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   27-MAR-2024, entry version 126.
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; 284812.Q9Y7Y5; -.
DR   MaxQB; Q9Y7Y5; -.
DR   PaxDb; 4896-SPBC342-06c-1; -.
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 H3K56 acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; IMP:PomBase.
DR   GO; GO:0140889; P:DNA replication-dependent chromatin disassembly; IEA:InterPro.
DR   GO; GO:0031508; P:pericentric heterochromatin formation; IMP:PomBase.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR   InterPro; IPR016849; Rtt109.
DR   PANTHER; PTHR31571; ALTERED INHERITANCE OF MITOCHONDRIA PROTEIN 6; 1.
DR   PANTHER; PTHR31571:SF2; HISTONE ACETYLTRANSFERASE RTT109; 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
//