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Database: UniProt/TrEMBL
Entry: A0C6J0_PARTE
LinkDB: A0C6J0_PARTE
Original site: A0C6J0_PARTE 
ID   A0C6J0_PARTE            Unreviewed;       449 AA.
AC   A0C6J0;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Chromosome undetermined scaffold_152, whole genome shotgun sequence {ECO:0000313|EMBL:CAK66407.1};
GN   ORFNames=GSPATT00035536001 {ECO:0000313|EMBL:CAK66407.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK66407.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK66407.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK66407.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; CT868044; CAK66407.1; -; Genomic_DNA.
DR   RefSeq; XP_001433804.1; XM_001433767.1.
DR   AlphaFoldDB; A0C6J0; -.
DR   STRING; 5888.A0C6J0; -.
DR   EnsemblProtists; CAK66407; CAK66407; GSPATT00035536001.
DR   GeneID; 5019589; -.
DR   KEGG; ptm:GSPATT00035536001; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; KOG2682; Eukaryota.
DR   HOGENOM; CLU_610401_0_0_1; -.
DR   InParanoid; A0C6J0; -.
DR   OMA; DHSFWCY; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR   GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR11085:SF10; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-2; 1.
DR   PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02146; SIR2; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00236};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT   DOMAIN          61..166
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          190..449
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   ACT_SITE        321
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   449 AA;  51108 MW;  3016848CAC04557E CRC64;
     MQLNPNHPFI FYQTIPILVY KYLINQNNYY IIQIANMDQG ADGFQIVLDG GQVGYAVQPK
     EDCPHFQQQD LHELMKFTEQ HRNTLFSQPC VQCGDASENW VCMHCREIHC SRFVNSHMVE
     HNKKSGHQIV LSLTDLSFWC YDCSSYITNY LISKASKLLS SIKFNNQEDK KDETQEIKQL
     IEQISNLKVT NEDEFTYAKL VDGLKNKKFQ RVCVLAGAGM SVAAGIPDFR TPGTGLYSQI
     QKYNLPSPES VFEIEYFKKN PEAFYCVAKE FLLSFDAKPT LAHKFLKFLD SRGQLLKCFT
     QNIDGLELDA GVSQDKVIQA HGHMRTARCI ECQEEVSIKD FMSHIKKGDI HRCEKCPKKG
     LVKPDVVFFG EGLPGEFFYS WNCLKDADLL IVIGTSLKVM PFAASVAKVG PTTPIILINR
     ENVLNGRKNL LHLDGDIEEN CKKLLQDTN
//
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