ID G2XXY1_BOTF4 Unreviewed; 1195 AA.
AC G2XXY1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Similar to transcription factor Cys6 {ECO:0000313|EMBL:CCD45318.1};
GN ORFNames=BofuT4_P120240.1 {ECO:0000313|EMBL:CCD45318.1};
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:CCD45318.1, 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 -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
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DR EMBL; FQ790277; CCD45318.1; -; Genomic_DNA.
DR AlphaFoldDB; G2XXY1; -.
DR STRING; 999810.G2XXY1; -.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_271367_0_0_1; -.
DR InParanoid; G2XXY1; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 2.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR11085:SF7; NAD-DEPENDENT HISTONE DEACETYLASE HST3; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02146; SIR2; 3.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 2.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 283..313
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT DOMAIN 542..893
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 100..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 697
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 705
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 731
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 734
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 1195 AA; 131863 MW; FABD68819D4B1B5B CRC64;
MPTINVLPTS AAELQEIADI LAKSRKVVVV TGAGISTNVG IPDFRSEHGL YSMIQAQYDA
ALENPPWEIN DYDIDDRPKK KRRVTERYYY ELVTADGVRV ELPPEESSEL PSQQPSEQSS
EQSSQQCSQS PSKEPSAQPE TPALAPSRRS SRRHIPLVRD NLKNESQRSS LVTATIDSNA
SSTNDNSINK SAILPPKRQT RNASSVQDNP IKESPKPSSQ GQPAHNLHDS LSQATPISKS
HMLPPKRQAS RSRTSLLAQD GIKIESPKPN IKGKSSKLRA IRACDRCRVR KIKCGDIRPS
CEPCAKSKVE CITTENPNRR VSQIEDTKLH EELNPSMEME LDSEGSNTEE NASQQLLQES
SEYSSQYSSE NSRLPQDLES IDNNKQKRTR RSLRISSPLP IAKEESSNAT RISSDSSLSN
SLRRESSLRS TIQASTTNQE SIHSQSRTLQ RSSSLIPSVA SSIIESKTSR QSMRSRADSL
PPPLTEQSSS LPRKTSRRNT PALELSNSKL SSTTNTESVS TTSSATPSVS SSDCSSNNNN
NNNSKRNLLS EVSSVTTASE FEEPPSQSSQ SSSRTLPNLK GKDLFDSVIW SDPFSTSIFY
MFISNFRRRI YNDVKSTTTT HQFIRSLRDN GRLVRNYTQN IDCLEEREGL TTDLELGAGD
RTRFQTKIQG KSLTAGTDER GGKETPPATG VECVLLHGSL RKLRCGVCSK LTSWDEEDRE
TTTMAGSAPD CPSCISSSIS RQDKGRRGLA VGRLRPDIVL YGEEHPHANL VGPLIIHDLK
LGPDVLLILG TSLRVHGLKI MVKEFAQAVH ARGGSVIFVN QTKPPESQWG DVIDYWVEWD
CDAWVLDLKK RRSDIWQPYT NVTQNASSKD PAPPKQRNPS DKIPPYRPQC KRDDKTNAVH
FTFKILDDLR KLKDAEGNGS ARPMYWVPFD RRPFRASTGQ IPENKPIKKS RSSVLPIRKG
RKSLPASSSI KVPTASTSSK SHRRKTIPDS TPAKTRPTEP HRSGAWLEDS LLKIVRRLTN
NTLSEDLLED LRGRVPFEQL AENVPGNSIG YKRSFSDVGI DGALEGVGLP NMRGLLDSSI
SIKGMSLSSL PPTGSPESGR KDLRKGKGKM IDIGERERAS SLLGPALEKD QNTIVVQSRQ
VQAIKHSYGT RSKRNSMEIS SEDIGVSGSG SGNAGDTIVV LNRDRMSIGA VCNDR
//
