SIR2B_PLAF7
ID SIR2B_PLAF7 Reviewed; 1304 AA.
AC Q8IKW2; A0A144A2E0;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=NAD-dependent protein deacetylase Sir2B;
DE Short=PfSir2B {ECO:0000303|PubMed:19402747};
DE EC=2.3.1.286 {ECO:0000255|PROSITE-ProRule:PRU00236};
DE AltName: Full=Regulatory protein SIR2 homolog B;
DE AltName: Full=SIR2-like protein B;
GN Name=Sir2B {ECO:0000303|PubMed:19402747};
GN ORFNames=PF14_0489, PF3D7_1451400;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP FUNCTION IN VAR GENE REPRESSION.
RX PubMed=19402747; DOI=10.1371/journal.pbio.1000084;
RA Tonkin C.J., Carret C.K., Duraisingh M.T., Voss T.S., Ralph S.A.,
RA Hommel M., Duffy M.F., Silva L.M., Scherf A., Ivens A., Speed T.P.,
RA Beeson J.G., Cowman A.F.;
RT "Sir2 paralogues cooperate to regulate virulence genes and antigenic
RT variation in Plasmodium falciparum.";
RL PLoS Biol. 7:E84-E84(2009).
CC -!- FUNCTION: Regulates the expression of the surface antigen-coding var
CC genes central to the malaria pathogenesis. Cooperates with Sir2A to
CC mediate silencing and mutual exclusive expression of only 1 of the 60
CC subtelomeric var genes at a time, coding for functionally different but
CC epitopically variant versions of the erythrocyte membrane protein 1
CC (PfEMP1) molecule, to evade the detection by host immune surveillance.
CC {ECO:0000269|PubMed:19402747}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9NXA8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NXA8};
CC -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC {ECO:0000305}.
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DR EMBL; LN999946; CZU00209.1; -; Genomic_DNA.
DR RefSeq; XP_001348663.1; XM_001348627.1.
DR AlphaFoldDB; Q8IKW2; -.
DR SMR; Q8IKW2; -.
DR STRING; 5833.PF14_0489; -.
DR PRIDE; Q8IKW2; -.
DR EnsemblProtists; CZU00209; CZU00209; PF3D7_1451400.
DR GeneID; 812071; -.
DR KEGG; pfa:PF3D7_1451400; -.
DR VEuPathDB; PlasmoDB:PF3D7_1451400; -.
DR HOGENOM; CLU_267116_0_0_1; -.
DR InParanoid; Q8IKW2; -.
DR OMA; SEYIVVH; -.
DR PhylomeDB; Q8IKW2; -.
DR Proteomes; UP000001450; Chromosome 14.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070932; P:histone H3 deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:GeneDB.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 2.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 1: Evidence at protein level;
KW Metal-binding; NAD; Reference proteome; Transferase; Zinc.
FT CHAIN 1..1304
FT /note="NAD-dependent protein deacetylase Sir2B"
FT /id="PRO_0000417367"
FT DOMAIN 36..433
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 545..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 53..72
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 274..277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 371..373
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 399..401
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 417
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
SQ SEQUENCE 1304 AA; 154720 MW; 9E368BB10D0915B3 CRC64;
MSCMNYASRL SKNEYKGPLG EEEFFEDTEE EKKKVKELIE KIRSSEYIVV HSGAGISTSS
GLQDFRGPTG IWTNEHLNEL KNKKKRNHDF KDNKRKLKSN DINCKNTSDM CSPSFFHKEK
KENTLNIVKR ERYYNEDNVD MNACNERVVH PNHVYVNHED DNNNNNNNNN NDNNLYNNVY
NSVGSNDHTN KESILIKKEN NSENVRKDIH DKVNTKNVKK IDVKETNNLD PENYVIFGKR
KKKVIELHLA LPSKTHIMIN ELINKNIIKF MITQNIDSLH HRCGKHFSKT AEIHGNIFTE
RCDFCGRRYL RDYLISTISF KPTGSLCFLC SFPPIGVCTD VLLDWNNSYE EFFHLNSIKH
SQIADFHFCL GSSFYIVPAS SYPSKKKYAN ANSYSCVINY QKSFLSKEVN LNIHSNVNNI
SDIIIKEFSL NPLSIRSARI TIVRCPINTL DVICDKLISI HNIKMKHKSM RQHSIDYSQM
GNKDEKYNNE KYVKRNMTEC LYYNKEGECY EKRKYKLMEK KFFPNNQQNE FIPNRINIFE
QKFHEHNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN SSSSIDSSCS INSNYHISKN
INPDFSFVEN QSNIYENYKE QTFILICPMI INIKTVRLES FHKVYIKLLD DIKGLWFIKT
NFSCILEVEL WYHSFILLKL DFNKSDPFIQ LNAWNVNVAY TYGDDIDDFD YFKNDENIKK
PFNLYKNKYI SNMRREGHVN NLYTLDNEKV KSNTSNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNDNNN NNISDHNIYD DHNNNNNKNH NNYDKDNSNE SYYCSEILNE
HVHVGYNPNN YEPNCKVYIL AYLDNLRTRN INNNVNNNNF SRFNLTQSCK LLYNIYCVLN
KDNEQKKNST IKETYDKLDY FIKNFDFNRD SCLYTNNFIN MLIQNERHGN QSRYKFRERR
KRLLNDYSSC SSDDDQSGKN IFIFYNLYMN QYKKKEDNEI NDIYKKYDVH EKNIYDESKQ
YVHKVRVRTD LINHKSVYKI LKNNYLVNIN NMKLMEKKNN SEKLFLINDK DNNSLLSINN
KENFNCIPSR QNNVKKNSEY MHEEENNKTN SNENIARLNN NDFIQVMETE KQKKYNSFDK
YNSDRSSIND TFDEIKYNKN NDNNNDDNNY DDNKNDDDNN NDDNNNNDDN NNNDDNNNND
DNNNGYIYSP VLFINKKFKL GELVYKIPKY VKPQKIYTPY KKISRNKKYS NTLQKDRYEK
WKMLYEELIN NENKTYIIDS VLYKEISYLP YWILNYVNDL FECM
