ID A0A395T0D2_9HYPO Unreviewed; 957 AA.
AC A0A395T0D2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305};
GN ORFNames=FLONG3_3682 {ECO:0000313|EMBL:RGP78203.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP78203.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP78203.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP78203.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00236}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGP78203.1}.
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DR EMBL; PXOG01000074; RGP78203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395T0D2; -.
DR STRING; 694270.A0A395T0D2; -.
DR Proteomes; UP000266234; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 2.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
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 SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000266234};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..600
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 67..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 105150 MW; D8A8EFF68294E4D6 CRC64;
MPTTHVSPES QDELKDIANG LLKARKVIVV TGAGISTNSG IPDFRSENGL YSLISAQFDA
ATQQARLLEN TDDKPSDVDT RPAPKRRRTL RHEFSKAEED LSETKDEIEV QLEDPEPVEE
KIADTIQVEG VPEDEEQPSD PDAVPLINPR TTRSTIAVAQ PPTSPLSSPP PEDFRITPPS
AFRRARQSHL NDSEIPPSSS PLSSPPPVLF EPFSSHASTE EGPDSRSSTS PSEVDDTPPS
LPQSLSQTSL GGKNTLPNMK GKDMFDASIW ADPLRTSVFY TFATTLRQKV RDVEPTSSHR
FISHLRDRGK LVRCYTQNID QIEEKVGLST CLTDGPGSRG RFSRKSTANL NQLNRMVDEV
NAMTEGNSDK SQQSSDNEAS QQSQPSQPRA DIVVASQAES DQGVSEDART AVQNLRRDLP
KSGVECVFLH GSLELLRCFL CGRVCSWDDD GRQLETMSGQ QPECPHCVGA TVAREERGKR
ALGVGKLRPD IVLYGEEHPN AHLISPIVTH DLALCPDLLL ILGTSLRVHG LKVMVREFAK
AVHAKGGKVV FVNYTKPPES SWGDVIDYWV QWDCDAWVSD LQEKIPKLWQ TPDPPKLKKK
RESGGTGEEG EKTDAKRSTA AYPVALRDTK AVAAYLVPRI MKDLHRITGH DPLEPREIVT
PIIVTAPAGT LPDPSPAGPL EPPSNKPVAV QKRARRSRKS APGALEKSKK PPSTLNPNHG
RTLRSAETVE PSKVEEPEVP FSHILRPERF LQESSIIDSV KGRVRKRRRI DGEEVELPSV
GRRQSSQKAA AAEIEGSLRL PPLNPQPPTP HNSPPFERLV PMEPPHCETP PKYYMNAQLQ
PVSPVAAPNP GPLTQVSHNT SRRVTRSQRS SMGLEESPAP FTTGFPPERS LGLYCSPQDS
YSLVMKPGLC QAESDTLAAL SMLKHGQVHE VVARDFVLPP QRGVRTRSSS RLRNEGV
//
