ID CHL1_YEAST Reviewed; 861 AA. AC P22516; D6W404; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 22-FEB-2023, entry version 189. DE RecName: Full=ATP-dependent DNA helicase CHL1; DE EC=3.6.4.12 {ECO:0000269|PubMed:10931920}; DE AltName: Full=Chromosome loss protein 1; DE AltName: Full=Chromosome transmission fidelity protein 1; GN Name=CHL1; Synonyms=CTF1; OrderedLocusNames=YPL008W; ORFNames=YP8132.05; 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=2265610; DOI=10.1002/j.1460-2075.1990.tb07884.x; RA Gerring S.L., Spencer F., Hieter P.; RT "The CHL 1 (CTF 1) gene product of Saccharomyces cerevisiae is important RT for chromosome transmission and normal cell cycle progression in G2/M."; RL EMBO J. 9:4347-4358(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [3] 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 [4] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP GLY-47 AND LYS-48. RX PubMed=10931920; DOI=10.1093/nar/28.16.3056; RA Holloway S.L.; RT "CHL1 is a nuclear protein with an essential ATP binding site that exhibits RT a size-dependent effect on chromosome segregation."; RL Nucleic Acids Res. 28:3056-3064(2000). RN [5] 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 [6] RP FUNCTION, INTERACTION WITH ECO1, AND SUBCELLULAR LOCATION. RX PubMed=15020404; DOI=10.1534/genetics.166.1.33; RA Skibbens R.V.; RT "Chl1p, a DNA helicase-like protein in budding yeast, functions in sister- RT chromatid cohesion."; RL Genetics 166:33-42(2004). RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15226378; DOI=10.1242/jcs.01231; RA Petronczki M., Chwalla B., Siomos M.F., Yokobayashi S., Helmhart W., RA Deutschbauer A.M., Davis R.W., Watanabe Y., Nasmyth K.; RT "Sister-chromatid cohesion mediated by the alternative RF-CCtf18/Dcc1/Ctf8, RT the helicase Chl1 and the polymerase-alpha-associated protein Ctf4 is RT essential for chromatid disjunction during meiosis II."; RL J. Cell Sci. 117:3547-3559(2004). RN [8] RP FUNCTION. RX PubMed=14742714; DOI=10.1091/mbc.e03-08-0619; RA Mayer M.L., Pot I., Chang M., Xu H., Aneliunas V., Kwok T., Newitt R., RA Aebersold R., Boone C., Brown G.W., Hieter P.; RT "Identification of protein complexes required for efficient sister RT chromatid cohesion."; RL Mol. Biol. Cell 15:1736-1745(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-172, 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: ATP-dependent DNA helicase important for chromosome CC transmission and normal cell cycle progression in G(2)/M CC (PubMed:10931920). May have a role in changing DNA topology to allow CC the loading of proteins involved in maintaining sister chromatid CC cohesion in the vicinity of the centromeres (PubMed:15020404, CC PubMed:14742714). Has a specific role in chromosome segregation during CC meiosis II (PubMed:15226378). {ECO:0000269|PubMed:10931920, CC ECO:0000269|PubMed:14742714, ECO:0000269|PubMed:15020404, CC ECO:0000269|PubMed:15226378}. 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 Evidence={ECO:0000269|PubMed:10931920}; CC -!- SUBUNIT: Interacts with ECO1. {ECO:0000269|PubMed:15020404}. CC -!- INTERACTION: CC P22516; P43605: ECO1; NbExp=2; IntAct=EBI-4600, EBI-22988; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10931920, CC ECO:0000269|PubMed:15020404, ECO:0000269|PubMed:15226378}. CC -!- MISCELLANEOUS: Present with 98 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. CC DDX11/CHL1 sub-subfamily. {ECO:0000305}. 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; U33335; AAB68097.1; -; Genomic_DNA. DR EMBL; X56584; CAA39922.1; -; Genomic_DNA. DR EMBL; Z48483; CAA88378.1; -; Genomic_DNA. DR EMBL; Z71255; CAA95033.