RT109_CANAL
ID RT109_CANAL Reviewed; 359 AA.
AC Q5AAJ8; A0A1D8PRQ8;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Histone acetyltransferase RTT109;
DE EC=2.3.1.48 {ECO:0000305|PubMed:20601951};
GN Name=RTT109; OrderedLocusNames=CAALFM_CR00410WA; ORFNames=CaO19.7491;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20601951; DOI=10.1038/nm.2175;
RA Wurtele H., Tsao S., Lepine G., Mullick A., Tremblay J., Drogaris P.,
RA Lee E.H., Thibault P., Verreault A., Raymond M.;
RT "Modulation of histone H3 lysine 56 acetylation as an antifungal
RT therapeutic strategy.";
RL Nat. Med. 16:774-780(2010).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20080646; DOI=10.1073/pnas.0912427107;
RA Lopes da Rosa J., Boyartchuk V.L., Zhu L.J., Kaufman P.D.;
RT "Histone acetyltransferase Rtt109 is required for Candida albicans
RT pathogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1594-1599(2010).
RN [6]
RP FUNCTION.
RX PubMed=21749487; DOI=10.1111/j.1365-2958.2011.07754.x;
RA Stevenson J.S., Liu H.;
RT "Regulation of white and opaque cell-type formation in Candida albicans by
RT Rtt109 and Hst3.";
RL Mol. Microbiol. 81:1078-1091(2011).
CC -!- FUNCTION: Histone chaperone-dependent acetylase that modifies 'Lys-56'
CC of histone H3 (H3K56ac), to promote genomic stability, DNA repair and
CC transcriptional regulation during mitotic S-phase (PubMed:20601951,
CC PubMed:20080646). Plays an important role in the regulation of white-
CC opaque genotoxin induced-switching (PubMed:21749487).
CC {ECO:0000269|PubMed:20080646, ECO:0000269|PubMed:20601951,
CC ECO:0000269|PubMed:21749487}.
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:0000305|PubMed:20601951};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000305|PubMed:20601951};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q07794}.
CC -!- DISRUPTION PHENOTYPE: Leads to a decreased pathogenicity in mice and
CC increased susceptibility to killing by macrophages in vitro.
CC {ECO:0000269|PubMed:20080646}.
CC -!- SIMILARITY: Belongs to the RTT109 family. {ECO:0000305}.
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DR EMBL; CP017630; AOW30812.1; -; Genomic_DNA.
DR RefSeq; XP_718648.1; XM_713555.1.
DR PDB; 7BWZ; X-ray; 1.77 A; A=1-359.
DR PDB; 7BX0; X-ray; 1.50 A; A=1-359.
DR PDB; 7BX1; X-ray; 1.58 A; A=1-359.
DR PDB; 7BXW; X-ray; 1.78 A; A=1-359.
DR PDB; 7C3O; X-ray; 1.89 A; A=1-359.
DR PDBsum; 7BWZ; -.
DR PDBsum; 7BX0; -.
DR PDBsum; 7BX1; -.
DR PDBsum; 7BXW; -.
DR PDBsum; 7C3O; -.
DR AlphaFoldDB; Q5AAJ8; -.
DR SMR; Q5AAJ8; -.
DR BioGRID; 1222772; 1.
DR STRING; 237561.Q5AAJ8; -.
DR GeneID; 3639678; -.
DR KEGG; cal:CAALFM_CR00410WA; -.
DR CGD; CAL0000176178; RTT109.
DR VEuPathDB; FungiDB:CR_00410W_A; -.
DR eggNOG; KOG4534; Eukaryota.
DR HOGENOM; CLU_050421_0_0_1; -.
DR InParanoid; Q5AAJ8; -.
DR OMA; ADTNGYC; -.
DR OrthoDB; 594915at2759; -.
DR PRO; PR:Q5AAJ8; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IMP:CGD.
DR GO; GO:0032931; F:histone acetyltransferase activity (H3-K56 specific); IMP:CGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0016573; P:histone acetylation; IMP:CGD.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IMP:CGD.
DR GO; GO:1900429; P:negative regulation of filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036166; P:phenotypic switching; IMP:CGD.
DR GO; GO:1900239; P:regulation of phenotypic switching; IMP:CGD.
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 PIRSF; PIRSF027124; Histone_acetylase_Rtt109; 1.
DR SMART; SM01250; KAT11; 1.
DR PROSITE; PS51728; RTT109_HAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA damage; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Transferase; Virulence.
FT CHAIN 1..359
FT /note="Histone acetyltransferase RTT109"
FT /id="PRO_0000420188"
FT DOMAIN 1..359
FT /note="Rtt109-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01064"
FT ACT_SITE 264
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT BINDING 176
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT BINDING 180
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT BINDING 195..197
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT BINDING 205
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT MOD_RES 266
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q07794"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 39..51
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 54..67
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 167..177
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 199..213
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:7BX0"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:7BX0"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 304..314
FT /evidence="ECO:0007829|PDB:7BX0"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 327..338
FT /evidence="ECO:0007829|PDB:7BX0"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:7BX0"
SQ SEQUENCE 359 AA; 41735 MW; DABD3DCD9A24DDF4 CRC64;
MLPPDILQNG EFETIYFQTN PTYIKSPIHI PKSTIGKPDT VKIRHFFALL HQDLVVLGLE
VFVYLQIYSD FVEKYVYVSK CDTVGLEKST IKIGKVIGPV LQYIINYNGY KIKMKNLDEK
SKDLSDPSTL VRLQRLRDKL PDIYPNLPYY NDIPPKEECI EYRTLPKTQN LRLCVFTKPA
KEYLFPNSAK NPYKNLLNGQ SLLRWWISII DSITKGWNNH KLMIPGADKY ATRKFIEKYS
DWSEGHIFKK DGLAVQAIPL FPDDPKGRFL ELVIVECRYG KMTVSRFYQE LAYRQEFLLG
DCVSLIGCCK ENLEVTYHDD SVSTVTISEY KEFMNSLKSV DFSDRVEVSN FVSNYRKSK
