CHL1_ASPCL
ID CHL1_ASPCL Reviewed; 731 AA.
AC A1CJ34;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=ACLA_033610;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027056; EAW09158.1; -; Genomic_DNA.
DR RefSeq; XP_001270584.1; XM_001270583.1.
DR AlphaFoldDB; A1CJ34; -.
DR SMR; A1CJ34; -.
DR STRING; 5057.CADACLAP00003140; -.
DR PRIDE; A1CJ34; -.
DR EnsemblFungi; EAW09158; EAW09158; ACLA_033610.
DR GeneID; 4703543; -.
DR KEGG; act:ACLA_033610; -.
DR VEuPathDB; FungiDB:ACLA_033610; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR OMA; HAINQSI; -.
DR OrthoDB; 186062at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0045005; P:DNA-templated DNA replication maintenance of fidelity; IEA:EnsemblFungi.
DR GO; GO:0034085; P:establishment of sister chromatid cohesion; IEA:EnsemblFungi.
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..731
FT /note="ATP-dependent DNA helicase chl1"
FT /id="PRO_0000351002"
FT DOMAIN 1..299
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 247..250
FT /note="DEAH box"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 731 AA; 82217 MW; 6E467D954774DD62 CRC64;
MCQKYDTLSG DRDVEHDEHF VLEDYDSESE DQNISSKSLG HSSELSMSTL ALLERFKKQY
SAPTEEEETV GDDEPKIFYC SRTHSQLAQF ASELRRVEMP PSLPKELSEK LTDSEALEER
VKHLSLGSRK NLCINPRVMK LENATAINER CMDLQQPGMA VEHRCPYLPS KDDEPQVLQF
RDHTLATVKD IEDMGKLGKH IGVCPYYASR SVIKHSEIVT LPYPLLLQRS AREALGLSIK
NHIVIIDEAH NLMDAISNIH SVTITLSQLQ TAIFQLTTYA RKFKTRLKGK NRTYIAQVIR
LVSSVADHLR SIQGSNQPPD GAVKTSDLMA GKGVDQINPY KLSHYLQESK LARKVDGYVE
YSKDTANRQS HGKPSTPVLF HVQSFLLPLM NPSAEGRLFY MKDQNDIQLK YLLLDPTNHF
REIVEDARAV ILAGGTMSPM SDYMNHLFPY VPASRLDTFS YGHVIPPENL VAHTLAQGVM
GCAFDFTYES RDSEKMIIDL GRTVATLCQA IPDGVVAFFP SYDYLSRILH IWKKPLGADK
NQTILGLIER KKPILYESRD MTTKSDDILQ EYTRTIDSGS GALLLSVIGG KLSEGINFSD
RLGRGVLIIG LPFPNIRSAV WQAKLQYVEQ KAYSGSSGSE TDRQMIAKAA GRDFYENACM
RAVNQCIGRA IRHRNDYAAI VMIDRRYDKP NIQGKLPAWI KQSMVRSPTQ RPAGATVQNL
IKFFAARGSL D