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11420.1; -; Genomic_DNA. DR PIR; S12499; S12499. DR RefSeq; NP_015317.1; NM_001183822.1. DR AlphaFoldDB; P22516; -. DR BioGRID; 36169; 491. DR DIP; DIP-4044N; -. DR IntAct; P22516; 4. DR MINT; P22516; -. DR STRING; 4932.YPL008W; -. DR iPTMnet; P22516; -. DR MaxQB; P22516; -. DR PaxDb; P22516; -. DR PeptideAtlas; P22516; -. DR EnsemblFungi; YPL008W_mRNA; YPL008W; YPL008W. DR GeneID; 856099; -. DR KEGG; sce:YPL008W; -. DR AGR; SGD:S000005929; -. DR SGD; S000005929; CHL1. DR VEuPathDB; FungiDB:YPL008W; -. DR eggNOG; KOG1133; Eukaryota. DR GeneTree; ENSGT00950000182970; -. DR HOGENOM; CLU_006515_2_0_1; -. DR InParanoid; P22516; -. DR OMA; QTHQFRD; -. DR OrthoDB; 124793at2759; -. DR BioCyc; YEAST:G3O-33927-MON; -. DR BRENDA; 3.6.4.12; 984. DR BioGRID-ORCS; 856099; 0 hits in 10 CRISPR screens. DR PRO; PR:P22516; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; P22516; protein. DR GO; GO:0000785; C:chromatin; IMP:SGD. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IMP:SGD. DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central. DR GO; GO:0034085; P:establishment of sister chromatid cohesion; IMP:SGD. DR GO; GO:0036297; P:interstrand cross-link repair; IGI:SGD. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3. DR InterPro; IPR006555; ATP-dep_Helicase_C. DR InterPro; IPR010614; DEAD_2. DR InterPro; IPR045028; DinG/Rad3-like. DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS. DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3. DR InterPro; IPR006554; Helicase-like_DEXD_c2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013020; Rad3/Chl1-like. DR PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1. DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1. DR Pfam; PF06733; DEAD_2; 1. DR Pfam; PF13307; Helicase_C_2; 1. DR SMART; SM00488; DEXDc2; 1. DR SMART; SM00491; HELICc2; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR TIGRFAMs; TIGR00604; rad3; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell cycle; DNA-binding; Helicase; Hydrolase; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..861 FT /note="ATP-dependent DNA helicase CHL1" FT /id="PRO_0000055138" FT DOMAIN 6..458 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT REGION 161..188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 393..396 FT /note="DEAH box" FT BINDING 42..49 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 86 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 172 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MUTAGEN 47 FT /note="G->A,V: No ATPase activity; increase in chromosome FT missegregation." FT /evidence="ECO:0000269|PubMed:10931920" FT MUTAGEN 48 FT /note="K->R: No ATPase activity; increase in chromosome FT missegregation." FT /evidence="ECO:0000269|PubMed:10931920" SQ SEQUENCE 861 AA; 98806 MW; 15D0CC397A77F8F2 CRC64; MDKKEYSETF YHPYKPYDIQ VQLMETVYRV LSEGKKIAIL ESPTGTGKTL SLICATMTWL RMNKADIFTR METNIKTNED DSENLSDDEP DWVIDTYRKS VLQEKVDLLN DYEKHLNEIN TTSCKQLKTM CDLDKEHGRY KSVDPLRKKR KGARHLDVSL EEQDFIPRPY ESDSENNDTS KSTRGGRISD KDYKLSELNS QIITLLDKID GKVSRDPNNG DRFDVTNQNP VKIYYASRTY SQLGQFTSQL RLPSFPSSFR DKVPDEKVKY LPLASKKQLC INPKVMKWKT LEAINDACAD LRHSKEGCIF YQNTNEWRHC PDTLALRDMI FSEIQDIEDL VPLGKSLGIC PYYASREALP IAEVVTLPYQ YLLSESTRSS LQINLENSIV IIDEAHNLIE TINSIYSSQI SLEDLKNCHK GIVTYFNKFK SRLNPGNRVN LLKLNSLLMT LIQFIVKNFK KIGQEIDPND MFTGSNIDTL NIHKLLRYIK VSKIAYKIDT YNQALKEEES SKNENPIKET HKKSVSSQPL LFKVSQFLYC LTNLTSEGQF FFEKNYSIKY MLLEPSKPFE SILNQAKCVV LAGGTMEPMS EFLSNLLPEV PSEDITTLSC NHVIPKENLQ TYITNQPELE FTFEKRMSPS LVNNHLFQFF VDLSKAVPKK GGIVAFFPSY QYLAHVIQCW KQNDRFATLN NVRKIFYEAK DGDDILSGYS DSVAEGRGSL LLAIVGGKLS EGINFQDDLC RAVVMVGLPF PNIFSGELIV KRKHLAAKIM KSGGTEEEAS RATKEFMENI CMKAVNQSVG RAIRHANDYA NIYLLDVRYN RPNFRKKLSR WVQDSINSEH TTHQVISSTR KFFSMRSLNS R //