CHL1_YEAS7
ID CHL1_YEAS7 Reviewed; 861 AA.
AC A6ZWN8;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=ATP-dependent DNA helicase CHL1 {ECO:0000250|UniProtKB:P22516};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P22516};
DE AltName: Full=Chromosome loss protein 1 {ECO:0000250|UniProtKB:P22516};
GN Name=CHL1; ORFNames=SCY_5715;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: ATP-dependent DNA helicase important for chromosome
CC transmission and normal cell cycle progression in G(2)/M (By
CC similarity). May have a role in changing DNA topology to allow the
CC loading of proteins involved in maintaining sister chromatid cohesion
CC in the vicinity of the centromeres (By similarity). Has a specific role
CC in chromosome segregation during meiosis II (By similarity).
CC {ECO:0000250|UniProtKB:P22516}.
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:0000250|UniProtKB:P22516};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22516}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000305}.
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DR EMBL; AAFW02000135; EDN61130.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZWN8; -.
DR SMR; A6ZWN8; -.
DR PRIDE; A6ZWN8; -.
DR EnsemblFungi; EDN61130; EDN61130; SCY_5715.
DR HOGENOM; CLU_006515_2_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProt.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein.
FT CHAIN 1..861
FT /note="ATP-dependent DNA helicase CHL1"
FT /id="PRO_0000351020"
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:0000250|UniProtKB:P22516"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22516"
SQ SEQUENCE 861 AA; 98822 MW; 130B15C4A5FFA65A 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 DKVPNEKVKY LPLASKKQLC INPKVMKWKT LEAINDACAD
LRHSKEGCMF 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
PSKDITTLSC 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
