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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