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Database: UniProt
Entry: A0A151GDI7_9HYPO
LinkDB: A0A151GDI7_9HYPO
Original site: A0A151GDI7_9HYPO 
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
//
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