ID A0A1Y2LKL2_EPING Unreviewed; 863 AA.
AC A0A1Y2LKL2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=B5807_11126 {ECO:0000313|EMBL:OSS44365.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS44365.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS44365.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS44365.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(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}.
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DR EMBL; KZ107858; OSS44365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2LKL2; -.
DR STRING; 105696.A0A1Y2LKL2; -.
DR InParanoid; A0A1Y2LKL2; -.
DR OMA; QTHQFRD; -.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000193240; 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:UP000193240}.
FT DOMAIN 6..425
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 109..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 96103 MW; D7FA3A1F026F3988 CRC64;
MSNDNVARDF HHPYQPYDIQ IEFMNAVYDC LEDGKVGIFE SPTGTGKSLS LICGSLTWLR
DHKRRMFETG FDVDTKDSDD PPWMLEHARK QRKQEAFRHR QELNERLAKI KAKEQRAKDR
DTAETQIYKR QKINSSESNN RSDESQFALN DYESDQEAGR TEKFADSGLS AETQALMDKL
GYVHGGTKTE DGEVPDETKI FFCSRTHSQL TQFASEISRI KMPPSITSDE SVGDDNIDRC
IEDVKHLTLG SRKNLCINPK VSCLGNATAI NERCLELQQA RSSESRCSFM PTKDSEVLLN
EFRDHALAKI RDIEDLGTLG NKLGICPYYA SRPATKFCEI VTLPYPLLLQ RSAREVLGLS
LKDHIVIVDE AHNLMDAIAG IYSVSVTLAQ VEQARGQLTT YLQKFRNRLK GKNRVYVAQI
IRILDSIITY LQSIKSSSKA TDGLVDMVSI MSGKGVDQIN IFKLNAYLQD SKLARKVDGY
TAFAEDASVD PRDLKRKQEP HHTPRNTVPV LMHVQSFLLS LMNPSAEGRF FYSKEEEDGG
LSLRYMLLDP TYHFKDIVED ARAVVLAGGT MSPMSDYEHH LLPYLDSGKI QTLSCGHVIP
PSNLLAAPIT TGANGVEFDF TFEGRNKEST IVSLGQAIIS MAHKIPDGLV VFFPSHAYLD
TCIASWKQPS PQPSKQPTWA RLEQTKPIFL EQRSNQQSVT SSAAKEAAVD SVLTAYSAAV
VSGAGRGALL FAVIGGTLSE GINFSDALGR GVIVVGLPFP NPHSAEWKAK TQYITTKENA
RGADGKAAAK DYYENACMRA VNQCVGRAIR HKGDYAAILM LDKRYGGERI QRKLPKWIRG
SLLPGVGVQG AEKALERFFA VRR
//
