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Database: UniProt
Entry: G2XNU1_BOTF4
LinkDB: G2XNU1_BOTF4
Original site: G2XNU1_BOTF4 
ID   G2XNU1_BOTF4            Unreviewed;       885 AA.
AC   G2XNU1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|PROSITE:PS51192};
GN   ORFNames=BofuT4_P076300.1 {ECO:0000313|EMBL:CCD42547.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD42547.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; FQ790246; CCD42547.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2XNU1; -.
DR   STRING; 999810.G2XNU1; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_0_1; -.
DR   InParanoid; G2XNU1; -.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177}.
FT   DOMAIN          675..866
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          63..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   885 AA;  96478 MW;  015E040809955591 CRC64;
     MSQQSSAPAD SLAAIATLTD EITLQQVYLV SLNDSSGDQS ARKAEIEAEI AILRKELSAI
     QASSSHAQAS STSHDNSYTR PSDIGRSKMN STVARGSNAG YQFKEEGEPA GSLSSTASTP
     GSGASMFGSG SHRADLPTRK RTLSKHLDMF VPFEEVKSRR TTPSPFATGV TTPSGSSGYG
     YNANGDGYFD LTMDDDIVMF DPAFTERQKQ EEQKFQRERK DAEFASSLAE SSIPVSNTPM
     ANSKPSAFHR MYGGHSGGLS QASTSRNIQA AKSSVIPNTR DTHNSDSSSR SLPWKKGSSS
     SLKAEPRTSS HTQPSPSGFI GWGSGDTTDK GEPRTLFYTQ PSPPGFVDWG SDGTTGVHRE
     QSFTSMNSNS MPGAYIDDAA SDSSLEIIDS SAFKDNGRQK ATVSKTSNYY SQPGPIYSSE
     TRVLGDIAVG RTNTSLQGDP ASSNWAKKSP NGMENPSGNI SDASTWMIGS YDGGMNNESR
     VEEQNSYSTP WEEDQLFAPY NGMNAGYKDF SMSGTSSAMS YNDTNPSGAY LFDYSNSTMP
     LTVPGSITGS VHSSHPQTSM HGPGSAFSID SLSEHGMGST NFNSLRGTIN NARNFSDVES
     NLSFLPTPFA YTPQMTERME HVINDPRKTE KEIKDLLENI KAEIEIPLED REGTPEGLRY
     PLYEHQKIAL TWLKQMEEGS NKGGILADDM GLGKTISTLS LILSRPSTDH ARKTTLIAAP
     VALLRQWNSE IASKTLPTHK PSVYMAHGNS KRATWDDLRE YDVVLTTYGT LGAEYTRLVK
     FEEESKRNGI TNHDPKQMAK DFPFLGPNSR FYRVILDEAQ CIKNKTTKAA ASAYRLTALT
     RFCLTGTPMM NNITELYSLI KFLRIRPYSS WTSFVKVCIS GIPYF
//
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