RT109_SCHPO
ID RT109_SCHPO Reviewed; 369 AA.
AC Q9Y7Y5;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Histone acetyltransferase rtt109;
DE EC=2.3.1.48 {ECO:0000269|PubMed:17369611, ECO:0000269|PubMed:17690098, ECO:0000269|PubMed:20656950};
GN Name=rtt109; Synonyms=kat11; ORFNames=SPBC342.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17369611; DOI=10.1074/jbc.m701197200;
RA Xhemalce B., Miller K.M., Driscoll R., Masumoto H., Jackson S.P.,
RA Kouzarides T., Verreault A., Arcangioli B.;
RT "Regulation of histone H3 lysine 56 acetylation in Schizosaccharomyces
RT pombe.";
RL J. Biol. Chem. 282:15040-15047(2007).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17690098; DOI=10.1074/jbc.m702496200;
RA Han J., Zhou H., Li Z., Xu R.-M., Zhang Z.;
RT "Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated
RT by ASF1 is required for replisome integrity.";
RL J. Biol. Chem. 282:28587-28596(2007).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20656950; DOI=10.1165/rcmb.2009-0443oc;
RA Kottom T.J., Han J., Zhang Z., Limper A.H.;
RT "Pneumocystis carinii expresses an active Rtt109 histone
RT acetyltransferase.";
RL Am. J. Respir. Cell Mol. Biol. 44:768-776(2011).
CC -!- FUNCTION: Histone chaperone-dependent acetylase that modifies 'Lys-56'
CC of histone H3 (H3K56ac), which occurs predominantly in newly
CC synthesized H3 molecule during G1, S-phase and G2/M of cell cycle
CC (PubMed:17369611, PubMed:17690098, PubMed:20656950). Histone H3 'Lys-
CC 56' acetylation is required for S-phase-linked DNA damage tolerance and
CC proper silencing in pericentromeric heterochromatin (PubMed:17369611).
CC {ECO:0000269|PubMed:17369611, ECO:0000269|PubMed:17690098,
CC ECO:0000269|PubMed:20656950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:17369611, ECO:0000269|PubMed:17690098,
CC ECO:0000269|PubMed:20656950};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000269|PubMed:17369611, ECO:0000269|PubMed:17690098,
CC ECO:0000269|PubMed:20656950};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q07794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000250|UniProtKB:Q07794};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the RTT109 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB46776.1; -; Genomic_DNA.
DR PIR; T40279; T40279.
DR RefSeq; NP_596749.1; NM_001023769.2.
DR AlphaFoldDB; Q9Y7Y5; -.
DR SMR; Q9Y7Y5; -.
DR BioGRID; 277461; 65.
DR STRING; 4896.SPBC342.06c.1; -.
DR MaxQB; Q9Y7Y5; -.
DR PaxDb; Q9Y7Y5; -.
DR PRIDE; Q9Y7Y5; -.
DR EnsemblFungi; SPBC342.06c.1; SPBC342.06c.1:pep; SPBC342.06c.
DR GeneID; 2540945; -.
DR KEGG; spo:SPBC342.06c; -.
DR PomBase; SPBC342.06c; rtt109.
DR VEuPathDB; FungiDB:SPBC342.06c; -.
DR eggNOG; KOG4534; Eukaryota.
DR HOGENOM; CLU_740004_0_0_1; -.
DR InParanoid; Q9Y7Y5; -.
DR OMA; FARAQPQ; -.
DR PhylomeDB; Q9Y7Y5; -.
DR PRO; PR:Q9Y7Y5; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032931; F:histone acetyltransferase activity (H3-K56 specific); IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IDA:UniProtKB.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR016849; Rtt109.
DR PANTHER; PTHR31571:SF2; PTHR31571:SF2; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR SMART; SM01250; KAT11; 1.
DR PROSITE; PS51728; RTT109_HAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA damage; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..369
FT /note="Histone acetyltransferase rtt109"
FT /id="PRO_0000353836"
FT DOMAIN 1..346
FT /note="Rtt109-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01064"
FT REGION 345..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT BINDING 117
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT BINDING 136..138
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT BINDING 146
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT MOD_RES 221
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
SQ SEQUENCE 369 AA; 42373 MW; 4031DC6370CDF54B CRC64;
MPDLWSESIL EGRKLSIYHL KSTLEKCPFL FGQSKKSKDF QFGSHLFLVE EQNVFIFGME
CIVYEKNKEF IVFVSKADST GFGSKGVSCN SLAFCCLVTL IDGLRKQGAE NVTLTLFAIA
QGQYLFPESV DNGQKHVLND SGLLRWWVNC LEKLRKYYTD SEAPNDSEKQ KNSTLLPKAY
LFVPGLENIR SYLPNRHWIE SNAITTGKAV EELPRFPDDP KCRYLCELQD EKSDMSVEEF
WDTLTYRQEC SSGKLVGFFT LQLQFYQTRE FIAKDNFGDS GVMIPAKLYR VTYDTLLKHP
FGSLSDAQSS TEKFLSNTLS AVQNLKDFHY KRYKLDICGL AKRDDRKNHN HSKPATQANI
LQPRKKVKK
