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Database: UniProt
Entry: A0A2H3II07_9EURO
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ID   A0A2H3II07_9EURO        Unreviewed;       839 AA.
AC   A0A2H3II07;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   RecName: Full=ATP-dependent DNA helicase CHL1 {ECO:0000256|ARBA:ARBA00017386};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   AltName: Full=ATP-dependent DNA helicase chl1 {ECO:0000256|ARBA:ARBA00016387};
DE   AltName: Full=Chromosome loss protein 1 {ECO:0000256|ARBA:ARBA00029709};
GN   ORFNames=PENO1_038480 {ECO:0000313|EMBL:PCH02256.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH02256.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCH02256.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCH02256.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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.
CC       {ECO:0000256|ARBA:ARBA00025396}.
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:0000256|ARBA:ARBA00001665};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCH02256.1}.
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DR   EMBL; NPFK01000086; PCH02256.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3II07; -.
DR   STRING; 290292.A0A2H3II07; -.
DR   OrthoDB; 124793at2759; -.
DR   Proteomes; UP000218381; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:DNA damage response; IEA:UniProt.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
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; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   NCBIfam; TIGR00604; rad3; 1.
DR   PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PCH02256.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT   DOMAIN          6..399
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
SQ   SEQUENCE   839 AA;  94310 MW;  411EC7665ACDF7EF CRC64;
     MTTLGPREKF HHPYTPYDIQ LQFMSSLYDC IEAGKVGIFE SPTGTGKSLS LICGALTWLR
     DHKRKEFLKS IDGLAADDDE PDWMVEYAKK ERTQALTQKW REKTDIVSPN TEDDSFFELD
     EYESDTETGK SVSITGFSDI EGLSASTVAL LDRFKGRVTS QKEKENDNEN QTRIYYCSRT
     HSQLSQFAQE LRRVNLPSSL PSPEKNVEGE KQEHADLEEV IKHLTLGSRK QLCINTRVSA
     LGNATAINER CMELQQSGVA ADKKCSYLPN KESEDVLLDF RDRILSTVQD IEDISQVGRQ
     LAICPYYAAR KVIDQCEIIT LPYPLLLQRS SREALELSLR DHVVIIDEAH NLMDAISNIH
     SVSVTLEQLR TSLFQLTTYA RKFQTRLKGK NRVYVTQVIR LVSALAENLQ LLSQKHKSSE
     AIVQYSDLIS GKGVDQINPY KLTRYLQESK LARKVDGYVE HANNQDGKVN SGKTTREKTT
     APVLFQVQSF ILTLMNPSDE GQLFLNKADG GVLLRYMLLD PTNHFRDIVD EARAVILAGG
     TMSPMSDYAD HLFSYVSPEK LDTFSFGHVI PPKNLTARIL AKGVLGSDFN FTFDQRNSDS
     MITDLGQTIA NLCAVIPDGV VAFFPSYDYL NQVLNTWRKP DKSGKGGSIF SAIEKYKPIV
     YESNNQKKES STDDILLEYS KKVESGSGAL LLSVVGGRLS EGINFSDKLG RGVLIVGLPF
     PNIHSAVWKA KIGRIEKQTY AKLTQNGTEL SMLRRREAET AAKAAGRDFF ENSCMRAVNQ
     CIGRAIRHRN DYAAIILIDR RYETQRIQGK LPAWIRQSLV SSATSNIRGD LTSFFKTHQ
//
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