ID A0A395P110_TRIAR Unreviewed; 956 AA.
AC A0A395P110;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Sir2 family {ECO:0000313|EMBL:RFU82045.1};
GN ORFNames=TARUN_125 {ECO:0000313|EMBL:RFU82045.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU82045.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU82045.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU82045.1,
RC ECO:0000313|Proteomes:UP000266272};
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:RFU82045.1}.
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DR EMBL; PXOA01000010; RFU82045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395P110; -.
DR STRING; 490622.A0A395P110; -.
DR Proteomes; UP000266272; 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:UP000266272};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..602
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 59..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 104142 MW; 6FE9F32E82AEC6B2 CRC64;
MPTQHVEPES HSLLQDVANA LLKARKVVVV TGAGISTNSG IPDFRSENGL YSLIQAQFDA
ASQQTRSTER SKTDGAGAGD GGGEEDRPTK RRKISRESSP DPDEVSRQLN EDIEARAESE
ASASSSKETD TQQTEPASGL NASKEACLST PISKPTLPST PQQTTSPTSS PPREEFMLPP
SSLRAADRKR IADISHNVTS SPLSSPPPVL FDPFHPSSPS DENMSRRSST TPSEVDEAHD
APNAISASQA SNVGKTSLPN MKGKDLFDAS VWSDPTRTSV FYQFATSLRQ KVRDAEPTSS
HKFISHLRDR GKLVRCYTQN IDQIEEKVGL STSLLAGPGS RGRFSRKSTA NATQLSKMVE
EVVSSGESGA GDVGMSSQSS NGSSEQTPTN APDQRQASAA SSQPNGKTEE DETATPPDQH
KPAPRKEAPA LRSGVECVFL HGSLQLLRCF LCGQVCSWDD DDREVETLSG QQPECPHCVG
ATEARQERGK RALGVGKLRP DIVLYGEEHP NAHLISPIVT HDLALYPDML LILGTSLRVH
GLKVMVREFA KTVHSKGGRV VFVNFTKPPE SSWGDIIDYW IQWDCDAWVT DLQIRVPKLW
QDPEPPKPKK KRESGGAAEE NREEKKKPPA QNPVALRDTK VNGAYCTLKI LKELRRITGS
SPPPPASLPL PLPLRRASVA ATTDPDLPAP VEAVLEAAVM DPPRISTPRT KPKRARKSAP
GALDRPKRTP STLNPNHGRN KKPVEEVKQE VPETPSQPPS VNTVEEFSSI LHSVKSNPRI
RKRKIIDGEE FVFPAVGKKR AALDSLYKGS DEDKKKLPPL RPMPEQAPTL ATSPSEPEGS
EEEPLASISI NLRAATTFTR PEAFYIQDPL VTLLEKAPQW KALEMNHGEL KRTRRRVSKR
FRPVEIESKA QAEANAALAL AGLKTNSPMV AQVAHAVPGN GYTELTNWAA NWNCKK
//
