ID   A0A1L7XRT7_9HELO        Unreviewed;       964 AA.
AC   A0A1L7XRT7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305};
GN   ORFNames=PAC_17675 {ECO:0000313|EMBL:CZR67776.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR67776.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR67776.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR67776.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-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}.
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DR   EMBL; FJOG01000047; CZR67776.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7XRT7; -.
DR   STRING; 576137.A0A1L7XRT7; -.
DR   OrthoDB; 1344271at2759; -.
DR   Proteomes; UP000184330; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00296; SIR2; 1.
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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184330};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..648
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          101..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          847..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..765
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   964 AA;  106480 MW;  86A544B774F3A43B CRC64;
     MPTIKVGPGS DLELQQIADA LGKSKKVVVV TGAGISTNCG IPDFRSENGL YSMIQAQYDA
     ALLNPPWEQS NTFDIDDRPK KKRKTWFYEV VAPDGKVVDV IDPDLEPAEQ QTRRSSRSRS
     TNTTNSRSNT PQPTETPALA PGTQAVDAIS VEIHSAKEEP LISSTSAATP YSRRATPTTA
     PDRESSVINK KLAAAKEAPR RSSRSRSMNP AKSRAGSPRT TAEGQSNTDD EGLRLIDQGT
     RQSSLARSTD TNDTRASTPL SAIESQEVDT FDEHPETVNN EPRPSSRSRS TNTTNSRSST
     PKSIESSLTS LSSNTPELPD STPQNSSELS LNADQSTLSQ TSENLEPSTQ PSTSRSTGLS
     RTTSDVSTSR TLPNLKGRDL FDSMIWSDPF TTSIFYMFIS SLREKIQNVS YTTETHRFLR
     VLRDGGKLVR NYTQNIDMLE QREGLCQELE KGPGAKGRFN ARAQREARKS GIGADIDQNG
     GCEVVPLHGS LQWLRCSLCG KPSSWDEPAN KSAMLSGTAP DCGPCTTNSG NRTSRGRRGL
     AIGRLRPDIV LYGEEHPHSN LISPIVTHDL GLGPDILLIM GTSLRVHGLK VMIREFAKAV
     HTKGGKVVFV NQTKPSESIW GEFIDYWVEW DCDEWVMDLR DRREDIWTGV VEENTKETTE
     TTKRRRPQAL RDDKLNGAYL TFKILDTLSR VRDESGGMAS RFLYWPAPAS RVSNISLPDR
     EQQTKAPVKK GQSTKKNSKS APIKKTGAKP NKRKSEPEPY KETEEDRKNL AYIVSKIWED
     LRKKAPDLSA IPPPPPELRI PFSKFTSNKA LPDYLTPFAF SSTSNHIPNV GTWPLDKMNL
     VSLPPSGSTI PIHTPKSKPK TEEKPKPQPR PNHGYGTRAS RRFSSAETIV VDRGETDVQM
     EQELPAQQEP MVQLGEEQEQ EDTIVAKSED PMTPVSSRIK RNCSIGALVS SSPEQWHDAM
     EVVS
//