ID A0A151GDI7_9HYPO Unreviewed; 1045 AA.
AC A0A151GDI7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=SNF2 family helicase/ATPase {ECO:0000313|EMBL:KYK55156.1};
GN ORFNames=DCS_07118 {ECO:0000313|EMBL:KYK55156.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK55156.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK55156.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK55156.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KYK55156.1}.
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DR EMBL; LAYC01000003; KYK55156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GDI7; -.
DR STRING; 98403.A0A151GDI7; -.
DR InParanoid; A0A151GDI7; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000076580; Chromosome 03.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45626:SF16; SNF2 DOMAIN-CONTAINING PROTEIN / HELICASE DOMAIN-CONTAINING PROTEIN / ZINC FINGER PROTEIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:KYK55156.1};
KW Helicase {ECO:0000313|EMBL:KYK55156.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000313|EMBL:KYK55156.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076580}.
FT DOMAIN 227..412
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 832..995
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..638
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..818
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 116665 MW; 02B9126D05E20D48 CRC64;
MVNERAPPNL SLQTAERAKD GKPARERSPD DDDIASLIKG FASIKSKFRE PTSGPLSRSA
FGHPTKMMSS LKQKANVFIQ QKSRPEHHLG TKISGPRPPS YHDRKAPPIP TFNSNMPLKT
PLSGGGEEEV FYTDPKKAND DLKALLEGGL DEDDDEGDIE PQPGQRDLKQ DVPTKADKQD
TRAPPTSQQK KGFRVGKDGH VPGLNVKLLP HQVEGVNWMR GRELGPVKRG KVPKGGLLAD
DMGLGKTLQT VSLILTHQKP LEGEEGWDKR FEGISKTTLV VAPLALIRQW ENEIKSRVEK
AHGLKVLVHH GPQRTKNFKE LTSYDVVITT YQILVSEFGS SSSAANGLKA GCFGLHWWRV
VLDEAHTIKN RNAKSTKSCY ALRSEYRWCL SGTPMQNNLD ELQSLVRFLR IAPYDDLKQW
KEHIDVPLKN GKGHVAIRRL HSILRCFMKR RTKEILKVDG ALNPGGKPTA EGESSATGFR
HTKRNVVTIS TELPPAERKF YDRVEARADK SMEAMMRDKI SYANAFTLLL RLRQVCNHPK
LVEGKLEKDK DALSIGSSQR TADADMDAMA DMFSGMGIVS KNCSICGRIL SNVDVDLGRD
NCTECHEDLE YFKNEKVPER KRTKRKHRAK KGKGKKGCKK AEKVGPKVEA EREKGPVGRR
PRNRNAIIDS DDDEGDEGSW LVSKKEQGEL RLGKAGGEED ENAEGGGDWI GSEDSADDTT
DDKDQSNLSG FVVDDEVAKK EDGYRSAGED EDDNSLLSVS ALTKQMASQT LDDKPTEAKD
FATGSGSTLD AGDSDDGSDS SNDETELYST SDDDDDDDYA AAKNQQVLAS AKIRELIKIL
QAEVREHKFI VFSQFTSMLD LVEPFMRKEG FTFTRYDGSM KNDEREESLR RLREDKTVRV
LLCSLKCGSL GLNLTAATRV IIVEPFWNPF VEEQAIDRVH RLTQTVDVTV YKLTVANTVE
ERILELQEKK RLLAEQTIEG GSKKDALKLG INEIVELFKP GGYQHDSMPG EYGFAADERR
RAMQGMNVLR MKAPRKEDAV YGRRW
//