ID   CHL1_NEUCR              Reviewed;        1068 AA.
AC   A7UXD4;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 2.
DT   03-AUG-2022, entry version 84.
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=NCU11409;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002242; EDO65430.2; -; Genomic_DNA.
DR   RefSeq; XP_001728521.2; XM_001728469.2.
DR   AlphaFoldDB; A7UXD4; -.
DR   SMR; A7UXD4; -.
DR   STRING; 5141.EFNCRP00000009337; -.
DR   EnsemblFungi; EDO65430; EDO65430; NCU11409.
DR   GeneID; 5847921; -.
DR   KEGG; ncr:NCU11409; -.
DR   VEuPathDB; FungiDB:NCU11409; -.
DR   HOGENOM; CLU_006515_2_0_1; -.
DR   InParanoid; A7UXD4; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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: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:0034085; P:establishment of sister chromatid cohesion; IBA:GO_Central.
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   TIGRFAMs; TIGR00604; rad3; 1.
DR   PROSITE; PS00449; ATPASE_A; 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..1068
FT                   /note="ATP-dependent DNA helicase chl1"
FT                   /id="PRO_0000351013"
FT   DOMAIN          31..556
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          85..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          933..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           502..505
FT                   /note="DEAH box"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1068 AA;  118554 MW;  655C822DF7BA3E3E CRC64;
     MASTLPIPDI NVIAPSFIQR DSQNSDNMKP PPTDFNHPYT PYPIQTAFMQ TLYSVLDRTV
     AVSPPTTTNS TNNTAPSATF SSTAATLIPS NPSTSPSTPP LINPTTAPTV HLADRATEPS
     LSVTPRTTTS KDKDKGPSSS SSVPKGHAQI ALFESPTGTG KSLSLICGSL TWLRNHKRLQ
     FDSEIEKIQQ QMEASGEPEW MVESAIKRKR EELAQKYEEM ERTLERIRQK EREMEKEGEE
     GQARGGKRRK LDRGKGDEEK GGKKKESGGS RGLTASDEDK EFLIGDWRDE GGLDENDPMG
     QLSKETRELL EKVGMGTAGG KKEANEGPVA EEEIKIFYTS RTHSQLTQFI QELRRPEFPA
     SVPTPNPQEK PAKEIVKQIP LSSRQKLCIN PTVNKLGTLA AINERCQSLQ QPKTPKDQRC
     PYLPNAANLK ATHEFRDTAL ATLPDIEDLY QTGKQLQICP YYASRAAIPG AEVITLPYPL
     LLQKSAREAL GIRLEGNIVI IDEAHNIMDA VSNVHAAEIK YTDLKRAKLS LGMYYQRFHQ
     KLTGENKVMV AQLQRVVEAL GVYLKTKLDK AALGLKADQE GIVLDTSLLL KTGGADQINL
     YKLIRYVQES KLAFKIEGYI SYCEEEGRDT DDEEAETEIK ARQGRPPVLH TLCSFLTALT
     NLSSEGRIFY EKIPPPRGEL QDMKLSYMLL SPTHAFSSIA ESARAVILAG GTMSPFEDYK
     AHLFPDVPPE KITTLSCGHV IPPDNLCVWT LGSIAPNPKV DTGIGEDCFD FTFAKRSNPN
     MINRLGLVLL NLCSVVPDGV VAFFPSYGYL EEVIGVWKTH EQAMGPKTIW ERLESKKALF
     IDSKTESSEQ TLQKYSDVIH SEVRPLSPAG SRVKGAMLLS VIGGKMSEGI NFSDRLGRCV
     VVVGMPYPNP HSPEWLARRE YLEANFIKRY TASQQTSTAT APLPAPVIPP PSNTTHYSTN
     PSSSRNKDKH KPANVRKLAA RDSHQFYENA TLRAVNQSIG RAIRHQNDYA AIVLIDNRFE
     KEHVRAKLPG WIREGWDETQ RQAKEDGKAL KGLQGMMGRV NMFFRGKN