HAT11_DICDI
ID HAT11_DICDI Reviewed; 486 AA.
AC Q86J12; Q555T7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Histone acetyltransferase type B catalytic subunit DDB_G0274269;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:O14929};
GN ORFNames=DDB_G0274269;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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:O14929};
CC -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
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DR EMBL; AAFI02000012; EAL70027.1; -; Genomic_DNA.
DR RefSeq; XP_643973.1; XM_638881.1.
DR AlphaFoldDB; Q86J12; -.
DR SMR; Q86J12; -.
DR STRING; 44689.DDB0237834; -.
DR PaxDb; Q86J12; -.
DR EnsemblProtists; EAL70027; EAL70027; DDB_G0274269.
DR GeneID; 8619399; -.
DR KEGG; ddi:DDB_G0274269; -.
DR dictyBase; DDB_G0274269; -.
DR eggNOG; KOG2696; Eukaryota.
DR HOGENOM; CLU_036024_2_1_1; -.
DR InParanoid; Q86J12; -.
DR OMA; HNANECI; -.
DR PhylomeDB; Q86J12; -.
DR Reactome; R-DDI-3214847; HATs acetylate histones.
DR PRO; PR:Q86J12; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:InterPro.
DR Gene3D; 3.90.360.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR019467; Hat1_N.
DR InterPro; IPR037113; Hat1_N_sf.
DR InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su.
DR PANTHER; PTHR12046; PTHR12046; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF10394; Hat1_N; 1.
DR PIRSF; PIRSF038084; HAT-B_cat; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Coiled coil; Reference proteome; Transferase.
FT CHAIN 1..486
FT /note="Histone acetyltransferase type B catalytic subunit
FT DDB_G0274269"
FT /id="PRO_0000367831"
FT DOMAIN 189..386
FT /note="N-acetyltransferase"
FT REGION 33..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..69
FT /evidence="ECO:0000255"
FT COILED 392..481
FT /evidence="ECO:0000255"
FT COMPBIAS 33..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 299
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT BINDING 260..262
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT BINDING 267..273
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT SITE 218
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:O14929"
SQ SEQUENCE 486 AA; 57832 MW; B47394CB3F8294E7 CRC64;
MTNRIKSSNT LLTFDANEVT NIKLVWDIEE LKNKDNKENK DKENKAHIKD EGEEEEQKEK
KEEEEKEDDG GPISFHPTYS HQIFNEDKIQ GYEPCKIDIY MGAGSLTSYI DTNYTLQSKN
LTNVEGEFLK VFSKQDPPIS KQSFYKYIEE KEKLFKPIGK KIHEYSIIDK ESGKETEYEI
YFGRITDQVV FRYHEKLQIF VLWYIDGSSY IWTDDPNWDI FFIFEKRIID GEKRYGITGY
STIYNFYHHP EQTRARISQY LILPPYQRMG HGKYLFNSIY QYYKTNDGFY GPIYDITIED
PADEFNLLRN YVDLKNIMDE KLFDNVILDL NANNKSVFEE IRKKLLIPYK QSKLCLEIYL
FSKFLGTPNS DTKYKEYRIS IKKRLYKQNI GDSEQIEKIK QQVAEENQEN LRLEQEELQE
LQDIENKKNG TNIKVDIKPK ELTTPPGPEK NKEEIEKDRL EEILELYKEL EKNYHKTLSS
LNLISK
