CHL1_LODEL
ID CHL1_LODEL Reviewed; 892 AA.
AC A5DUW8;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=LELG_01154;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981524; EDK42976.1; -; Genomic_DNA.
DR RefSeq; XP_001528634.1; XM_001528584.1.
DR AlphaFoldDB; A5DUW8; -.
DR SMR; A5DUW8; -.
DR STRING; 379508.A5DUW8; -.
DR PRIDE; A5DUW8; -.
DR EnsemblFungi; EDK42976; EDK42976; LELG_01154.
DR GeneID; 5235889; -.
DR KEGG; lel:LELG_01154; -.
DR VEuPathDB; FungiDB:LELG_01154; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR InParanoid; A5DUW8; -.
DR OMA; QTHQFRD; -.
DR OrthoDB; 186062at2759; -.
DR Proteomes; UP000001996; 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; 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..892
FT /note="ATP-dependent DNA helicase CHL1"
FT /id="PRO_0000351011"
FT DOMAIN 11..474
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 80..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 416..419
FT /note="DEAH box"
FT COMPBIAS 100..125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 892 AA; 101159 MW; 30C503E9EC01A509 CRC64;
MTSLPSPSAR TCRDYHHPYD PYDIQLQFMD ALYETLQNGY KIGMFESPTG TGKTLSIICS
SMTWLRDYKR NYNLNTKLLE GNVSNNDDKQ AGEDHEGTKG KDDDDDDDDD DDDDDDDDDD
DDEPEWVKMA YQKSIVDKSK NKLKDFERHL NEVDQAYKRR VQKNKEANLG TKIRNVARKQ
QTQEDPEESF LPNDYNETNQ ESFINDVESR NLQLSTEIER LMKSSIINNN GSGSNAVDDA
AAAAAAAATD DECPTKIFFT SRTHSQLNQF SSQLRLTKFD ASFKDLEERT KYLPLGSRKQ
LCINDKVKNR KGEQSINDAC IDLQKTKKGC TYLPNPSNSS TISSATKEFA DLSLAQIRDI
EDLGDLGSSL HTCPYYSVRE GIKLAEVISL PYQLLLQSGS RDALKLDIKN SIIIIDEAHN
IFDTLTSLYS VKITAAQLSR TIKALKIYMT KFLKKLNSGN RINLMKLTKL CKLLMDFLQS
DLAKSAKLGD QVVGEEIFQG STGDLVNIHK MEAYLNKSKI AFKLQSYMEK IGVEDVGTDF
KLNSSSPILF DIVKFLKCLS YPKKEGKFFW DRIYGDNGGC EVSLNYMLLD PCAVFKEIVD
QAKCVILCGG TMEPTSDFTD YLFPSIKHNK IKKFACGHII PKNNLKVIPV GQYYGNFDFL
YNRRNDLDQF KRLGEFLIKI CEIVPAGIVV FISSYQLLSD IVKIWRETTI YSRLNLLKQV
FEESVENTKL TSLLSEYSYV INTQCKGAIL LAVVGGKMSE GINFSDNLAR AVIMVGMPYP
NAFSGEIVAK RNFIEEQVIT KGGTIQQARA KSYEYYDNLC MKAVNQSIGR SIRHAKDYAI
IILLDYRYQT PKVQGKLSKW VRDRIANNTT ANTFDPFLET KKFFSFPIRS TK
