ID W5PFU8_SHEEP Unreviewed; 2041 AA.
AC W5PFU8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:ENSOARP00000009313.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000009313.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000009313.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000009313.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000009313.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMGL01071541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01071542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; W5PFU8; -.
DR STRING; 9940.ENSOARP00000009313; -.
DR PaxDb; 9940-ENSOARP00000009313; -.
DR Ensembl; ENSOART00000009450.1; ENSOARP00000009313.1; ENSOARG00000008677.1.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_001232_0_1_1; -.
DR OMA; AFQHQSG; -.
DR Proteomes; UP000002356; Chromosome 25.
DR Bgee; ENSOARG00000008677; Expressed in pituitary gland and 53 other cell types or tissues.
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; 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; 1.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
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 258..309
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 704..978
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 72..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 983..1010
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 460..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1088
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1122
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1347
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1394
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 880
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 2041 AA; 227126 MW; A2E07D8BA6A4BA73 CRC64;
MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV
LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK SAKGSRGSCN DLRNVDWNKL LRRAIEGLEE
PNGSSLKNIE KYLRSQSDLT STTTNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGGLD
GKGAPKYPSA FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC
GSSGHPSCLK FCPECIECKT CSACRIQGKN ADNMLFCDSC DRGFHMECCD PPLSRMPKGM
WICQVCRPKK KGRKLLHEKA AQIKRRYAKP IGRPKNKLKQ RLLSVTSDEG SMNAFTGRGS
PGRGQKTKVC TTPSSGHAAS GKDSSSRLAV TDPTRPGATT KITTTSTYIS ASTLKVNKKT
KGLIDGLTKF FTPSPDGRRS RGEIIDFSKH YHPRKKVSQK QSCTSHVLAP GTTQKLKPPL
SSLPPPTPIS GQSPSSQKSS TSVSSTSPQS SSSQSSVPSF SSLTNNSQLK ALFDGLSHIY
TTQGQSRQKG HPSYAPPKRM RRKTEFPLTA KSKAHFFGKR DIRSRFISHS SSSSWGMARG
RIFKAIAHFK RTTFLKKHRM LGRLKYKVTP QMGTPSPGKG SLTDGRIKPD QDDDTEIKIS
IKQESTDINV IGNKDTVTEE DLDVFKQAQE LSWEKIECES GVEDCGRYPS VIEFGKYEIQ
TWYSSPYPQE YARLPKLYLC EFCLKYMKSK NILLRHSKKC GWFHPPANEI YRRKDLSVFE
VDGNMSKIYC QNLCLLAKLF LDHKTLYYDV EPFLFYVLTK NDEKGCHLVG YFSKEKLCQQ
KYNVSCIMIM PQHQRQGFGR FLIDFSYLLS RREGQAGSPE KPLSDLGRLS YLAYWKSVIL
EYLYHHHERH ISIKAISRAT GMCPHDIATT LQHLHMIDKR DGRFVIIRRE KLILGHMEKL
KTCSRTNELD PESLRWTPIL ISNAAVSEEE REAEKEAERL MEQASCWEKE EQEILSSRAN
SRQSPAKVQS KNKYLHSPES RPVAGERGQL MELSKESSEE EEEEEEEEEE EEEEEEEEEE
EEEEEEENIQ SSPPRLTKPQ SVAIKRKRPF VVKKKRGRKR RRINSSVTTE TISETTEVLN
EPFDNSDEER PMPQLEPTCE TEVEEDSRKP VPRRAFQHQP GKKRQTEEEE GEDNHCFKST
DPCRNNVDDG ANNLKEASRD NPEPLKCKQW PKGTKRALSK WRPNKERKTG FKLNLYTPPE
TPLEPDDQVT AEEQKETPAD KTSPTSTRIE EGVKEAVEPL LPQNENGREE TCAPVSPNKS
PGGKPEDELI KPEEEEEEEE EEEEERNVEK DASGAKSQGK EEPEVCMDKE DPVNLDDHEE
EEEEEEEPSH NEGHDADDED DSHMASAEAK EEHPREAFKE VLENQGAFLD LSVPPSHSNP
EVLMDCGVDL PASCNSEPKE LAGATETAPE SDEEPPGEQA QKQDQKNSEE ADSEFKEGNT
ATLEIDSETV QAVQSLTQEN SEQDDTFQDC AETQEACRSL QNYTHADQSP QISAALDDCQ
QSDHSSPVSS VHSHPGQSVR SVNSPSVPAL ENSYAQISPD QSAISVPSLQ NMETSPMMDV
PSVSDHSQQV VDSGFSDLGS IESTTENYEN PSSYDSTMGG SICGNGSSQN SCSYSNLTSS
SLTQSSCAVT QQMSNISGSC SMLQQTSISS PPTCSVKSPQ GCVVERPPSS SQQLAQCSMA
ANFTPPMQLA EIPETGNANL GLYERMGQSD FGAGHYPQPS ATFSLAKLQQ LTNTLIDHSL
PYSHSAAVTS YANSASLSTP LSNTGLVQLS QSPHSVPGGP QAQATMTPPP NLTPPPMNLP
PPLLQRNMAA SNIGISHSQR LQTQIASKGH VSMRTKSASL SPAAATHQSQ IYGRSQTVAM
QGPARTLTMQ RGMNMSVNLM PSPAYNVNSV NMNMNTLNAM NGYSMSQPMM NSGYHSNHGY
MNQTPQYPMQ MQMGMMGTQP YAQQPMQTPP HSNMMYTAPG HHGYMNTGMS KQSLNGSYMR
R
//
