ID   A0A1J9SCU0_9PEZI        Unreviewed;       618 AA.
AC   A0A1J9SCU0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Sir2 family histone deacetylase hst4 {ECO:0000313|EMBL:OJD37668.1};
GN   ORFNames=BKCO1_600048 {ECO:0000313|EMBL:OJD37668.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD37668.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD37668.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD37668.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJD37668.1}.
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DR   EMBL; MNUE01000006; OJD37668.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9SCU0; -.
DR   STRING; 236234.A0A1J9SCU0; -.
DR   OrthoDB; 1327719at2759; -.
DR   Proteomes; UP000183809; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR   InterPro; IPR026590; Ssirtuin_cat_dom.
DR   PANTHER; PTHR11085:SF6; NAD-DEPENDENT HISTONE DEACETYLASE HST4; 1.
DR   PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02146; SIR2; 1.
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:UP000183809};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          89..401
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..43
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..505
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  67558 MW;  24AED991C63EBFA4 CRC64;
     MAVDAYCAGC SRESSPLSSP PSSPCPPSDY EYPSPPPSQD PSTKGSPLPD AMEPARACDD
     DGPPRKKRRT AEPKPRVTRH LNLQEDAIDE TEREALDLLL KVLHKKRKIV MIVGAGISVA
     AGIPDFRSSK GLFNTLKQQH NLKSSGKDLF DASVYRDPDT TATFHEMVRS LSHQAKLARP
     TAFHQLIATL ADEGRLLRLY SQNVDGIETS LQPLATQIPL PQKGPWPKTV LLHGGLEKMV
     CAKCNDVTDF EPELFHGPIP PPCKTCEEAD QVRTLHAGKR SHGIGLLRPR MVLYNENGPD
     DEAIGSVTTA DLRARPDAVI VVGTTLKVPG VRRITREMVN TVRDRKDGLT VWINNEPEPK
     GVDLENCWDL VVRGPCDAVA RQAALRIWND RSETMAKFLT EEEYRASKEK PSPEVRILSS
     PRKDRVLQVK GIPTPASSPK IQPQDPPIED EITVASRPST PPKKATTQSK GKGKNLSNVP
     LAERPKPKST SVKTAPKKKA APKKKSNASA KPNDKITNAF SVSKPAAQNV PELKSKPQRR
     GRKTDTANGP MAPVSPQSAK NNTAPPHNDP HTPKTLSLET KQIKAESNAE VATERGGSPK
     EVITPTGYLP KDMKRLLH
//