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Histone acetyltransferase type B catalytic subunit (EC 2.3.1.48)

 HAT1_NEUCR              Reviewed;         508 AA.
Q7RYU8;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
15-DEC-2003, sequence version 1.
28-MAR-2018, entry version 85.
RecName: Full=Histone acetyltransferase type B catalytic subunit;
EC=2.3.1.48 {ECO:0000250|UniProtKB:Q12341};
Name=hat-1; ORFNames=NCU06472;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
-!- FUNCTION: Catalytic component of the histone acetylase B (HAT-B)
complex. Acetylates 'Lys-12' of histone H4 which is required for
telomeric silencing. Has intrinsic substrate specificity that
modifies lysine in recognition sequence GXGKXG. Involved in DNA
double-strand break repair. {ECO:0000250|UniProtKB:Q12341}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000250|UniProtKB:Q12341}.
-!- SUBUNIT: Component of the HAT-B complex composed of at least hat-1
and hat-2. The HAT-B complex binds to histone H4 tail.
{ECO:0000250|UniProtKB:Q12341}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CM002238; EAA28127.1; -; Genomic_DNA.
RefSeq; XP_957363.1; XM_952270.3.
ProteinModelPortal; Q7RYU8; -.
SMR; Q7RYU8; -.
EnsemblFungi; EAA28127; EAA28127; NCU06472.
GeneID; 3873462; -.
KEGG; ncr:NCU06472; -.
EuPathDB; FungiDB:NCU06472; -.
HOGENOM; HOG000164382; -.
InParanoid; Q7RYU8; -.
KO; K11303; -.
OMA; MAHQIFG; -.
OrthoDB; EOG092C3YYH; -.
Proteomes; UP000001805; Chromosome 3, Linkage Group III.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0010485; F:H4 histone acetyltransferase activity; IBA:GO_Central.
GO; GO:0042393; F:histone binding; IBA:GO_Central.
GO; GO:0006348; P:chromatin silencing at telomere; IEA:InterPro.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
Gene3D; 3.90.360.10; -; 2.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR019467; Hat1_N.
InterPro; IPR037113; Hat1_N_sf.
InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su.
PANTHER; PTHR12046; PTHR12046; 1.
Pfam; PF10394; Hat1_N; 1.
PIRSF; PIRSF038084; HAT-B_cat; 1.
SUPFAM; SSF55729; SSF55729; 1.
3: Inferred from homology;
Acyltransferase; Chromatin regulator; Complete proteome; Cytoplasm;
DNA damage; DNA repair; Nucleus; Reference proteome; Transferase.
CHAIN 1 508 Histone acetyltransferase type B
catalytic subunit.
/FTId=PRO_0000227726.
REGION 44 46 Interaction with histone H4 N-terminus.
{ECO:0000250|UniProtKB:Q12341}.
REGION 207 209 Interaction with histone H4 N-terminus.
{ECO:0000250|UniProtKB:Q12341}.
REGION 249 251 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q12341}.
REGION 256 262 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q12341}.
ACT_SITE 284 284 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q12341}.
SITE 178 178 Interaction with histone H4 N-terminus.
{ECO:0000250|UniProtKB:O14929}.
SEQUENCE 508 AA; 57696 MW; D2DCF7829D6855D7 CRC64;
MSGDDDWWTS SNEALLVSLV TPSDTGVKTL DTFHPEYTNN IFGEKEQIFG YKGLRINLQY
NASDMLPNLK VSYKKKYQPT ADEEALDINE VLSEFLPEIA FQKQSDFETR LKSIPDNWTP
PGTLVTSFTN KDGEYEVYSG KITDPAVKQL LNRIQILVPF FVDGGTPIDM EDPDVDRWTI
YFLYNKRPLL NQPDKFSYHF AGYSTLYRYY AFQPPAESES KTPTDTPTFS VDGDFDLDTL
PCRTRISQFI IIPPFQQKGL GSRLYSIIYQ QYLKHEPTIE LTVEDPNEAF DDMRDLADLA
FLSKQPEFQA LKIDTSVEIP EEGKAPSNIV DQAAWEACRK KFKIVPRQFA RVLEMYLMSQ
LPESVRPGLG APEDEDYEEQ SGRSKSKGHE KALPKPTPED EHTYRLWMML VKRRLYVHNR
DALGQLELKE RREELAKVFA GVEFDYARLL IKAEEQGKLA QADGETAGDQ VPATPSAANG
KRKLDEVEQA EGTAAASSKK AKVESGHA


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