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Database: UniProt
Entry: H2UAS2_TAKRU
LinkDB: H2UAS2_TAKRU
Original site: H2UAS2_TAKRU 
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
//
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