ID A9V9J9_MONBE Unreviewed; 489 AA.
AC A9V9J9;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Regulatory protein SIR2 homolog 7 {ECO:0000256|ARBA:ARBA00043038};
DE AltName: Full=SIR2-like protein 7 {ECO:0000256|ARBA:ARBA00041832};
GN ORFNames=MONBRDRAFT_28831 {ECO:0000313|EMBL:EDQ85877.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ85877.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ85877.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC {ECO:0000256|ARBA:ARBA00038170}.
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DR EMBL; CH991570; EDQ85877.1; -; Genomic_DNA.
DR RefSeq; XP_001749356.1; XM_001749304.1.
DR AlphaFoldDB; A9V9J9; -.
DR STRING; 81824.A9V9J9; -.
DR EnsemblProtists; EDQ85877; EDQ85877; MONBRDRAFT_28831.
DR GeneID; 5894652; -.
DR KEGG; mbr:MONBRDRAFT_28831; -.
DR eggNOG; KOG1905; Eukaryota.
DR InParanoid; A9V9J9; -.
DR OMA; CMEHEGS; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 2.20.28.200; -; 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; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085:SF1; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-7; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 164..423
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 489 AA; 53883 MW; 64801AD233085E34 CRC64;
MAAAVSAMAA ATEVEAESKQ GVEQEGKRSK QVADQEIEQE IKQEIEQELK QEVEQEGSKE
MSQGESKERS EEESKERSEE DKVAEIESMR ARRAAERRKQ LQEKRIKLAN ETRMRRLAAR
PESSWSSDDA TFVEANPELM ALMRQRHSRR RQREDREAEA TDDPETLRHK ATKVATLLQQ
ARTAVVYTGA GLSTASGIPC YRGQHGIYTK TAKNSTADTT VAPTPAPTTL DLTACSPTRA
HQALTALVQG GVVQHVVSQN VDGLHRRSGL SPQHLSEIHG NAFLEYCPVC SNNGVQASGL
YARRFDVTGL TARHRHATGR NCPACATPLL DTIVHYGEAA HCSPVHNWEG IEALLPQVDL
ILVLGSSLKV LKHYKPLWQP LQKKASLIVV NLQWTPLDAR AALVVRATCD AFLEALLNAL
PTARRPAVPD YDMGHDALWA MAVPLTPAED QAAKEPASQI SLREGWFAKG VTGGQRRAKR
VKEELEALT
//
