; Bromodomain; 1.
DR   CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR   CDD; cd22568; EBM_STH1; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029295; SnAC.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF1012; NUCLEAR PROTEIN STH1_NPS1; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF14619; SnAC; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM01314; SnAC; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Bromodomain; Cell cycle; Chromatin regulator;
KW   Direct protein sequencing; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1359
FT                   /note="Nuclear protein STH1/NPS1"
FT                   /id="PRO_0000074361"
FT   DOMAIN          307..383
FT                   /note="HSA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT   DOMAIN          482..647
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          795..956
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          1270..1340
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          1090..1246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           597..600
FT                   /note="DEGH box"
FT   COMPBIAS        1090..1108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1110..1130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1154..1186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1216..1236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         495..502
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         505
FT                   /note="S->F: Temperature-sensitive."
FT                   /evidence="ECO:0000269|PubMed:9799253"
FT   MUTAGEN         646
FT                   /note="P->L: Temperature-sensitive."
FT                   /evidence="ECO:0000269|PubMed:9799253"
FT   MUTAGEN         763
FT                   /note="C->Y: Temperature-sensitive. Reduced sporulation
FT                   efficiency."
FT                   /evidence="ECO:0000269|PubMed:10320476"
FT   MUTAGEN         792
FT                   /note="K->E: Complete inactivation."
FT   MUTAGEN         806
FT                   /note="S->L: Temperature-sensitive; when associated with
FT                   M-881. Altered cell cycle distribution."
FT                   /evidence="ECO:0000269|PubMed:9799253"
FT   MUTAGEN         881
FT                   /note="T->M: Temperature-sensitive; when associated with
FT                   L-806. Altered cell cycle distribution."
FT                   /evidence="ECO:0000269|PubMed:9799253"
FT   CONFLICT        105..106
FT                   /note="DK -> NE (in Ref. 3; AAZ22501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="D -> N (in Ref. 3; AAZ22501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="K -> R (in Ref. 3; AAZ22501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        546
FT                   /note="N -> T (in Ref. 2; AAA35120)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        566
FT                   /note="V -> I (in Ref. 3; AAZ22501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1010
FT                   /note="A -> R (in Ref. 2; AAA35120)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1074..1080
FT                   /note="Missing (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1114
FT                   /note="A -> V (in Ref. 3; AAZ22501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1157
FT                   /note="I -> V (in Ref. 3; AAZ22501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1221
FT                   /note="G -> S (in Ref. 3; AAZ22501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1246
FT                   /note="S -> P (in Ref. 3; AAZ22501)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..13
FT                   /evidence="ECO:0007829|PDB:6K15"
FT   TURN            18..20
FT                   /evidence="ECO:0007829|PDB:6K15"
FT   HELIX           21..23
FT                   /evidence="ECO:0007829|PDB:6K15"
FT   TURN            26..33
FT                   /evidence="ECO:0007829|PDB:6K15"
FT   HELIX           52..65
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           69..72
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           75..101
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           112..126
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           167..171
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           189..207
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   TURN            220..224
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   STRAND          234..236
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           237..249
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           251..266
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           274..277
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           280..289
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   HELIX           299..317
FT                   /evidence="ECO:0007829|PDB:6V8O"
FT   STRAND          1205..1209
FT                   /evidence="ECO:0007829|PDB:6LQZ"
FT   STRAND          1213..1215
FT                   /evidence="ECO:0007829|PDB:6LQZ"
FT   HELIX           1252..1263
FT                   /evidence="ECO:0007829|PDB:6KMJ"
FT   TURN            1268..1270
FT                   /evidence="ECO:0007829|PDB:6KMJ"
FT   HELIX           1276..1278
FT                   /evidence="ECO:0007829|PDB:6KMJ"
FT   TURN            1284..1286
FT                   /evidence="ECO:0007829|PDB:6KMJ"
FT   HELIX           1290..1293
FT                   /evidence="ECO:0007829|PDB:6KMJ"
FT   HELIX           1300..1308
FT                   /evidence="ECO:0007829|PDB:6KMJ"
FT   HELIX           1315..1332
FT                   /evidence="ECO:0007829|PDB:6KMJ"
FT   HELIX           1338..1356
FT                   /evidence="ECO:0007829|PDB:6KMJ"
SQ   SEQUENCE   1359 AA;  156743 MW;  269A91BD853C20D0 CRC64;
     MLQEQSELMS TVMNNTPTTV AALAAVAAAS ETNGKLGSEE QPEITIPKPR SSAQLEQLLY
     RYRAIQNHPK ENKLEIKAIE DTFRNISRDQ DIYETKLDTL RKSIDKGFQY DEDLLNKHLV
     ALQLLEKDTD VPDYFLDLPD TKNDNTTAIE VDYSEKKPIK ISADFNAKAK SLGLESKFSN
     ATKTALGDPD TEIRISARIS NRINELERLP ANLGTYSLDD CLEFITKDDL SSRMDTFKIK
     ALVELKSLKL LTKQKSIRQK LINNVASQAH HNIPYLRDSP FTAAAQRSVQ IRSKVIVPQT
     VRLAEELERQ QLLEKRKKER NLHLQKINSI IDFIKERQSE QWSRQERCFQ FGRLGASLHN
     QMEKDEQKRI ERTAKQRLAA LKSNDEEAYL KLLDQTKDTR ITQLLRQTNS FLDSLSEAVR
     AQQNEAKILH GEEVQPITDE EREKTDYYEV AHRIKEKIDK QPSILVGGTL KEYQLRGLEW
     MVSLYNNHLN GILADEMGLG KTIQSISLIT YLYEVKKDIG PFLVIVPLST ITNWTLEFEK
     WAPSLNTIIY KGTPNQRHSL QHQIRVGNFD VLLTTYEYII KDKSLLSKHD WAHMIIDEGH
     RMKNAQSKLS FTISHYYRTR NRLILTGTPL QNNLPELWAL LNFVLPKIFN SAKTFEDWFN
     TPFANTGTQE KLELTEEETL LIIRRLHKVL RPFLLRRLKK EVEKDLPDKV EKVIKCKLSG
     LQQQLYQQML KHNALFVGAG TEGATKGGIK GLNNKIMQLR KICNHPFVFD EVEGVVNPSR
     GNSDLLFRVA GKFELLDRVL PKFKASGHRV LMFFQMTQVM DIMEDFLRMK DLKYMRLDGS
     TKTEERTEML NAFNAPDSDY FCFLLSTRAG GLGLNLQTAD TVIIFDTDWN PHQDLQAQDR
     AHRIGQKNEV RILRLITTDS VEEVILERAM QKLDIDGKVI QAGKFDNKST AEEQEAFLRR
     LIESETNRDD DDKAELDDDE LNDTLARSAD EKILFDKIDK ERMNQERADA KAQGLRVPPP
     RLIQLDELPK VFREDIEEHF KKEDSEPLGR IRQKKRVYYD DGLTEEQFLE AVEDDNMSLE
     DAIKKRREAR ERRRLRQNGT KENEIETLEN TPEASETSLI ENNSFTAAVD EETNADKETT
     ASRSKRRSSR KKRTISIVTA EDKENTQEES TSQENGGAKV EEEVKSSSVE IINGSESKKK
     KPKLTVKIKL NKTTVLENND GKRAEEKPES KSPAKKTAAK KTKTKSKSLG IFPTVEKLVE
     EMREQLDEVD SHPRTSIFEK LPSKRDYPDY FKVIEKPMAI DIILKNCKNG TYKTLEEVRQ
     ALQTMFENAR FYNEEGSWVY VDADKLNEFT DEWFKEHSS
//