CHL1_CAEEL
ID CHL1_CAEEL Reviewed; 830 AA.
AC Q21489;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=ATP-dependent DNA helicase chl-1 {ECO:0000250|UniProtKB:P22516};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P22516};
DE AltName: Full=Chromosome loss protein homolog {ECO:0000312|WormBase:M03C11.2};
GN Name=chl-1 {ECO:0000312|WormBase:M03C11.2};
GN ORFNames=M03C11.2 {ECO:0000312|WormBase:M03C11.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21968058; DOI=10.1016/j.dnarep.2011.09.011;
RA Chung G., O'Neil N.J., Rose A.M.;
RT "CHL-1 provides an essential function affecting cell proliferation and
RT chromosome stability in Caenorhabditis elegans.";
RL DNA Repair 10:1174-1182(2011).
CC -!- FUNCTION: Required for normal cell proliferation and chromosome
CC stability. Plays a role in DNA repair during replication.
CC {ECO:0000269|PubMed:21968058}.
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:Q96FC9};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22516}.
CC -!- DISRUPTION PHENOTYPE: Uncoordinated and sterile with cell proliferation
CC defects in germ and somatic cells. Hermaphrodite gonads have fewer
CC cells with 13% of homozygotes having only one gonad arm. Most
CC hermaphrodite mutants contain sperm but only 20% contain oocytes that
CC develop as far as diakinesis and those that develop exhibit abnormal
CC karyotypes. Mutant adults contain significantly fewer D neurons and
CC seam cells than wild type. No poly-guanine tract deletions but double
CC mutants of chl-1 and dog-1 display increased deletion frequency when
CC compared to dog-1 mutants. {ECO:0000269|PubMed:21968058}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000255}.
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DR EMBL; Z49128; CAA88959.2; -; Genomic_DNA.
DR RefSeq; NP_499295.2; NM_066894.4.
DR AlphaFoldDB; Q21489; -.
DR BioGRID; 41650; 2.
DR STRING; 6239.M03C11.2; -.
DR EPD; Q21489; -.
DR PaxDb; Q21489; -.
DR EnsemblMetazoa; M03C11.2.1; M03C11.2.1; WBGene00010839.
DR EnsemblMetazoa; M03C11.2.2; M03C11.2.2; WBGene00010839.
DR GeneID; 176457; -.
DR KEGG; cel:CELE_M03C11.2; -.
DR UCSC; M03C11.2; c. elegans.
DR CTD; 176457; -.
DR WormBase; M03C11.2; CE44273; WBGene00010839; chl-1.
DR eggNOG; KOG1133; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR HOGENOM; CLU_006515_2_1_1; -.
DR InParanoid; Q21489; -.
DR OMA; QTHQFRD; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; Q21489; -.
DR PRO; PR:Q21489; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010839; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034085; P:establishment of sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
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; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..830
FT /note="ATP-dependent DNA helicase chl-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000431240"
FT DOMAIN 1..403
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 124..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 351..354
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 124..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 830 AA; 94650 MW; D5F2AB7337D39DF7 CRC64;
MDEFSFPFQP YDIQLNLMRE IRQCIEQRKI GIFESPTGTG KSLSVLCSTM TWLEAEELRI
STDLSTRLGE VHTKITECDK ITTADNWETA VREKMRAQDV ETEILEQIQS RERLQSRIDQ
ARRGMVEVSR KRKAPARDTD QFLEPQDEAA PSEEYNNDEK SEKQRDSDFF DDVDEEEEKP
LKCLKIFYAS RTHSQLEQLA EELAKTRFQP RIVTCASRGT LCVNEEVKKL KLNHLINEKC
MELRKNGMSE KEKVQKLEKG TTKKTKTCAT SCEFYNSTQI EDVVNGVLSN KLKSTLEVSK
QGKLSNGCPY FATRKSVPQC QLVLLPYQVL LHDGTRKAWG IELKDNVIVL DEAHNVLNTI
SSLYSAEIST KSLTLALRLI REYNAHYKLK LLAHNLLYMK QLESLTSKML IFLNSQSKED
VMTMAQLARN LNILEINLFK LAEYMEKTDL CKKFHGFYMR LQKEEIKKEN EKPKLTGIQK
LMAAKEAEPE PEAEPLPPPK PVPSPLFSLK SFIDALTNKC EDGRIIVEKS ATEAKFRFML
LNPADRLSEV VTSARATILV GGTMEPAQLL VETLSRGSIG ADSIRRFSCC HVIDDSQLLA
VTVERTVDGK PFQLTYQTRG ADTTLRSLAT SIQALIPHIP NGVVIFVPSY DFLFNFQKKM
KEFGILKRIE EKKAVFTESR QPTSDVWDRF SRAAKTSKGA ILFAVVGGKM SEGINFCDEL
GRAVIVIGLP YPNKTSVELR ERMKFLDTQM PNGGNLLYES LCMHAVNQAI GRAIRHRRDY
AAVYLFDDRY AKESTRRKLS TWIGDRTQVK LGFGEIIRKT RSFFEANSKK
