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 14-OCT-2015, entry version 138. DE RecName: Full=ATP-dependent RNA helicase CHL1; DE EC=3.6.4.13; DE AltName: Full=Chromosome loss protein 1; DE AltName: Full=Chromosome transmission fidelity protein 1; GN Name=CHL1; Synonyms=CTF1; OrderedLocusNames=YPL008W; GN ORFNames=YP8132.05; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2265610; RA Gerring S.L., Spencer F., Hieter P.; RT "The CHL 1 (CTF 1) gene product of Saccharomyces cerevisiae is RT important for chromosome transmission and normal cell cycle RT 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., RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., RA 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., RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., RA Zollner A., 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 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 RT exhibits 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., RA Dephoure N., 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 RT sister-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- RT CCtf18/Dcc1/Ctf8, the helicase Chl1 and the polymerase-alpha- RT associated protein Ctf4 is essential for chromatid disjunction during RT 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 RT insights into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Important for chromosome transmission and normal cell CC cycle progression in G(2)/M. May have a role in changing DNA CC topology to allow the loading of proteins involved in maintaining CC sister chromatid cohesion in the vicinity of the centromeres. Has CC a specific role in chromosome segregation during meiosis II. CC {ECO:0000269|PubMed:10931920, ECO:0000269|PubMed:14742714, CC ECO:0000269|PubMed:15020404, ECO:0000269|PubMed:15226378}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBUNIT: Interacts with ECO1. {ECO:0000269|PubMed:15020404}. CC -!- INTERACTION: CC 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 CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH CC subfamily. DDX11/CHL1 sub-subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. 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 ProteinModelPortal; P22516; -. DR SMR; P22516; 350-828. DR BioGrid; 36169; 249. DR DIP; DIP-4044N; -. DR IntAct; P22516; 4. DR MINT; MINT-526050; -. DR MaxQB; P22516; -. DR PaxDb; P22516; -. DR PeptideAtlas; P22516; -. DR EnsemblFungi; YPL008W; YPL008W; YPL008W. DR GeneID; 856099; -. DR KEGG; sce:YPL008W; -. DR EuPathDB; FungiDB:YPL008W; -. DR SGD; S000005929; CHL1. DR eggNOG; COG1199; -. DR GeneTree; ENSGT00530000063199; -. DR HOGENOM; HOG000241266; -. DR InParanoid; P22516; -. DR KO; K11273; -. DR OMA; ENLCMRA; -. DR OrthoDB; EOG7QC84W; -. DR BioCyc; YEAST:G3O-33927-MONOMER; -. DR NextBio; 981143; -. DR PRO; PR:P22516; -. DR Proteomes; UP000002311; Chromosome XVI. DR GO; GO:0000790; C:nuclear chromatin; IMP:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro. 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; IMP:GOC. 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; IPR010614; DEAD_2. DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS. DR InterPro; IPR013020; DNA_helicase_DNA-repair_Rad3. DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3. DR InterPro; IPR006554; Helicase-like_DEXD_c2. DR InterPro; IPR027417; P-loop_NTPase. 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; 3. 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; Complete proteome; DNA-binding; Helicase; KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1 861 ATP-dependent RNA helicase CHL1. FT /FTId=PRO_0000055138. FT DOMAIN 6 458 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT NP_BIND 42 49 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 393 396 DEAH box. FT MOD_RES 86 86 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT MOD_RES 172 172 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT MUTAGEN 47 47 G->A,V: No ATPase activity; increase in FT chromosome missegregation. FT {ECO:0000269|PubMed:10931920}. FT MUTAGEN 48 48 K->R: No ATPase activity; increase in FT chromosome missegregation. FT {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 //