ID   CHL1_ASPFU              Reviewed;         782 AA.
AC   Q4WWE9;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=AFUA_3G05590;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000002; EAL93004.1; -; Genomic_DNA.
DR   RefSeq; XP_755042.1; XM_749949.1.
DR   AlphaFoldDB; Q4WWE9; -.
DR   SMR; Q4WWE9; -.
DR   STRING; 746128.CADAFUBP00004258; -.
DR   EnsemblFungi; EAL93004; EAL93004; AFUA_3G05590.
DR   GeneID; 3512045; -.
DR   KEGG; afm:AFUA_3G05590; -.
DR   VEuPathDB; FungiDB:Afu3g05590; -.
DR   eggNOG; KOG1133; Eukaryota.
DR   HOGENOM; CLU_006515_2_0_1; -.
DR   InParanoid; Q4WWE9; -.
DR   OMA; QTHQFRD; -.
DR   OrthoDB; 186062at2759; -.
DR   Proteomes; UP000002530; Chromosome 3.
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; -; 2.
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   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..782
FT                   /note="ATP-dependent DNA helicase chl1"
FT                   /id="PRO_0000351003"
FT   DOMAIN          1..352
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          23..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           300..303
FT                   /note="DEAH box"
FT   COMPBIAS        23..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         80..87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   782 AA;  88226 MW;  80DC4271948E5647 CRC64;
     MLEFAKRESA RAVTEKRRAL EARLEKIKVE EEKQRHATDH PKEARKRRRV DTSSGDPGPE
     QDDQFILDDY DSDADERMAS SKKLSDISGL STSTLELLER FKEQFSAPVE DEIGHEDDDV
     KIFYCSRTHS QLSQFSSELR RVKMPSSMPA ELSTSDANTD EVQERVKHLT LGSRKNLCIN
     PKVMSLGNAA AINERCLELQ QPGIAAEKRC PYLPSKEDEG QILQFRDHTL ATIKDIEDMG
     KLGKRMGICP YYASRSVLKH SENVLLKAQK IVTLPYPLLL QRSARDALDL SIKNHVVIID
     EAHNLMDAIC NIHSVTIRLS QLQTALLQLT TYAHKHKARL KGKNRSYIAQ IIRLVSSIRD
     HLRSILGQNL PAEGTVDPSD LMAGKGVDQI NPYKLSRYLQ ESKLARKVDG YVEFLKNKNQ
     QSDDKPSSPV LFLVQSFLLS LMNPSAEGRF FYLKCHDDIQ LRYMLLDPTN QFREIVEDAR
     AVILAGGTMS PMSDYRNHLF SYIAPSRLDT FSYGHVIPPE NLIAHTLVNG VLGSEFDFTY
     DSRDSEKMIL DLGRTVATLC QAIPDGVVAF FPSYDYLSRI VAIWRKPLEG EKGETILSLI
     EREKSILYEG RDMGPKTDDL LQEYTRTIDS GQGALLLSVV GGKLSEGINF SDKLGRGVLI
     IGLPFPNIRS AVWQAKIQYV EQKTYNSSSG SEKDRQSIAK AAGKDFYENA CMRAVNQCIG
     RAIRHRNDYA AIVMIDRRYE KANIQGKLPA WIKESMLRRS VRRPASALAA DLSNFFSGRS
     PR