CHL1_CANAL
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 03-AUG-2022, entry version 101.
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}.
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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 PRIDE; Q5AD67; -.
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; 186062at2759; -.
DR PRO; PR:Q5AD67; -.
DR Proteomes; UP000000559; Chromosome 2.
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; 3.
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..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
