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Database: UniProt
Entry: Q5KCG7_CRYNJ
LinkDB: Q5KCG7_CRYNJ
Original site: Q5KCG7_CRYNJ 
ID   Q5KCG7_CRYNJ            Unreviewed;       525 AA.
AC   Q5KCG7;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 2.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   OrderedLocusNames=CNH00950 {ECO:0000313|EMBL:AAW44982.2};
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW44982.2, ECO:0000313|Proteomes:UP000002149};
RN   [1] {ECO:0000313|EMBL:AAW44982.2, ECO:0000313|Proteomes:UP000002149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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:0000256|ARBA:ARBA00024456};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC         Evidence={ECO:0000256|ARBA:ARBA00024456};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AE017348; AAW44982.2; -; Genomic_DNA.
DR   RefSeq; XP_572289.1; XM_572289.1.
DR   AlphaFoldDB; Q5KCG7; -.
DR   STRING; 214684.Q5KCG7; -.
DR   PaxDb; 214684-Q5KCG7; -.
DR   EnsemblFungi; AAW44982; AAW44982; CNH00950.
DR   VEuPathDB; FungiDB:CNH00950; -.
DR   eggNOG; KOG4534; Eukaryota.
DR   HOGENOM; CLU_019224_0_0_1; -.
DR   InParanoid; Q5KCG7; -.
DR   OrthoDB; 2787984at2759; -.
DR   Proteomes; UP000002149; Chromosome 8.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032931; F:histone H3K56 acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; IBA:GO_Central.
DR   GO; GO:0140889; P:DNA replication-dependent chromatin disassembly; IEA:InterPro.
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   4: Predicted;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          252..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  56323 MW;  2EF2F2FA7D1DF079 CRC64;
     MLVPSHLRDH LLHSLSPLPN TQPLGLTVLA SQPKRTRELF PHAVHPPKCT QQEWLVVFDS
     EMETDKVSIK DAGDGKSAKH PRVLIAAISA HLYTFSPSVP SVLYISKVDS SGYSSSATPL
     PLTRHLIRSF ILFFLAHCPA LRVQLFARAQ RQYLFANSAD WKGKKVLGGA GLCKWWKGVY
     EDVVSSWASS SPSPGPAGST GLKLKVEKQA MKLRFILPGY DEQEAKALLG AGRPLPEGVE
     WTYTPPFTSP LIPSASGSGS GSDPKISLAT LIPSLPDDPK TRFLQELVSE HPRPPTSSAT
     AKDEQGGQEI SNDGSGPGTG RGGREGGKEG KTRKLHEAEE DAAQRKFAEN ILHSVGIAEF
     WERMGFRQEC ASGDVTGFFT LESVTEVESK RKSEESSPDA TTPIATAAAA ATPAIAKNAL
     LPQAITERLL TALTNLDFAS PSLAIEGSTI WLEQTRSIVV GEVGKVGWDL CVGRIEAKAG
     QAGQTGQANM GVGDGGAREG AGEGVRKREE VVTMLQPRKK KKVVQ
//
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