ID   CHL1_CANAL              Reviewed;         842 AA.
AC   Q5AD67; A0A1D8PGA4;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 106.
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=CAALFM_C201240CA;
GN   ORFNames=CaO19.2000, CaO19.9551;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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}.
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; CP017624; AOW27172.1; -; Genomic_DNA.
DR   RefSeq; XP_719450.1; XM_714357.1.
DR   AlphaFoldDB; Q5AD67; -.
DR   SMR; Q5AD67; -.
DR   STRING; 237561.Q5AD67; -.
DR   EnsemblFungi; C2_01240C_A-T; C2_01240C_A-T-p1; C2_01240C_A.
DR   GeneID; 3638794; -.
DR   KEGG; cal:CAALFM_C201240CA; -.
DR   CGD; CAL0000177726; orf19.9551.
DR   VEuPathDB; FungiDB:C2_01240C_A; -.
DR   eggNOG; KOG1133; Eukaryota.
DR   HOGENOM; CLU_006515_2_0_1; -.
DR   InParanoid; Q5AD67; -.
DR   OrthoDB; 124793at2759; -.
DR   PRO; PR:Q5AD67; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR   GO; GO:0034085; P:establishment of sister chromatid cohesion; IBA:GO_Central.
DR   GO; GO:0036297; P:interstrand cross-link repair; IEA:EnsemblFungi.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
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; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   NCBIfam; TIGR00604; rad3; 1.
DR   PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
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..842
FT                   /note="ATP-dependent DNA helicase CHL1"
FT                   /id="PRO_0000351006"
FT   DOMAIN          6..417
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          476..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           359..362
FT                   /note="DEAH box"
FT   COMPBIAS        484..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   842 AA;  97275 MW;  A241696BAC817F99 CRC64;
     MVSESCSRNY NHPYTPYDIQ IQLMDAIYNT IENGYKIGLF ESPTGTGKTL SIICSSMTWL
     RTFKRNNTFL ETNNEVEDVY ESESEEDEPE WVKKAYQSSI VNRSKNKLIE YEHYLDKIEK
     EHAQNKRKEE ELEIKVHKRR KAMTAAGTDL SEESYLPMDY YSDSEVGKIE DQNLAITKEI
     NRLLKKVENK EEVSYINECP IKIFFSSRTH SQLNQFSSQL RLTNFQASFE DLEERTKYIP
     LGSRKQLCIN EKVRSKGNDQ SVNDACLDLQ RETNGCQYLP KNYMMSSVTK EFADLSLAKI
     RDIEDLNELG IELNICPYYS VRKGIEMTEI ISLPYQMIFQ DTTRKILNLD IKDSIIIIDE
     AHNIIDVITS MYSIKITSDQ LNKVIKSLKI YLNKFLKRLN SGNRINLMKL IKICQILLKF
     LNTNSEKVKS GDEVQIQDIF KDSTGDLVNI HKLDQFLTKS KIAYKIESYI EKTEMETDNG
     EKKGRITNSG GSSSSSSSSN PLLFTIIKFL RTLTNLSKEG KFFWDNENGT ISLNYMLLDP
     SAVFKEIVDQ AKCVLLCGGT MEPMSDYMDY LFPSVPTNKI NTFACGHVIP KENLQVFPIS
     QWNDTNFEFS YQKRNDSKQL MALGEFLIEI TKRVPYGVVI FFPSYKYLDQ VLQFWRDTKI
     LTSIESEKTI FREPKDPSNV EKVLNEYGYL IQTERKGAIL FSVVGGKMSE GINFSDDLAR
     AVIMVGLPYP NAYSGEMVTK RKYIETSELS NGGTTTDAKE KSRNYYENLC MRAVNQSIGR
     SIRHINDYSI IYLVDRRFST PRIQNKLSQW VKERISITTT NNNNNNSIYI MESTTDFFNI
     IR
//