ID   CHL1_VANPO              Reviewed;         829 AA.
AC   A7TTL0;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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; ORFNames=Kpol_187p1;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480585; EDO14396.1; -; Genomic_DNA.
DR   RefSeq; XP_001642254.1; XM_001642204.1.
DR   AlphaFoldDB; A7TTL0; -.
DR   STRING; 436907.A7TTL0; -.
DR   PRIDE; A7TTL0; -.
DR   EnsemblFungi; EDO14396; EDO14396; Kpol_187p1.
DR   GeneID; 5542382; -.
DR   KEGG; vpo:Kpol_187p1; -.
DR   eggNOG; KOG1133; Eukaryota.
DR   HOGENOM; CLU_006515_2_0_1; -.
DR   InParanoid; A7TTL0; -.
DR   OMA; QTHQFRD; -.
DR   OrthoDB; 186062at2759; -.
DR   PhylomeDB; A7TTL0; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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; 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..829
FT                   /note="ATP-dependent DNA helicase CHL1"
FT                   /id="PRO_0000351018"
FT   DOMAIN          1..433
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           368..371
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   829 AA;  94536 MW;  2AEC1E579C97F629 CRC64;
     MLMSFNHPYQ PYEIQLQLMQ CIYGALSSGK KIAILESPTG TGKTLSLLCS SITWLRDNKL
     HLLSQNLNNG GIAINSSIEL SDDDDFSDDE PNWVNESYNS SILDNKLLAL NDYEKHLDTI
     ANKHYKIDKN LIGNDNNNNK VKRRKIEHIP VGFEEDEFLP QDYISDSEEL EQTKSEALSN
     EVKALLAKLD SKSNDEQTTS TELLQELNPV KIFFASRTHS QLKQFASQLK LPKFKSSFDE
     KFVSNERLKY LPLGSRKQLC INKSITSKWK STEAINDACK ELLQSEKGCP YHNKNTSNTL
     FRDHVFTGVH DIEDILALGE SLNVCPYYAT RDSITSAEII TLPYQYLLSE STRDSLNIDL
     SNSIVIVDEA HNLIDTINTI HSSHISLQEL KTCQIGLQMY FAKFKSRLNA GNRVNLLKLI
     KLLDILIEYI NKNFKKSGQE ISANEIFNNT NADTLNIHKL NQFIKVSKIA YKIDTYLNSL
     SKESDNENNE ESKNKSTPLL FKVASFLSSL TNPNEEGKFF FEKNKSIKYM LLEPSQSFKS
     ILDEARCVIL AGGTMEPISD FFDNLFPDII KDKSVTFACD HVIPDDNLNT YIIEEPKFEF
     TFDKRQNPEL VNKHLFQFFI KLSVNVPPTG GIVAFFPSYS YLQFVIDNWR SNGLFDKLNK
     IREIFYESKN GSDPLDEYIK VIEARNPAIL FAVVGGKLSE GINFQDDLCR AVVMTGLPYP
     NVMSGELLIK KNHIETKILK NGGSKADVSC ATKDFFDTIC MKAVNQSVGR AIRHIDDYSN
     IYLLDQRYSN SKIKDKLSQW VRKRIQPETN LELIMEKSNR TFQTKKTSN