CHL1_CANGA
ID CHL1_CANGA Reviewed; 830 AA.
AC Q6FKT4;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=CAGL0L08844g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380958; CAG62130.1; -; Genomic_DNA.
DR RefSeq; XP_449160.1; XM_449160.1.
DR AlphaFoldDB; Q6FKT4; -.
DR SMR; Q6FKT4; -.
DR STRING; 5478.XP_449160.1; -.
DR PRIDE; Q6FKT4; -.
DR EnsemblFungi; CAG62130; CAG62130; CAGL0L08844g.
DR GeneID; 2891091; -.
DR KEGG; cgr:CAGL0L08844g; -.
DR CGD; CAL0136034; CAGL0L08844g.
DR VEuPathDB; FungiDB:CAGL0L08844g; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR InParanoid; Q6FKT4; -.
DR OMA; QTHQFRD; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0045005; P:DNA-templated DNA replication maintenance of fidelity; IEA:EnsemblFungi.
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; 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; 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.
FT CHAIN 1..830
FT /note="ATP-dependent DNA helicase CHL1"
FT /id="PRO_0000351007"
FT DOMAIN 3..438
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 373..376
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 830 AA; 94515 MW; 10AE67FE16487583 CRC64;
MDNATKFHHP YSPYDIQLDL MQCVYDTLAN PVKKVAIVES PTGTGKTLSL ICSTLTWLRD
NKADILSSVD TLHSNEDDSH DSEPEWVKDT YKESILKDKL ELLDEYEKYL EELHLKENKI
IKFGTSIEDK SKVKRRKVTS SSKAKIEVSI EDEDEFVAKP YESDGEETTD LEKKEALSKE
VQELLAKFDS SKKNTDNVEL GRFASASQNQ VRIFFSSRTH SQLNQFAEQL KLTNFPSSFP
DKVAHERVKY MPLGSKKQLC INPDVKKWKT LEGINDACSE VRRSKEGCPF YQNTPKWHNS
KETNHFRDQV FSDIHDIEDI AKVGESLAVC PYYAARDFIP SSEIVTLPYQ YLLSESTRSQ
LRLDLKGSIV VIDEAHNLVD TINSIHSAEI SLSELKQSYN SIILYMKKFK SRLNPGNRVN
LLKLSKLITV LINFITTHYK KPGLEVDAFS ILESNNTDML NVHRVLKYIK TSHIAYKLDT
YIQKLQEKES PSNQKPSSQP LLYKISKFLE CLNNTSSEGS FFFERGPSLR YMLLEPSRIF
QDIIDSARCV ILAGGTMEPV SQLLQYLVPK LDDSSITKFS CNHVIPDSHL RTYIVNEPQF
EFTFEKRNSV NLVQNHLFNF YLELSTTIPK TGGIIGFFPS YKYLDEIIVS WRKAGLFEKL
DKERKVFYEM KDGPDPLPDY TSAVANSEGA ILFAIVGGKL SEGINFGGNL CRAIVMTGLP
YPNVFSGELI ISRKHLEEKV LNGGGSKTDA NMAAKEFFEN ICMKAVNQSV GRSIRSINDY
SLIYLLDKRY ANANIQSKLS QWVRSRIQSV STVRDVMASS KEFFDQIADT
