ID G5C9N3_HETGA Unreviewed; 490 AA.
AC G5C9N3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Histone acetyltransferase KAT2B {ECO:0000313|EMBL:EHB18244.1};
GN ORFNames=GW7_18074 {ECO:0000313|EMBL:EHB18244.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB18244.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB18244.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000256|ARBA:ARBA00008607}.
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DR EMBL; JH174058; EHB18244.1; -; Genomic_DNA.
DR AlphaFoldDB; G5C9N3; -.
DR STRING; 10181.G5C9N3; -.
DR InParanoid; G5C9N3; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR037800; GCN5.
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 PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Transferase {ECO:0000313|EMBL:EHB18244.1}.
FT DOMAIN 270..418
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 437..490
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
SQ SEQUENCE 490 AA; 56174 MW; E535872EEDBD7BA5 CRC64;
MNRLLGIVLD VEYLFTCVHK EEDADTKQVY FYLFKLLRKS ILQRGKPVVE GSLEKPPFEK
PSIEQGVNNF VQYKFSHLPS KERQTIVELA KMFLNRINYW HLEAPSQRRL RSPNDDISGY
KENYTRWLCY CNVPQFCDSL PRTSQLGIQT VISPPPVAGT VSYNSNSSSL EQPNGGSTSP
ACKASCGFEA NPGEKRKMND SHVLEEVKRP RVMGDIPMEL ISEVMSTITD PASMLGPKTN
FLSAHSARDE ATRLEERRGM TEFHVAGNSL NQKPNKKILM GLVGLQNVFS HQLPRMPKEY
ITRLIFDPKH KTLALIKDSH VIGGICFRMF PSQGFTEIVF CAVTSSEQVK GYGTHLMNHL
KEYHIKHDIL NFLTYADEYA IGYFKKQGFS KEIKIPKTKY VGYIKDYEGA TLMGCELNSQ
TPYTEFSVII KKQKEVKSHQ SAWPFMEPVK RTEAPGYYDV IRFPMDLKTM SERLKNRYYV
SKKLFMADLQ
//