CHL1_DEBHA
ID CHL1_DEBHA Reviewed; 820 AA.
AC Q6BZD9;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=DEHA2A02112g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382133; CAG84382.2; -; Genomic_DNA.
DR RefSeq; XP_456430.2; XM_456430.1.
DR AlphaFoldDB; Q6BZD9; -.
DR SMR; Q6BZD9; -.
DR STRING; 4959.XP_456430.2; -.
DR PRIDE; Q6BZD9; -.
DR EnsemblFungi; CAG84382; CAG84382; DEHA2A02112g.
DR GeneID; 2899632; -.
DR KEGG; dha:DEHA2A02112g; -.
DR VEuPathDB; FungiDB:DEHA2A02112g; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR InParanoid; Q6BZD9; -.
DR OMA; QTHQFRD; -.
DR OrthoDB; 186062at2759; -.
DR Proteomes; UP000000599; Chromosome A.
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; IPR014001; Helicase_ATP-bd.
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; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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; Repeat.
FT CHAIN 1..820
FT /note="ATP-dependent DNA helicase CHL1"
FT /id="PRO_0000351009"
FT DOMAIN 12..410
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 352..355
FT /note="DEAH box"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 820 AA; 94146 MW; F6813CEEBDED2AB9 CRC64;
MGNLEANDVG NNSRKYNHPF EPYDIQIQLM DAIYDAIDNY KIGLFESPTG TGKTLSLICS
SMTWLREYKK NSTFRETEDS ESEDEPEWVK QAYQKTIANR TKVRAQEYER LLDDLSENYD
VSKVSVLPEK KVKRQKPEQE QDENFIPADY YSDSELDSKY ENDKLTSEIN ELLSRVDGPK
ETVEPVNDCP VKIFFSSRTH SQLSQFSHQL NMTEFESSLD NIPERIKFSP LASRKQLCIH
PKISKLSNVS SINDACIDLQ QSSKNSCEYI PKLHNTQSEE IVKKFSDLSF TKIHDIEDLG
KLGNKLKICP YYSVRKGIDV TEIIALPYQM LLQDSTRSAL NLNIDDSIII IDEAHNLLDV
ISSIYSVSIT SNELSDITKS LKFYLNKFIK RLNSGNRINI MKLIKLCQVL EKFISSNSKD
GKIKHGDEII TSDIFEGTTG DLVNIHKIEQ FLNKSKIAYK IESYMQKLND SESIKNRSNP
LLFKITKFLK CLTNPSKEGK FFWDKTNDSV SINYMLLDPS EIFRDIVKRA RCVLLCGGTM
EPMNDYTNYL FPYIPPEQIK KFSCGHIIPQ ENLEVFPIGN YNDISFEFSF DKRNNSKMII
ELGHAILNII ESTPDGIVIF FPSYKYLNVV MNVWRQNKII ESLTKVKAIF QEPEDSSKVE
KVLNDYSSTN KSEKHSALLL SVVGGKMSEG INFSDELARG VIMIGLPFPN IFSAELIAKR
KFIEESTIAK GGTKSQAMVN AKNFYENICM RAVNQSIGRS IRHKNDYSII YLFDQRYGSD
KIQDKLSGWV KQKLFTRGRC TDFNQVIKET QDFFRQKLLG
