ID G3W6G6_SARHA Unreviewed; 1862 AA.
AC G3W6G6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 73.
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:ENSSHAP00000011021.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000011021.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000011021.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000011021.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 STRING; 9305.ENSSHAP00000011021; -.
DR Ensembl; ENSSHAT00000011115.2; ENSSHAP00000011021.2; ENSSHAG00000009496.2.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000157372; -.
DR HOGENOM; CLU_001232_1_1_1; -.
DR TreeFam; TF106483; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
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; cd04301; NAT_SF; 1.
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; 1.
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; 1.
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 Activator {ECO:0000256|ARBA:ARBA00023159};
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:UP000007648};
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 213..272
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 269..320
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 532..806
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 72..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 811..838
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 845..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..908
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..943
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 708
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1862 AA; 206410 MW; 045BDBA616C92E96 CRC64;
MVKLANPLYT EWILEAIQKV KKQKQRPSEE RICHAVSASH GLDKKTVSEQ LELSVQDGSV
LKVTNKGLAS YKDPDNPGRF SSLKPGTFPK SAKGSRGSCN DLRNVDWNKL LRRAIEGLQE
PNGSSLKNIE KYLRSQSDLT STTNNAAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGSLE
GSGAPKYSNT FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC
GSSGHPSCLK FCPELTTNVK ALRWQCIECK TCSACRIQGK NADNMLFCDS CDRGFHMECC
DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK QRMLSVTSDE
GSTNAFTGRG SPGRGQKTKV CTTPSSGHAA SVKDSSSRLA VTDPTRPGAT TKITTTSTYI
SASTLKVNKK TKGLIDGLTK FFTPSPDGRR SRGEIIDFSK HYRPRKKVSQ KQSCTSHVLA
TDTEIKISIK QEGTDVNVIG SKDSVTEEDL DVFKQAQELS LEKIGCKNGV ESSGRYPSVI
EFGKYEIQTW YSSPYPQEYA RLPKLYLCEF CLKYMKSKNI LLRHSKKCGW FHPPANEIYR
RKDLSVFEVD GNVSKIYCQN LCLLAKLFLD HKTLYYDVEP FLFYVLTKND EKGCHLVGYF
SKEKLCQQKY NVSCIMIMPQ YQRQGFGRFL IDFSYLLSRR EGQAGSPEKP LSDLGRLSYL
AYWKSVILEY LYYHHEKHIS IKGISRATGM CPHDIATTLQ HLRMIDKREE KFVIIRREKL
ILGHMEKLKT NARVNELDPE SLRWTPLLVS NAAVSEEERE AEKEAERLME QASCWEKEDQ
EILSARANSR QSPAKVQSKN KYLRSPESVP MAGDRGQSTE PTKDSSEEEE EEEEEEEEEE
EEEEEEEENH RSSPPRLTKP QSLAMKRKRP FILKKKRGRK RRRINSSVTT ETISETTEVL
NEPFDNSDDE RPMPQLEPTC EIEGEEDDLK PAIKKVFQFQ SGKQRQTEEE EKDNHCFNND
DPCRNNTDNS NNLKEDSVDN PESLKCKQGW PKGMKRGPSK WKQSKDRKTG FKLNLYTPPE
TPMEPDYQVT GEEQKESTQE ELSHMSGVAE AAAKEADLPK QPQSEDGGVT AAPPSPRPLP
LEKSEDQGLK PEEEEGEEEE EEEEEEGVLE GDSNRANSRG GPRVEAFVGP KEPEHLEDHE
EEEEEEEPSR NEDHDADDED DSHLEAAEAQ KEELPTEAFK GVLENQDTFL DLSVPAGPPN
PETLMDCSMD LAAPCSGEPK ECPADAKGVP EPDGGHPGGP AEGEGQKKRE DRNPEFKEET
PETMEIDSET VQAVQSLTQE NPGQDDTFQE CAETQEACQS LQSYSQADQS PPMAPLDDCP
QSNHSSPVSS VHSHPGQSVR SVSSPSVPAL ESSYPQISPD QGAISVPSLQ NMETSPMMDV
PSVSDHSQQV VDSGFSDLGS IESTTENYEN PSSYDSSMGS SICGNTSSQN SCSYSSLTSS
NLTQSSCAVT QQMSGMNGSC SMMQPASISS PPTCNVKSPQ GCVGERPPSG SQQLPQCSLA
ATFTPPMQLA EIPEAGGANL GLYERMGQSE FGAGHYPQPS ATFSLAKLQQ LTNTLIDHSL
PYSHSAAVTS YANSASLSTP LSNTGLVQLS QSAHSVPGGP QAQATMTPPP NLTPPPMNLP
PPLLQRNMAA SNLGISHTQR LQTQIASKGH AAMRTKSASL PPAAAAHQPQ LYGRASQTVA
MQGPARTLTM QRGMNMSVNL MPAPAYNVNS VNMNMNTLNA MNGYGMSQPM MNSGYHGNHG
YMNQTAQYPM QMQMGMMGTQ PYAQQPMQTP PHGNMMYTAP GHHGYMNTGM AKQPLNGSYM
RR
//
