CHL1_YARLI
ID CHL1_YARLI Reviewed; 803 AA.
AC Q6CAX3;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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; OrderedLocusNames=YALI0C23639g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382129; CAG82511.1; -; Genomic_DNA.
DR RefSeq; XP_502189.1; XM_502189.1.
DR AlphaFoldDB; Q6CAX3; -.
DR SMR; Q6CAX3; -.
DR STRING; 4952.CAG82511; -.
DR EnsemblFungi; CAG82511; CAG82511; YALI0_C23639g.
DR GeneID; 2909620; -.
DR KEGG; yli:YALI0C23639g; -.
DR VEuPathDB; FungiDB:YALI0_C23639g; -.
DR HOGENOM; CLU_006515_2_0_1; -.
DR InParanoid; Q6CAX3; -.
DR OMA; QTHQFRD; -.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
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; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProt.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0045005; P:DNA-templated DNA replication maintenance of fidelity; IEA:EnsemblFungi.
DR GO; GO:0034085; P:establishment of sister chromatid cohesion; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..803
FT /note="ATP-dependent DNA helicase CHL1"
FT /id="PRO_0000351019"
FT DOMAIN 5..388
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 330..333
FT /note="DEAH box"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 803 AA; 90691 MW; 8ECAEB0538BD47EE CRC64;
MENTKRREFS HPYTPYPIQV DFMEALYDCI ESYKVGIFES PTGTGKTLSL ICGSMTWLRK
NKAQLAVSTA SADENEPAWV LEQTIQLARE EFSRNREMLQ KRLDKMRRKN MRARISYEQG
FKRAKKAPEP VDDSQFLPED YSEVIKPEVQ RLLSALAPPV ENDFQEPVKI IFASRTHSQL
SQFVGQMQHT TFPPSSDLQD LESTKLISLG SRKQLCINPR VSHMNSVQAM NDACRDLREG
KKGGCKYYKN PHDALGKVDI NTFRDTTLAE ILDIEDLYKL GKHTSTCPYY ASRASIPASE
VITVPYQILL SRSARKAIDL PVKNSIVIID EAHNLLDTIT SLHTMSITKS QVSSASSGLQ
KYQHKFQNRL NSGNRVNLGY LVNMLQALEV FFEKAQKFHK KETAPGTPVT TSSLFDGSTA
DLINVNRLEK YIDESKIVFK IESYLEHVNG ETQEKSHSSS LVLSSVMEFL RQVNNPDSEG
VLCFDGPTKL KYQLLDPSEP FKDIVENARC VVLAGGTMEP TGDYLEYLLP YLSQDQIKLF
SCGHVIPPQN LSVQVIPNGP NYSFNFTFDK RNDEKMILDV AITLLVYSKI IPEGMVVFFP
SYKYLEQVVA VWKKAKKDGK NIYEILNDQK RIFVESQHDS VEKTLSEYAE EVPKGAILLS
VVGGKMSEGI NFSDGLARAV FMIGLPFPNL MSAEIIAKRK YIEQSVSEKM KAKGVSAKEA
LEASKGAARD FYMNICLRAV NQSVGRAIRH ANDYACIFLL DGRFGKPEIQ KKLSKWMREG
IREGSFKEAL GEVQQFFASH EKN
