CHL1_PICST
ID CHL1_PICST Reviewed; 835 AA.
AC A3LN13;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=PICST_54439;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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; CP000496; ABN64250.2; -; Genomic_DNA.
DR RefSeq; XP_001382279.2; XM_001382242.1.
DR AlphaFoldDB; A3LN13; -.
DR SMR; A3LN13; -.
DR STRING; 4924.XP_001382279.2; -.
DR EnsemblFungi; ABN64250; ABN64250; PICST_54439.
DR GeneID; 4836691; -.
DR KEGG; pic:PICST_54439; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR InParanoid; A3LN13; -.
DR OMA; QTHQFRD; -.
DR OrthoDB; 186062at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
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..835
FT /note="ATP-dependent DNA helicase CHL1"
FT /id="PRO_0000351015"
FT DOMAIN 8..421
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 130..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 363..366
FT /note="DEAH box"
FT COMPBIAS 147..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 835 AA; 95266 MW; C9D5AB0984FBC32C CRC64;
METSICSPEN RYSHPYKPYD IQIQLMDAIY DTIDNGYKIG LFESPTGTGK TLSIICSTMT
WLRDYKRENV FQPMAGLDGS DTDDSDSDDE PEWVKKAYRD TIVSRSENKM VDYEMYLEKI
QNEYENNIQT AGSIKSSRPP KKKRSTAKKQ ELHDEDFLPE DYYSDSEVKP NADKLTVLES
EISQLLDKVN GRTDEIEMTN DCPVNIYFSS RTHSQLNQFA HQLALTKFQS SFKGVEERTK
YLPIGSRKQL CINEKVKSFS KNDSNINDVC VDLQKSKEGC QFLPKDYLNS SLTKKLSDLS
LSKIHDIEEI ADLGSNMKVC PYYSVRKGVE MTEIISLPYQ ILLSESTRAI LNLQIEDSIV
VIDEAHNLMD TITSMHSVCI TIGEMNSIIK ALKFYLGRFL KKLNSGNRIH LMKLIKLCQL
VISFIQKSEK CNNIKVGNEI NTSDIYQNST GDMLNIHILE AFLAKSKIAY KIESYMEKVA
ENENEQAKTS SSNPLLYKIV QFLKCLVNPS KEGKFFWDST NGITSIKYML LDPSSVFKDI
VSKARCVILC GGTMEPMSEF KNFLFPYVED KKIKSFSCNH IIPPDNLKVY PVSSQNNVTL
EFSFDNRNNP LMIEALGASI VRICQSVPDG VVVFFPSYKY MNHILSIWKS TDVLTQIESQ
KKLFEEPTSA SQVQTILADY ANTIKEEKKG AILFSVVGGK MSEGINFADE LGRAVVMVGL
PYPNAYSGEI IAKRKFIESE AIARGCSMSE AQRNSQSYYE NLCMRAVNQS IGRSIRHIND
YSIIYLVDCR YQSSRIQNKL SSWVRKRIET RNYNMDQIME ETRDFFMCKT IARLA
