ID L8HWW7_9CETA Unreviewed; 754 AA.
AC L8HWW7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE Flags: Fragment;
GN ORFNames=M91_19815 {ECO:0000313|EMBL:ELR48408.1};
OS Bos mutus (wild yak).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR48408.1, ECO:0000313|Proteomes:UP000011080};
RN [1] {ECO:0000313|EMBL:ELR48408.1, ECO:0000313|Proteomes:UP000011080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX PubMed=22751099; DOI=10.1038/ng.2343;
RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA Wang J., Liu J.;
RT "The yak genome and adaptation to life at high altitude.";
RL Nat. Genet. 44:946-949(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000256|ARBA:ARBA00008607}.
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DR EMBL; JH882735; ELR48408.1; -; Genomic_DNA.
DR AlphaFoldDB; L8HWW7; -.
DR STRING; 72004.ENSBMUP00000011741; -.
DR Proteomes; UP000011080; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05509; Bromo_gcn5_like; 1.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR037800; GCN5.
DR InterPro; IPR016376; GCN5/PCAF.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR009464; PCAF_N.
DR PANTHER; PTHR45750; GH11602P; 1.
DR PANTHER; PTHR45750:SF2; HISTONE ACETYLTRANSFERASE KAT2B; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF06466; PCAF_N; 1.
DR PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011080};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:ELR48408.1}.
FT DOMAIN 425..573
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 662..732
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 492
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-1"
FT BINDING 496..498
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT BINDING 503..509
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT BINDING 534..537
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT NON_TER 754
FT /evidence="ECO:0000313|EMBL:ELR48408.1"
SQ SEQUENCE 754 AA; 86800 MW; EF0C8F90AC547F56 CRC64;
AEESCKCNGW KNPNPSPTPP RADLQQIIVS LTESCRSCSH ALAAHVSHLE NVSEEEMNRL
LGIVLDVEYL FTCVHREEDA DTKQVYFYLF KLLRKSILQR GKPVVEGSLE KKPPFEKPSI
EQGVNNFVQY KFSHLPPKER QTIVELAKMF LNRINYWHLE APSQRRLRSP NDDISGYKEN
YTRWLCYCNV PQFCDSLPRY ETAQVFGRTL LRSVFTVMRR QLLEQARQEK DKLPLEKRTL
ILTHFPKFLS MLEEEVYSQN SPIWDQDFLS ASSRTSQLGI QTVISPPPVA GTVSYNSSSA
SLEQQNGGSA SPSCRGASGL EANPVGLVGT CFVFEITHRL PFCFDHQGEK RKMNESHVLE
ETKKPRVMGD IPLELIHEVM STITDPTAML GPETNFLSAH SARDEAARLE ERRGVIEFHV
VGNSLSQKPN KKVLMWLVGL QNVFSHQLPR MPKEYITRLV FDPKHKTLAL IKDGRVIGGI
CFRMFPSQGF TEIVFCAVTS NEQVKGYGTH LMNHLKEYHI KHDILNFLTY ADEYAIGYFK
KQGFSKEIKI PKTKYVGYIK DYEGATLMGC ELNPRIPYTE FSVIIKKQKE IIKKLIERKQ
AQIRKVYPGL SCFKDGVRQI PIESIPGIRE TGWKPSGRER SKEARDPDQL YSTLRSILQQ
VKSHQSAWPF MEPVKRTEAP GYYEVIRFPM DLKTMSERLK NRYYVSKKLF MADLQRVFTN
CKEYNPPESE YYKCASILEK FFFSKIKEAG LIDK
//
