ID A7EVX7_SCLS1 Unreviewed; 1054 AA.
AC A7EVX7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDN93619.1};
GN ORFNames=SS1G_09486 {ECO:0000313|EMBL:EDN93619.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN93619.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
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; CH476633; EDN93619.1; -; Genomic_DNA.
DR RefSeq; XP_001589764.1; XM_001589714.1.
DR AlphaFoldDB; A7EVX7; -.
DR STRING; 665079.A7EVX7; -.
DR EnsemblFungi; EDN93619; EDN93619; SS1G_09486.
DR GeneID; 5485811; -.
DR KEGG; ssl:SS1G_09486; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_8_1; -.
DR InParanoid; A7EVX7; -.
DR OMA; QSCNHPD; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45626:SF14; ATP-DEPENDENT DNA HELICASE (EUROFUNG); 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:0000256|ARBA:ARBA00022840};
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:UP000001312}.
FT DOMAIN 264..453
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 818..975
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..686
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..805
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1054 AA; 118164 MW; 2F06052DBF811341 CRC64;
MVREISPAKV QAPRPEEPKD QYRSSQSNAA NHLSNIPRFG EATLPQSPLN RKSQQQYSEL
FIQPKSRPEF HRDTEKHTHP HLQAAKDAAR KIIDPFMPRA PADYNKPAVR APVPGSSSYA
TTHPAPQPTF GSLPNSNGGF QSINTYTSNN YVDLTTSKPN YNETHIYVDP AKAQEDLKAL
LEGVIEDEED TKPRTRSRRK KKDAEVDDLM VQMNGLNVES DEKLEVASED EEEDDGTVEG
INVKLLPHQV EGLEWMIGRE IGTGKRGIVP KGGILADDMG LGKTLQSISL ILSNPKPSSS
DETRSKRKLP SGLDKCTLVV APLALIRQWE AEIKDKVESS HSLRVCVHHG PQRTKRFQDL
RKYDVVITTY QILVSEWGNS SKDDDDEGVK VGCFGIHWYR VILDEAHTIK NRNAKATQAC
YSLRSHYRWC LTGTPMQNNL DELQSLIKFL RIKPYDNLRE WKDQIDRPMK NGRGDVAIKR
LRHYLQIFMK RRTKEILKKE GALNPGGKPS VAGQANSTGF KVVERKIEKV FAEFSPEERK
FYERLEARTD ASIEEMMGGS KVNYASALVL LLRLRQACNH PKLVGNKLGK DTDALSAETS
NAKSKSTTDF DEMADMFGSL GVGSKKCEVC QIGLGKEAIS QGAIRCLDCE ADLDEISGKK
LSPKKKTKEE RSKKDKKHKA SKPVPIRKPR NRNIIEDSDD EEEGEWLVGD KKRGALTLGK
AGGKEDENCE GGGEWLDSDH DSDLDDSFPD IKDIGKKKVV SLDSDDEETA DESFEESEEE
DSEEDESSEE EEEETDVEDE FGSSDEEAEL SRVAASTKIT HLMKILGKEA AQHKFIVFSQ
FTSMLDLVEP FLRQKGFKYT RYDGGMKNDL REASLDRLRN DENCRVLLCS LKCGSLGLNL
TAATRVVILE PFWNPFVEEQ AIDRVHRLTQ KIDVVVYKIT IKDTVEERIL LLQEKKRELA
NQTIEGGKGG AGKLGMKEIL QLFRRDAEQA PPATGAYDLG AKPRILKESA SRSPSKSAAN
LNSYGSQTAS APRKIAPTPF QAKKIEDSVY GRRW
//
