CHL1_KLULA
ID CHL1_KLULA Reviewed; 807 AA.
AC Q6CIF0;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=KLLA0F27181g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98997.1; -; Genomic_DNA.
DR RefSeq; XP_456289.1; XM_456289.1.
DR AlphaFoldDB; Q6CIF0; -.
DR SMR; Q6CIF0; -.
DR STRING; 28985.XP_456289.1; -.
DR PRIDE; Q6CIF0; -.
DR EnsemblFungi; CAG98997; CAG98997; KLLA0_F27181g.
DR GeneID; 2894899; -.
DR KEGG; kla:KLLA0_F27181g; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR InParanoid; Q6CIF0; -.
DR OMA; QTHQFRD; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
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:0034085; P:establishment of sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:EnsemblFungi.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:EnsemblFungi.
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..807
FT /note="ATP-dependent DNA helicase CHL1"
FT /id="PRO_0000351010"
FT DOMAIN 1..415
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 357..360
FT /note="DEAH box"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 807 AA; 92764 MW; 2ECE755906D2F38E CRC64;
MGKNFHHPYQ PYDIQTQLME HIYELLNSGK KVGIFESPTG TGKTLSLICS TVTWLREHKL
EKLNSKVDND NLSDSTFSSS DDEPEWVNQF YNDKIMKEKS KSLQEYENYL EGLSMSNIKP
VLRQLDIGDR KRKKTVPRHI EIEIEDDETN FLPEPYEQDS VSNQNDYEKG QINDEIQKLL
AKIDKGYDVK TENNMELKSP LKIYFSSRTH SQLTQFASQL TLPSFPPSSP TLEKERIKFL
PLASRKQLCI HAKVSKLKSD LINDACVETV KRQECQFYTN SRDLISSKQF RDYTFSEISD
IEDLVQLGHS LHVCPYYSSR TALEGAEIVT LPYQHILSFE IRESLGINLK DSIVIIDEAH
NLMDTITSIY SCEISLSDIK ICKKLMKIYL NKFKRKLNGK NRVNIMKLMK LLDILQAFIE
SHFEKGKEIS PQSMFRDSNA DLLNIHELVT YMRGSKIAYK IDSYADSKLK SDESNTNSVK
QPILFKISKF VLSLSNPSFE GSFFFEEGMI IKYMLLEPNQ IFKTIVNDSK CVILAGGTMQ
PTSEFIENLL PFVPSKDIVQ FSCNHIIPES NLDTFIVSEG FNFNYESRNN ESVMCKLYDF
LLELGCRVPH GIVVFFPSYG YLEHVIKFWQ LEEIFEKLSM NKRIFYETPG GSDILPQYSS
TILDKKKGAF LFSVVGGKLS EGINFQDNLA RAVVMVGLPY PNLYSSELLV KKRHIEQKVI
SAGGSLKDAK SATIEFYENI CMKAVNQSIG RAIRHANDYA CIYLVDNRYL NNKVQHKLSE
WVRKRVKSEL KTSEIFAQTS VFFASNR