ID A0A1V6XU80_PENNA Unreviewed; 853 AA.
AC A0A1V6XU80;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 26.
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=PENNAL_c0054G04264 {ECO:0000313|EMBL:OQE78703.1};
OS Penicillium nalgiovense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE78703.1, ECO:0000313|Proteomes:UP000191691};
RN [1] {ECO:0000313|Proteomes:UP000191691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(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:OQE78703.1}.
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DR EMBL; MOOB01000054; OQE78703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6XU80; -.
DR STRING; 60175.A0A1V6XU80; -.
DR OMA; QTHQFRD; -.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000191691; 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};
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:UP000191691}.
FT DOMAIN 1..421
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 106..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 853 AA; 95912 MW; 356344240872DEC6 CRC64;
MDFHHPYTPY DIQLQFMQAL YACLEDSKIA VFESPTGTGK SLSLICGSLT WLRDHKRKAF
QETVDATCDD DEPEWMIEHA KRESRRAITE KRQEFEARLA KIRQEEERLK QAQDSADRPR
KKLRRDDSAP ELVEDDDQFV LDDYDSDTEH QKKQNDSGNS DGLSASTLAL LERFQGKFST
KKDKEDDGDD EIKIFFCSRT HSQLSQFAGE LRRVNFPSSI PSDLDPESKN DLSKLEERVK
HLSLGSRKNL CINPKVRALE NNTAINEKCL DLQQASVAAD KKCSFIPTKD DEALALEFRD
HALATVKDIE DIAEVGKKLG ICPYYASRPV IKHSEIVTLP YPLLLQRSAR EALNLSVKGH
IVIIDEAHNL MDAIAGIHSV TVSLSQLQTA IGQLTTYARK FKSRLKGKNR NYVAQVIRLV
SSIAEHMKSI SQQKGPLEGS VQTSALMAGK GVDQINPYKL SRYLQESKLA RKVDGYLESS
QQPQPGRSKD KTTMPVLFHI QSFLLPLMNP SEEGRLFFQK SQDDVLLKYM LLDPTNHFRE
IAEDARAVIL AGGTMSPMSD YVNHLFSYLP PERLGTFSYG HVIPKSNLVA QSLTQGLMGN
EFDFTYEARN SEKMVTDLGR TIATLCQVTP DGVVAFFPSY DYLSHVLSVW KKPIPNGNGQ
STLNLLERNK KILYESREAV TTTDDLLQEY TEAVESGSGA LLLSIVGGKL SEGINFSDKL
GRGVFIIGLP FPNIRSAVWQ AKIQYLEEKT YKQASGSETE RKAAGKAAGR DFYENSCMRA
VNQCIGRAIR HMNDYAAIIM IDRRYESPRI QQKLPGWIRG SLVPAPPTRA AQITVQRLSK
FFAEKKAIAG YNL
//
