ID A0A3N4JMD5_9PEZI Unreviewed; 513 AA.
AC A0A3N4JMD5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=SIR2-domain-containing protein {ECO:0000313|EMBL:RPA99336.1};
GN ORFNames=L873DRAFT_1806870 {ECO:0000313|EMBL:RPA99336.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA99336.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPA99336.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPA99336.1,
RC ECO:0000313|Proteomes:UP000276215};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
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DR EMBL; ML120388; RPA99336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4JMD5; -.
DR STRING; 1336337.A0A3N4JMD5; -.
DR Proteomes; UP000276215; 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; 3.30.1600.10; 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:SF14; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-1; 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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000276215};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 157..466
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..59
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 513 AA; 56862 MW; 7212626B06884957 CRC64;
MATIPIAGAP NGAELPAHAA ESDEEEVLPI GGIEDELFEQ EDEEDNEDEE SGADEGEEWD
VSSVFDEWLA QSTDPVVFGP EEDAVTAEEG RNLRDLLRRV GEARFIDETL HTGTYTAKKL
LTAFGVRPPF FLEGSPDMAY LPFLGLVVTR DLRARQKLTE YNTLDDVVKL LKESSNIIVL
TGAGISTSLG IPDFRSKGSG LYSRLEGLGL SDPQEVFDLD VFREDPTIFY SIAGRIIPTI
DQISPTHAFI ELLQRKNKLL TQYTQNIDNL EIKAGINPEK LIQCHGSFAS ASCVQCGHKV
PGETIFPEML KGIVPECEAC LNRNANNGTS NNKVGKKRKR SKGSGSEKTS GDYRRKRYDE
SSDDDGGDDI PQAGVMKPDI IFFGEQLPAT FNKRLVDHDR SRCDLFICIG TSLKVAPVSE
IIGILPPHIP QIYISKTPVT HVNFDIELIG SCDDVVAELS RRAEWDLKHE MIPEDHDRIV
KVELEEGTVS RWIFERHGEE KKSVAEEEGA GEE
//
