CHL1_NEOFI
ID CHL1_NEOFI Reviewed; 861 AA.
AC A1D8E4;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=NFIA_071590;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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}.
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DR EMBL; DS027690; EAW21988.1; -; Genomic_DNA.
DR RefSeq; XP_001263885.1; XM_001263884.1.
DR AlphaFoldDB; A1D8E4; -.
DR STRING; 36630.CADNFIAP00005969; -.
DR EnsemblFungi; EAW21988; EAW21988; NFIA_071590.
DR GeneID; 4590531; -.
DR KEGG; nfi:NFIA_071590; -.
DR VEuPathDB; FungiDB:NFIA_071590; -.
DR eggNOG; KOG1133; Eukaryota.
DR HOGENOM; CLU_006515_2_0_1; -.
DR OMA; QTHQFRD; -.
DR OrthoDB; 186062at2759; -.
DR Proteomes; UP000006702; 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; -; 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; 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_0000351012"
FT DOMAIN 4..431
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 114..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 379..382
FT /note="DEAH box"
FT COMPBIAS 114..140
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; 96660 MW; CFF2A4E29DBF5342 CRC64;
MGSQPQNFNH PYSPYDIQLQ FMRALYTCLE EGKVAVFESP TGTGKSLSLI CGSMTWLREH
KRKALQDTVN KASCSAGDDD GEPEWMLEFA KRESARAVTE KRRALEARLE KIKVEEEKQR
HAHATDHPGE ARKRQRLDTS SGDPGQEQDD QFILDDYDSD AEERITYSKK LGDISGLSTS
TLELLERFKE QFSASAEDET GHEDDDVKIF YCSRTHSQLS QFSSELRRVK MPSSMPAELS
TSDANTDDAE ERVKHLTLGS RKNLCINPKV MSLGNATAIN ERCLELQQPG VAAEKRCPYL
PSKEDEGQVL QFRDHTLATI KDIEDMGKLG KRMGICPYYA SRSVLKHSEI VTLPYPLLLQ
RSARDALDLS IKNHVVIIDE AHNLMDAICN IHSVTITLSQ LQTALSQLTT YARKHKARLK
GKNRSYIAQI IRLISSIADH LRSTIGENLP AEGAVDPSDL MAGKGVDQIN PYKLSRYLQE
SKLARKVDGY VEFSKDKNQQ SDDKPSSPVL FLVQSFLLPL MNPSAEGRFF YLKFHDDIQL
KYMLLDPTNH FREIVEDARA VILAGGTMSP MSDYRNHLFS YIAPSRLDTF SYGHVIPPEN
LIAHTLVNGV LGSEFDFTYD SRDSEKMILD LGRTVAMLCQ AIPDGVVAFF PSYDYLSRIL
AIWRKPLVGE KGQTILSLIE RKKSILYEGR DMGAKTEDLL QEYTRTIDSG QGALLLSVVG
GKLSEGINFS DKLGRGVLII GLPFPNIRSA VWQAKIQYVE QKTYNSSSGS EKDRLSIAKA
AGKDFYENAC MRAVNQCIGR AIRHRNDYAA IVMIDRRYEK ANIQGKLPAW IKQSMLRRSV
RRPASALAAD LSNFFSGRSS G
