ID   CHL1_COCIM              Reviewed;         861 AA.
AC   Q1E5T3; J3KKY9;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=CIMG_02080;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAS36726.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; GG704911; EAS36726.3; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001248309.2; XM_001248308.2.
DR   AlphaFoldDB; Q1E5T3; -.
DR   STRING; 246410.Q1E5T3; -.
DR   EnsemblFungi; EAS36726; EAS36726; CIMG_02080.
DR   GeneID; 4565999; -.
DR   KEGG; cim:CIMG_02080; -.
DR   InParanoid; Q1E5T3; -.
DR   OrthoDB; 186062at2759; -.
DR   Proteomes; UP000001261; 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:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
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; 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..861
FT                   /note="ATP-dependent DNA helicase CHL1"
FT                   /id="PRO_0000351008"
FT   DOMAIN          4..428
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          220..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           376..379
FT                   /note="DEAH box"
FT   COMPBIAS        232..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   861 AA;  97469 MW;  CA6770667D9CDA4F CRC64;
     MNPSSKTFYH PYSPYDIQVQ FMRSLYTCIE ECKVGIFESP TGTGKSLSLI CGSLTWLRDH
     KRSVFLEDIE NSDGDDEPEW ILQYSRKEKR RIIRERRKRV EDRLSRIRKE ELLREKAAIA
     NIPFKKQRLE DGKRHLDKMA DDGAFELDEY DSDNQETSTH DAKSNSDLSA TTIALLEKLS
     GSAEIQDDFE EENAVKIFYC SRTHSQLAQF ARELRRVVFP PSIPPETEDG EIDTQGEGRR
     HPDTELEEPT KHVSLGSRKT MCINPKVRRL GNATAINERC LDLQSSNVLP GHKCPFAPSK
     ENELAINDFR DHVLAEVHDI EDIGKIGQRT GICPYYASRS VIGHSEIVTL PYQLLLQKSA
     RDALDISLKD HVIIIDEAHN LMDVIANIHS VNVSLTQLRI GLEQLTIYAR KYKARLKGKN
     RVYVAQVMRL LGSIAKYLES VLAARELREG AVDPSYLMSG KGIDQINLHK LSRYLQESKL
     ARKVDGYIES STSLEEKNPE TSTTVPVLFQ VQSFLLSLMN PSAEGRLFFE KNGNDVLLKY
     TLLDPTAHFR EAVEEARAVI LAGGTMSPMS DYRDHLFSYL APGQLRTFSY GHVIPTSNLS
     ARPVSRGILD TEFDFTFEKR NSRAMIIDLG KTISEICKAT PDGVVAFFPS YDFLNQVVEI
     WKQPCSNSGN PSILDSLGLV KPLLYESKEK AMNTEALLQK YANFIDEGKG ALLLSVMGGK
     LSEGINFSDR LGRGVIVIGL PFANIRSAEW QAKIQYVERK TYERSSGGEE TRRSKAKLAG
     RDFYENACMR VVNQCIGRAI RHQHDYAAIL MFDRRYGTAR IQSKLPEWIR RSLISAPIGA
     TISNLYTFFE EKSSIEVTKE K