CHL1_ASHGO
ID CHL1_ASHGO Reviewed; 801 AA.
AC Q750G3;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-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=AGL010W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54480.1; -; Genomic_DNA.
DR RefSeq; NP_986656.1; NM_211718.1.
DR AlphaFoldDB; Q750G3; -.
DR SMR; Q750G3; -.
DR STRING; 33169.AAS54480; -.
DR EnsemblFungi; AAS54480; AAS54480; AGOS_AGL010W.
DR GeneID; 4622955; -.
DR KEGG; ago:AGOS_AGL010W; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR InParanoid; Q750G3; -.
DR OMA; QTHQFRD; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0045005; P:DNA-templated DNA replication maintenance of fidelity; IEA:EnsemblFungi.
DR GO; GO:0034085; P:establishment of sister chromatid cohesion; IBA:GO_Central.
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; 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..801
FT /note="ATP-dependent DNA helicase CHL1"
FT /id="PRO_0000351001"
FT DOMAIN 2..412
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 347..350
FT /note="DEAH box"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 801 AA; 90288 MW; C97DDDF9AD7624A4 CRC64;
MGRCEFYHPF TPYRIQLELM QQIYGLLESG KKMGIFESPT GTGKTLSLIC STFTWLREHK
AGYLQGSTGA QDSEEDSEDE PAWVKENYEQ SVLADVTASM RAYEQRLAAV DTDLLVKGAA
KRQRVEVAVE RPDDGAEFLP DAYHSDVEER PSHAGGRGQL RKQLDADIKR LLRKLDEPDA
ADKSRLAANP LKVYFASRTH TQLGQFAAQL RLPQFPPSLA GLEQERVKFL PLGSRKQLCI
HKKVSKVKSD GINEACMDAV SKSECSFFSA AREPDIIRQF QDQAFSTIQD IEDLVGIGNT
LHACPYYSSR ELIEGAEVIT LPYQHLLLEN ARKTMGIDLR DSIIVIDEAH NLIDTINSIH
SASISLTELR QCKLALQAYL AKFKTRLNSG NRVNLLKLIK MVDVLSQFIE TQYKNGKRIN
DPNDIFMGTS MDVVNIHKLE KYMKTSKVAY KIDKYIQATT SNDLQDRGSR DIKQPILFKV
ASFLKTLANP SEEGQFFFEN GHVLKYMLLE PSEVLKSIVT EAKCVILAGG TMEPVNDFFT
QLVPYLAPTD VTTYSCGHVI PDDNLNAFIV SENFEFTFAN REDIALIERL FHFIYQLASR
VPFGMVVFFS SYKYIDFVVK TWTDRGLLSR LDAIKRIYHE TSDGADVLKG YSETIQSEKK
GAILLAVVGG RLSEGINFEN ELARAVVLVG LPFPNMFSGE MIVKQQHIKE KVIRNGGTQE
DVNKAVREFY ENICMKAVNQ SVGRAIRHAS DFANVYLIDK RYSGPRIQQK LSDWVRKRIQ
SASNIPKILS DTEAFFSGKG L
