ID   RT109_PNECA             Reviewed;         375 AA.
AC   D3G9N3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Histone acetyltransferase Rtt109 {ECO:0000303|PubMed:20656950};
DE            EC=2.3.1.48 {ECO:0000269|PubMed:20656950};
DE   AltName: Full=PcRTT109 {ECO:0000303|PubMed:20656950};
GN   Name=Rtt109 {ECO:0000303|PubMed:20656950};
OS   Pneumocystis carinii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX   NCBI_TaxID=4754 {ECO:0000312|EMBL:ACR39370.1};
RN   [1] {ECO:0000312|EMBL:ACR39370.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP   OF ASP-84; ASP-218 AND ASP-219.
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) (PubMed:20656950). Histone H3 'Lys-56'
CC       acetylation may be required for S-phase-linked DNA damage tolerance (By
CC       similarity). Also acetylates 'Lys-9' of histone H3 (H3K9ac) (By
CC       similarity). Autoacetylates (PubMed:20656950).
CC       {ECO:0000250|UniProtKB:Q07794, 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:0000269|PubMed:20656950};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC         Evidence={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:20656950};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC         Evidence={ECO:0000269|PubMed:20656950};
CC   -!- SUBUNIT: Forms a complex composed of two RTT109 subunits and one VPS75
CC       homodimer (By similarity). Interacts with ASF1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q07794}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q07794}.
CC   -!- SIMILARITY: Belongs to the RTT109 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01064}.
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DR   EMBL; FJ588486; ACR39370.1; -; mRNA.
DR   SMR; D3G9N3; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032931; F:histone acetyltransferase activity (H3-K56 specific); IDA:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0097043; P:histone H3-K56 acetylation; IDA:UniProtKB.
DR   GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:InterPro.
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; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN           1..375
FT                   /note="Histone acetyltransferase Rtt109"
FT                   /id="PRO_0000453550"
FT   ACT_SITE        219
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q07794"
FT   BINDING         125
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q07794"
FT   BINDING         144..146
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q07794"
FT   BINDING         154
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"
FT   MUTAGEN         84
FT                   /note="D->A: Abolishes histone acetyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:20656950"
FT   MUTAGEN         218
FT                   /note="D->A: Mildly decreases histone acetyltransferase
FT                   activity; when associated with A-219."
FT                   /evidence="ECO:0000269|PubMed:20656950"
FT   MUTAGEN         219
FT                   /note="D->A: Mildly decreases histone acetyltransferase
FT                   activity; when associated with A-218."
FT                   /evidence="ECO:0000269|PubMed:20656950"
SQ   SEQUENCE   375 AA;  43516 MW;  F5D2A87AD44E03D7 CRC64;
     MDNLYTGISK SIESLPPEIT FSYGYIFTNF KKLKWPWLNK RKIDNVYLSN HFFFILQEDA
     MAYAIEVLIF FSSELSVFYI SKADSTGFFN RHGSPSPLKA VISTFLSYLI RRFSRKNIPS
     RISLFSRSQP QYLFPSSSLN PSKHILDDRE LVRWWLKVLD SVNGSQCPKK YVLIPGMDPR
     ETLKYTPQHV DTDLNWICGH PYESMGQSAG EIIPRFPDDP KTRFLDQLDR DGEVVSIDKF
     WELMAFRQEC IHGRIVGFFS LEFPGNDQDG TNNTITEDLD LQNGIQINEK IYRMVYEKLL
     RSDFETLEKS KGATLDLIND INNSKDIKDS VDWIKKVSGK KTSEDKKRKA IDISEQLKPV
     NILNESLIRK KSKKK