ID A7ENF0_SCLS1 Unreviewed; 2003 AA.
AC A7ENF0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=WSC domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SS1G_06849 {ECO:0000313|EMBL:EDO04366.1};
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:EDO04366.1, 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}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; CH476628; EDO04366.1; -; Genomic_DNA.
DR RefSeq; XP_001592608.1; XM_001592558.1.
DR STRING; 665079.A7ENF0; -.
DR GeneID; 5488565; -.
DR KEGG; ssl:SS1G_06849; -.
DR InParanoid; A7ENF0; -.
DR OrthoDB; 2720860at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR013783; Ig-like_fold.
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 InterPro; IPR002889; WSC_carb-bd.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF01822; WSC; 3.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00321; WSC; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51212; WSC; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..2003
FT /note="WSC domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002705736"
FT DOMAIN 862..960
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 982..1076
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 1757..1809
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1795..1997
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1262..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2003 AA; 216991 MW; 3E5FEDE58F49C8D5 CRC64;
MLFSPPYIFV LLAEIFVNVL VHGLSSTDEY RDADLQQTGY LQVHTPFLQS DIGCTGTPII
DPATDIAYFF AKTYIPNYRV PGNTGTANGV YYFHAVNIST LLDVFPPILI DGAIADNAPQ
KYFIGGVILQ RPSLTQVGSV VYGSFGGHCD LFNYTGLVMG IDINKAKIIT NWAVESGPLV
PQTNVLLQGG GGGEGGIWMS GMGLATDGAR IFLVTGNGGA HQNQGTPASG SSGCQTLGEA
TINLALDNTG VISVSDYFQP YDYQNMDAGD QDFGSGGIVL LDRTVFKGTG VDKMAVTAGK
NGKIYILNAN NLGGYKLGPG QTDNILQTIV TNAAVFGACG SYPLEGGFIY CTPVGLATSV
YQLTFTSSGI PQFSKIGQTN EISAGRVGVG IPTITSFNNQ IGTAILWMTD PDAGLRAWYA
VPQNGVLQKI KIPQIGGANK FQRPAFGNGR VYTTDSNGVL YCLGAPVNLP LNCTSPVDFG
VVALGSKSVQ NISCTAIIAI TSINGATVGN GYFSVNNSTL PTGPLNAGAT FIFPVTWDLT
NVQVGATANT SFGNVSPGIK STPLTILTTN AVAGYATLYP ISLTGTEVSS KPFLAIAPTT
VDYGGIIITS TSNINPQSAI FTISNKGLMS MTITGYAYTA DELDDNPVFI NSTVINGTWD
LGFGYFTAVG LPAIGSQVAP SSQLSIQSSF DPTNGTGSYN SYWQVWSDGG SVNIILEGIA
STAPITNFSI SNGEGGWLPQ ANLFMDFGKV APGSSSSQQI RICNVGGSSL EISKSKPPNG
VFHISDPTEL HESQQIAVND CAYGTVIFSA NVEEYNKPDL LLNNTWTLNT DDVNWGVHVV
EITGTVISKK VGPINSTTGQ TIYNYLGCFQ ESTTGPRLLP NQGYTPNVTV NDNDMCQEAC
YGLAQYSFAG TEYTSQCWCG NTPPPLAAQD VTDALCNFAC PGDPNDACGG TGYISVFYNP
TEYVAGTDPA LYGPKTVSSV GNYNYLGCYS EGTNGRALAG SSPQAPPTGF TIELCAAGCK
GFTYFGMECY CGATINAGSV LQASTIPAVN GCDMLCAGNA SEYCGGSSRL NMYQLNGTVS
TPTPAPTGPI TVTNLTGWSY LGCYNESTTG RALSGLENPI PGVNNSVEAC SAACAAWNYF
GVEYGDECYC GNAINTGSTL QVVEKSLEVY LVKYEMHLFG NVIEYEQAKR LRSSEAFEAK
VSLSKVFGFN GTAQTPIKAE DSELEEIDAV VWTPYPRSKS TEKGLGQTEV KAEDSELEEI
DATVWSSSRA GSAAQTPRKR PRSHSVSVSV SGVKLEGNDV QLKIESSDSS SSDERRSVSK
RRKSFWGKSI PFDRRVPHRT TSPEFRHAAE LMDQTKSART PTPDDKNPHN GETEYERDLE
NSDFSDIEDD ETMPSVAPGP LPSQKRRTLE KSVKTSEEWY ARYHRKKVKF QKRRNHRTFA
NDGAASKIHN FLNHDPITAH KEKPAEEQIT NIEASSKRDY FDQVLRNIRT DGRMHNCRGD
NTALKIAGEG FGRVNVRYRN ENTWCLKGVK TALYHHQLLC ASWMLGREYD PDGPSGGFNC
DVMGLGKTLE MLATIVGSPR PEGAEISEIG PTLIVVPSSI QSAQWVSEIG KHLADRGLNV
ILYAKSQKLS KNTLIKSDLV VTSYDQMRMS SPFPPPWWLL DLAKKLKVKS CTLDGRQSIE
DWIDDNREQC GEVLHKINWY RVVLDEAVTC LQQPIGQTIV SSSDSIHRES LSYRATNKDS
GHHGPLIGNE VIDVHICEIC NQEADDPRQV RNYRKDRNGE KSCDHIFCEI CIEVSINAQV
ARTDNIECPA NGCGRKFNPD RMISLDSWST GPEEDTGMKK GRDRVGFLPR LSQGEMKSND
QAHILREFET NPKFTILIIG LKVGGVGLNL AFANRAIMVD LWWNAATESQ ANGRIFRIGQ
EKETNFARFM MRESVDIRLL RMQVEKSIVI VGTLESKTEL TYAEALSFLG EVQWTNDSRL
KIIDDHEKLE EWLDDWLNKQ KKV
//
