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Database: UniProt
Entry: G2Y1G6_BOTF4
LinkDB: G2Y1G6_BOTF4
Original site: G2Y1G6_BOTF4 
ID   G2Y1G6_BOTF4            Unreviewed;      1505 AA.
AC   G2Y1G6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Snf2 family helicase protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BofuT4_P041170.1 {ECO:0000313|EMBL:CCD46506.1};
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:CCD46506.1, 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; FQ790282; CCD46506.1; -; Genomic_DNA.
DR   STRING; 999810.G2Y1G6; -.
DR   eggNOG; KOG0298; Eukaryota.
DR   HOGENOM; CLU_001592_2_0_1; -.
DR   InParanoid; G2Y1G6; -.
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   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd18070; DEXQc_SHPRH; 1.
DR   CDD; cd16449; RING-HC; 1.
DR   CDD; cd18793; SF2_C_SNF; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR   PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          351..552
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1156..1194
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          65..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1213..1236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..796
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1505 AA;  170333 MW;  84D6C610B494BCB3 CRC64;
     MAPVKPEWEQ DFAIIPEGSI FAPELEAQRT DNAKDNVPLE KAPSVFVADV TDALINYLTA
     DQNASEEPLT KRQKLTTGSR LESSSGHVSQ DYITVKQTAL EVRCLRSKLP LDCTTLNRQK
     IHFTSHWGRQ GGSTKPSNII LRDDNNNSLL TIPLSLEHAS MSIQDSFDDV LICLMVDRDS
     KRRTQQSSKL WTEAGISVYK TDESDYIRID FTIKWEITTN PTSIQPKKTD ALLKVLNTYF
     PNPNITSLKP LSAQDFYQSA HSPDPDDEIA ASIETPGLES TLYPFQKRAV QWMLRREGFE
     WSRATGCIER AQSKAIGRTP PSFFAVKDLQ GRSCYVSHLF AIVTFDLAAF FWVDQEIKGG
     ILAEEMGLGK TVEMIALMTL HTRHDQDPSI FDPFSGETLQ TTHATLIISP PSISKQWIDE
     IKTHAPKLKV TYYEGIKSRK LQYETTMNDF VTSDIVITTY SILTSEIHFT SLNPERTTLR
     SKSKYQRLKS PLMKFSWWRV CLDEAQMVES GVGKAATVAK MIPRINAWAI TGTPVRKNIN
     DLLGLLIFLK YELLVSVWRS LVYSKQDFHK LFGAISLRHS KQKVRGELIL PKQHRFVITL
     SFNPIEEQFY QEMFGKMCEE SGLDTEGEPL MDGWDPKVYA EVMRRWLVRL RQATNALPPK
     RSTRRKRIGD EPMVQTASKA LELMFSQTDV AIRANSRSLL LSQLKRGQLF EDSPRVQEAL
     DIWKECVTVS STFVDQARDE LSTEILSEKA RLAFHSESSS NSMIAETQGT IVPSKSQSIE
     GNGEKDLEAQ DGSDPDSRVV MSRARLRASL ELHHMGLFFL SNAYFQIKSN EEMTAVNSAE
     FENLDMLERQ GYEEAKELRR EILQDAFKRT DTMMSAIRRD TESSSAVQLP QFIPSTLKGG
     SESRRIMEEF EKLGINLDRQ AHQINEWRNH LIQILLSPLV DNDDEDIAIS GDEYENSIKV
     QEEVVVYVQA LRTMIADRQS SLSGVQNYLI DEEAKTAFRE AKHGKGPFPE KLIALFNIRA
     LFLHKIISVR GTLSELRTLI SKLKTNHSQN ELSIVEAQLK LAHNYLTDQT KAATNLEKEI
     GLFTKCMNLR VEYYKQLQAI SNQVAPYTGP NNDGVNQSFL RKEHALNQNI ASLRAKRRYL
     VHLKEEVENP KDKRTCVVCR EGFDLGVLTV CGHQYCSDCA KEWWKLSHRC PICKEMLIYE
     ELHNISYKPH EPTLTTEAEG TREPLKERSL NSNSPQKSAI YSDVSKATLS AIKNIELQDN
     KSFGTKIDTL ARHILYLRES DPGSKSIVFS QFTEFLPVLA SAFDAFRIGH SSIDRPNGVE
     KFKNDPGIEV FLLHSRAHSA GLTLVNASNI FFCEPLLNTA IALQGESRVH RIGQKFETNI
     WVMVMGNTVD QSIYELSFKR RLDHLGHTTM SKKGKERAVS DEELVTQALE EADSLEMQQS
     VPRNLLLKGH DGEAVSENDL WTCLFGGRTK RTTVNLIDGG SSDFLVEIEK SSGASTINES
     IANDA
//
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