ID A0A3E2HJD1_SCYLI Unreviewed; 969 AA.
AC A0A3E2HJD1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305};
DE Flags: Fragment;
GN ORFNames=B7463_g2790 {ECO:0000313|EMBL:RFU33517.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU33517.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU33517.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU33517.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
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:RFU33517.1}.
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DR EMBL; NCSJ02000034; RFU33517.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2HJD1; -.
DR OMA; FDSMIWS; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 8..659
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 89..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 501
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 509
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 535
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU33517.1"
FT NON_TER 969
FT /evidence="ECO:0000313|EMBL:RFU33517.1"
SQ SEQUENCE 969 AA; 106940 MW; A4E2200F3F2369B2 CRC64;
MPTVNVGPGS LPELQEIANI LAGSKKVVVI TGAGISTNCG IPDFRSENGL YSLIQAQYDT
VMKQAQITED FEQPPVKRRR VCERWTYVPM PCSDTDESTR SSPDPPQRSL KSRASSVEPH
ENKSSEALVV SKAPAKLPQP VQRRSLRSSL GIKLAEKNIT PGMPKASPFT EKQHLTRRHS
LRSAGSAQLF EDNTLHTSKE RASSEERKPT QRRGLRSRAN SEQLLKGIST TQGAKTKRTT
DNSQREQSRN QRSETTVINQ TKNKTSTVIE QERLDKPHNS SRRSLRLGAT SLPEHDSLLT
TLSTETELGH TQEPQQSFES NTIVAETKPD NSHITTEYSA ADTITSIPPP HLQKESSAAS
SSGNDEPSST QSSQSSQPSS RSSLPNLKGR DLFDSMIWSN ALTTSIFYMF ISTLREKIKH
DVKTTTDTHK FIKALRDGGR LVRNYTQNID ALEAREGLCT ELARGPGNRA RFSSKAQREP
RPADVSGGAT HDGGVEVVML HGSLVRLRCS ICGKLSSWDE ADRQSTTSAG QAPDCPLCSE
NSAKREGRGR RRVAIGRLRP DIVLYGEQHP DEQLVGSLIT HDLSLGPDVL LILGTSLRVH
SLKVMVREFA KAVHVRGGKV IFVNHTKPPE SIWGDVIDYW VQWDCDAWVL DLKERRKXEP
KEKPEPKNPA AVRDDKHNGV YLTFKALDAL AKVKDAEGNV ATRPSYYTKK PSENPTIPAF
NGNSTIQVVL PAHDPKLSAF ETIANSKKRP YRPNATRDDK KNGAYLVSTI IQSLRKILAS
PCSTTRPPLE LRSHNLPPFP LRSRSRPHER SKSPSYIPII QGLGWPLEKM SLATHPPSGY
STPRTKPYRI PSYSSSHSLS DPASSSSPPQ TDHWPSDTIV VAGSPNSQDA IVVDVPGETQ
DAIVVAVPSG LHRRHQQQQE QQLPSPRDSS DSMTPKSQRI KHIGSISCIL SSPFSHAGNK
DYTVHNNTE
//
