CHL1_PICGU
ID CHL1_PICGU Reviewed; 825 AA.
AC A5DNW6;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 81.
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=PGUG_04967;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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; CH408160; EDK40869.2; -; Genomic_DNA.
DR RefSeq; XP_001483012.1; XM_001482962.1.
DR AlphaFoldDB; A5DNW6; -.
DR SMR; A5DNW6; -.
DR STRING; 4929.XP_001483012.1; -.
DR EnsemblFungi; EDK40869; EDK40869; PGUG_04967.
DR GeneID; 5124774; -.
DR KEGG; pgu:PGUG_04967; -.
DR VEuPathDB; FungiDB:PGUG_04967; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR InParanoid; A5DNW6; -.
DR OMA; QTHQFRD; -.
DR OrthoDB; 186062at2759; -.
DR Proteomes; UP000001997; 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..825
FT /note="ATP-dependent DNA helicase CHL1"
FT /id="PRO_0000351014"
FT DOMAIN 6..415
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 67..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 359..362
FT /note="DEAH box"
FT COMPBIAS 67..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 825 AA; 93770 MW; 7F030820B94DAB08 CRC64;
MNRDDPRLTY NHPYKPYDIQ VQLMDAIYDT IQNKYKVGLF ESPTGTGKTL SIICSSMTWL
RNYKKTQDHS TMGSNSSNDN DPNQTSDSDE EPDWVKEAHI KNIRSRTSGL AIDYERHLEE
LSQTPHAGHT VELGQRTHKR KKRATNDDDF LPDDYNSDTD SNSVETKNAK LQQEINQIMK
RVDGSDGKTP GFVNTCPVTI FFSSRTHSQL SQFAHQLSIT SFESSLGEIA ERIKFMPLSS
RKQLCIHPKV SSLSSVSAVN DACVELQQKS DKRCEFMPRV NNPESDQLVQ RFADYSFAVI
KDIEELHELG ADLKVCPYYA SRRNIENSEI IALPYQMLLQ QATRKSLGLS IKDSIVIIDE
AHNLLDVISS INSVSITRKE LSSVIASLKL YYNKFTKRLN SGNRIHLMKL IKLCSLVETY
IKNCEIQNKC VPGSDVLIDE LFQGSTGDLL NIHRIEKYLD KSKIAYKIQT YIEQSREESD
EKQASSPLLF KVTAFLKSLV NPSKEGRFFW DKINDDTEIK YLLLDPSEMF RDVVESARCV
LLCGGTMEPV EDYYRYLFPY VPGEKIKKFT CGHIVPQENI EVLTVSSRKT TVFDFSYHKR
NDPSMLRELA LSLQDICERV PNGIIVFAPS YKYLNQLIST WRKDGNLAKI STLKQVFLES
SDSTSIESIL RDYGAAARGS GAILFSVVGG KMSEGVNFSD ELARAVIMLG LPYPNAFSGE
LIAKRKFIEE TTLSKGGTQA MAKKNSREYY ENICMRAVNQ SVGRSIRHAN DYSVIVLFDT
RYNSSHIQSK LSGWMRSSIR PERESFDMTL ERIADFFAAK TLTKR
