ID A0A3Q4HER2_NEOBR Unreviewed; 1627 AA.
AC A0A3Q4HER2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSNBRP00000020446.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000020446.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000020446.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; 32507.ENSNBRP00000020446; -.
DR Ensembl; ENSNBRT00000020998.1; ENSNBRP00000020446.1; ENSNBRG00000015694.1.
DR GeneTree; ENSGT00940000157372; -.
DR OMA; AFQHQSG; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000015694; Expressed in blood and 8 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; 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; PF00538; Linker_histone; 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 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:UP000261580};
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 363..637
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 704..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 642..669
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 763..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..853
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1023
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 539
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1627 AA; 182498 MW; 15921007CBF247DF CRC64;
MVKLANPLYT EWILEAIQKI KRQKQRPSEE RICHAVATSH GLDKKTVLEQ LELSVHDGSI
LKVTNKGSAS YKDPGHPGRV GSILPANAPV PSKESIWNSS DLRHIDWNKM LRRAIEGLDD
THGSSLKNIE RYLRNQDDLS DIVDNPAFRQ RLRLAAKRAV NNGRLSKNGP RYKLSHGSVE
GRSSRCPSAS TLVLSSVTLL PHERDQLRVD PIPICSFCLG TKESNRDKRP EELLSCADCG
SSGHPSCLKF SPELTSNVKR LRWQCIECKT CSSCRIQGKN ADEMLFCDSC DRGFHMECCD
PPLSRMPKGT WICQVCRPKE NGKKLLHKKA DQIKRRYAKP IGRPRNKLKQ RITGSRSSLM
NTDSVRCPAV IEFGKYEIQT WYSSPYPPEY SRLQKLYICE FCLKYMRSKN ILQRHTKKCG
WFHPPANEIY RKDNLSVFEV DGNVSKLFCQ NLCLLAKLFL DHKTLYYDVE PFLFYILTKN
DEKGCHLVGY FSKEKLCQQK YNVSCIMIMP QYQRQGFGRF LIDFSYLLTR QEGQAGSPEK
PLSDLGRLSY LAYWKSVILE HLYKHPDKHI SVKGISRATG MCPHDIAATL QQLGMIDRQD
GRIVLIRRER LIQRHMEKLR ANPRQIEVDP DALHWTPSTT LNAVLSEEER EAEMDAERLK
EQASCWEKEE REGYMMTHSS RQPLTKVHCK VPYRTYERRP APPWTRRIQL TEEVSDEEAD
DDDDDSDGSP PILTKAHAML AAKRKRTLVL KKRGRKRKRI NSSVTTETIS ETTEVLNEPF
DNSEDERPMP LLERTFRVGE MDEEDEEEAH KDKTPAAPIK RRRGRPRLEK NRPSKPRPVK
RKKGWPKGVK RGPPKWKLKN ERKMGFKLNL YTPPETPMEA EQHHIHTEEA KDGPHQDGVH
VDEGSKAGRG SASPNIMLDR FPSEPPSPAD HGSHKSSSPE ASPVASLVCS PAASPGAVSP
RQVDAADSPE PPEDDQQEVQ HEQKSPAKDV VHSTEGAVSL ENENEEDEEE GEQRAQIEDQ
DADDEDDRHS KTAGPENNAE DLEESSKDLP KCTPTFLDAK EDNDSELSQQ VSTSEEESLH
SPCPEHHLPL PPAERPILNP MLREDPPVCT EIDSETAQAV QSLTQETERE NVFQDCVESQ
EPCRNLQTYA HVSQSPQITS LDDCPQSDHS SPLSSAHSHP SQSVRSVNSP AVSILDSGYT
QISPDHSAIS VPSLHNMETS PMMDVPSVSD HSQQVVDSGF SDLGSIESTT ENYENPSSYD
STMGQNSCSY GSIPPSGLPQ SSCAVSQQMA AVNPGSCGMI QQNSLSSPPH CNVKSPQGCV
VVERPPSNSH QQQSMTQCAI PTNFATTMQL ADIPESGNPN FALYERINHQ GEYGSGHYSQ
SSGLSLAKLQ QFTNTFIEHP HSLPFNHSAS HPITSYANTP SLSSQHSSLV SLSQTPHRVP
NPQVQATVTP SPNLSSPPPM MLQRNMGIPH SQRIQPQMAS KNHISARSKS ASLSHHQQQM
YPRPPQAVAM QAPSRTLAAM PRMNMSMNIM PAPAYNVNSM NMPSLNAMNG YSMSQPMMNS
GYHGNHAYMN QSPQYSMQMG MMGTQPYPQQ PMQAPPHGNM VYTPAGHHGY MDTGISKQSL
KGPFIRR
//
