CHL1_YEAST
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 03-AUG-2022, entry version 187.
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}.
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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; 490.
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 PRIDE; P22516; -.
DR EnsemblFungi; YPL008W_mRNA; YPL008W; YPL008W.
DR GeneID; 856099; -.
DR KEGG; sce:YPL008W; -.
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 BioCyc; YEAST:G3O-33927-MON; -.
DR BRENDA; 3.6.4.12; 984.
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; -; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR028331; CHL1/DDX11.
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; PTHR11472; 1.
DR PANTHER; PTHR11472:SF41; PTHR11472:SF41; 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; SSF52540; 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
