ID H2UAS2_TAKRU Unreviewed; 1674 AA.
AC H2UAS2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=kat6b {ECO:0000313|Ensembl:ENSTRUP00000034039.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000034039.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000034039.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000034039.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000780};
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR Ensembl; ENSTRUT00000034165.3; ENSTRUP00000034039.3; ENSTRUG00000013356.3.
DR GeneTree; ENSGT00940000157372; -.
DR HOGENOM; CLU_001232_1_1_1; -.
DR Proteomes; UP000005226; Chromosome 1.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd15618; PHD1_MOZ_MORF; 1.
DR CDD; cd15527; PHD2_KAT6A_6B; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR048589; SAMD1-like_WH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF73; HISTONE ACETYLTRANSFERASE KAT6B; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF21524; SAMD1_WH; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 103..176
FT /note="H15"
FT /evidence="ECO:0000259|PROSITE:PS51504"
FT DOMAIN 212..271
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 268..319
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 402..676
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 66..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 681..708
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 839..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..896
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 578
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1674 AA; 187212 MW; FADF81097D2C2746 CRC64;
MVKLANPLYT EWILEAIQKI KRQKQRPSEE RICHAVATSH GLDKRTVLEQ LELSVHDGSI
LKVTNKGSTS YKDPGNPGRV GSIPPANVSV PSKESIWNSS DLRHIDWNKI LKRAIEGLDD
THGSSLKNIE RYLRNQDDLS NVVDNPAFRQ RLRLAAKRSV NNGRLFKNGP RYKISHGGAE
GRALRCASVS SLLLSSVTLL PHERDQLRVD PIPICSFCLG TKESNRDKQP EELLSCADCG
SSGHPSCLKF SPELTSNVKR LRWQCIECKT CSSCRIQGKN ADEMLFCDSC DRGFHMECCN
PPLSRMPKGT WICQVCRPKE NGKKLLHKKA DQIKRRYAKP IGRPRNKLKQ RIGELHLKQE
ARTTFAAMSR EHVTEEDIET FVHVRELAMQ VRKLTGSQMN TDSMRCPAVI EFGKYEIQTW
YSSPYPPEYS RLQKLYLCEF CLKYMRSKNI LQRHTKKCGW FHPPANEIYR KDNLSVFEVD
GNVSKLFCQN LCLLAKLFLD HKTLYYDVEP FLFYILTKND EKGCHLVGYF SKEKLCQQKY
NVSCIMIMPQ YQRQGFGRFL IDFSYLLTRQ EGQAGSPEKP LSDLGRLSYL AYWKSVILEY
LYKHPDKHIS VKGISRATGM CPHDIASTLQ QLGMIDRQDG RIVLIRRERL ILKHIESLRA
NPRRNDVDPD ALHWTPSTTL NAVLSEEERE AEMDAERLKE QASCWEKEER EGYMSHASRQ
PLTKVHCKVP YRTYERRPAM SWARRVQRSP EVSDDADDDD DSDASDGSPP ILTKAHAMLA
TKRKRTIVLK KRGRKRKRIN SSVTTETISE TTEVLNEPFD NSDDERPMPL LERTCRAGKM
EAEEEEQDEI LITPIKRRRG RPRLEKNVRK DAAKRPGRPR PVKRKKGWPK GVKRGPPKWR
LKSERKMGFK LNLYTPPETP MEAEQHHTQN EAKGEPDQDT ISADECYNAR SVNLDAVLER
LASEPPSPAD LVSQKSSSPE GSPLPSSVGS PTGVPDRADS PEPPEDDRAG HESDPEENSP
AKDVDHGAVS TVSLDNAKEE DDKNEQEATI EDRDAADEDV VRGKAMEPDG SKSELEQGVR
QAPDCITSFL VAKEDGDAEL SQPVSTGLCN EEEPPESAPS PCPNQLPPQP AERLMLSPVL
NENPPVCAEI DSETAQAVQS LTQESEREKV FQDCAESREP CRSLQTYTRV PNSPQLTPMD
DCPQSDHSSP LSSAQSHPSQ SVRSVNSPAV SILESSYTQI SPDHSAISVP SLHNMETSPM
MDVPSVSDHS QQVVDSGFSD LGSIESTTEN YENPSSYDST MGGSICGAGP SQNSCSYGSI
PPSGLAQSSC AVSQQMAAVN PGSCGMIQQN SLSSPPHCNV KSPQGCVVVE RPPSNSHQQQ
PMAQCAIPTN FTTTMQLADI PESGNPNLTL YERLNHQGEY GGGHYPQSSG LSLAKLQQFT
NTFIDHPRSL PFNHTASHPI TSYANTPSLS SQHSSLVSLS QTPHRVPNQQ VQATMTPPPN
LSSPPTMMLQ RNMGIPPSQR IQPQMAPKSH ISSRSKSAPL SHHQQQMYAR PPQAVTMQAP
SRTLAAMPRM NMSVNIMPAP AYNVNSMNMP SLNAMNSYSM SQPMMNSGYH GNHAYMNQSP
QYSMQMGMMG TQPYPQQPMQ APPHGNMVYT PAGHHGYMNT GMPKQSLKGS FIRR
//