ID A0A1S3SU29_SALSA Unreviewed; 2371 AA.
AC A0A1S3SU29;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=kat6b {ECO:0000313|RefSeq:XP_014067847.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014067847.1};
RN [1] {ECO:0000313|RefSeq:XP_014067847.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014067847.1};
RG RefSeq;
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 RefSeq; XP_014067847.1; XM_014212372.1.
DR STRING; 8030.ENSSSAP00000007681; -.
DR PaxDb; 8030-ENSSSAP00000007681; -.
DR GeneID; 106611767; -.
DR OMA; AFQHQSG; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR Bgee; ENSSSAG00000003755; Expressed in ovary and 14 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; 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:UP000087266};
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 112..185
FT /note="H15"
FT /evidence="ECO:0000259|PROSITE:PS51504"
FT DOMAIN 223..282
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 279..330
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 781..1055
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 67..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1884..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2084..2155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2180..2228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1092..1119
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 520..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1324
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1928..1955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..2011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2084..2115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2134..2155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2196..2228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 957
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 2371 AA; 261468 MW; 81EA9CF42884D05B CRC64;
MVELANPLYT EWILEAIQKI KRQKQRPSEE RICHAVATLH RLDKRTVLEQ LELSVHDGSI
LKVTNKGSVS YKDPEHPGRG VSSSTTSSLK PVSANLSVPL SKGSIWNPSD LRHVDWNKIL
RRAIEGLDDN HGSSLKNIQR YLRNQDDLSH VLDNPGFQQR LRLSAKRAVN NGRLEKNGPL
YRLNQGGSGA EGRSQRCPGA SPLALQCVTL LPHESDQLRA DPIPICSFCL GTKESNRDKR
PEQLLSCADC GSSGHPSCLK FSPELTTNVK RLRWQCIECK TCSSCRIQGK NADEMLFCDS
CDRGFHMECC NPPLSRMPKG TWVCQVCRPK ENGKKLLHKK ADEIKRRYAK PIGRPRNKLK
HRMSVSSGDG SMLARGGSGS PGRGQTLTVC STPSSGHAAS VKDATDRLAV ATSDPCWAGD
AVTFTTQFTT SSSTPSTTPP LTPTSSSSTP AVTLTVNKKT KGLIDGLSKF FTPSPVGRRS
SRAGEIIDPS ALKGSQSCSP ARKKPDTPPK LWKLTPSQSV VGLAAKSDTT PSQKLTTTTI
SPCTLPPPPP PTSLGHSPTT SLVSSSSTSA NSPQSSSSQS SVPSITSLSN HNQLKGLFDG
LSHIYATQGQ SRKKGLPCYA PPKRRHRKQD LGSCATASKI YPLIPHPPQQ RLGKKEMTKN
RLLLSSHSSH PRPGRPRGRP FKVVSHFRRS PFLKKHRTLG RLRCRVTPQK GPQETPGKGD
MTDEGRIKAE HDHGCEGELR VKQEPGFVAV SREHVTEEDV EIFTQVQELS SQRNGTMTIT
DSGRYPAVIE FGKYEIQTWH SSPYPPEYSR LQKLYLCEFC LKYMRCKNIL QRHAKKCGWF
QPPANEIYRK DDLSVFEVDG NVSKLFCQNL CLLAKLFLDH KTLYYDVEPF LFYILTKNDE
KGCHLVGYFS KEKLCQQKYN VSCIMIMPQY QRQGFGRFLI DFSYLLTRQE GQAGSPEKPL
SDLGRLSYLA YWKSVMVEYL YKQPDKHISV KGISRATGMC PHDIAATLQH LCMIDRQNGR
FVVIRRERLI QRHMEKLRAS PRLNQVDPDA LHWTPSPRLN QVDPDTLHWT PSPRLNQVDP
DALHWTPAVA LNAVLSEEER ELEMDAERLK EQASWENEER AVSYLVTSIH HPRPPTKVYS
KNPFRTYERR PTTAGDQRLH DSEECSDDED EDDSDGSPPI LTKAHAMFGV KRKRERAERA
VMLKKRGRKR RRINSSVTTE TISETTEVLN EPFDNSEDER PMPLLERTCR VGEMEEEEAE
GLRKPVKRRR GRPRLEKNID RDNREHWNEV LSKKPGRPRA VKRKKGWPKG VKRGPPKWRL
KKERKMGFKL NLYTPPETPL EAEEPHIQAE EPKEEPEDQD KASTITEEGS EPGRDLAGRD
TDMDKRLPSE PHSPMEEESP SKLSSPGVSP VASPMASSPV PSPMASRASS PVFSPVGSAM
GSPVRSPICD EPPEEDPQDS EHGDSQAPSP SKQLDHSTER SAEDDEEATH LDADDEDESR
MESTAEPEKE ERKQEPEPCQ EPPEAESCTT LTFLHPNDNN KDSERRQEGS EGMAYRREVE
RPANTGDERR DGIQEQAPTA VAAVDSDHPV DSESEESSSQ EAPRQPQQTE RDRERLAALN
PSAVLRDREE DRETAQAVQS LTQETARDTE TPQDSSSSVF HQEASHSLKT HPMVPHSPPH
TLTSLDEGCP QSDHSSPLSS AHSHPSQSVR SVSSPAVSIL ESSGGSSSGS GAGGGYTQIS
PDHGSSGGAS ISVPSSLHNM ETSPMMDVPS VSDHSSQQVV DSGFSDLGSI ESTTENYENP
SSYDSTLGGS ICGGAGGPGG PGGPPQNSCS YGPLPPSGLV QSSCAVSQQM GGVNPGSCGM
IQQNSLSSPQ HCNVKSPQGC VVVVERPPSN GQHSQRTQHS HSQHSQHSHS QTITHNPHGH
TRHTITPHNQ HPQHNQPHST PHNQHSQITQ HNPHTHPEHS QPHGVHHNQH SLHNQHGQHS
LHNQHGQHSL HNQHGQHSLH NQHSHSQQQA MTQCGMPTNF TAPIQLADIP ESGNPNLSSI
YERMNQEGYG SGHYSQPSAT FSLAKLQQLT NTLIDHPHSL PFNHSASHSH PITSYANSTS
LSSHSQHSGM VSLSQSPHPG HPRPHGVSPH PGGPQVQVQA TMTPPLTSPH PLSSPQMMLQ
RNAMGIPNIP TSQWTLQAQM APGGPKGPTH IAMRSKSAAS GLSSHPHHQQ QMYSHTRGPP
QTVTMQAPSS RTLAAMPRGM NMGTVNIMPA PGNPYNHAVS VNSMNMPSAA INHAMNGYHV
TTQGPTMMAA NGGYHSNQMS GHQMTAAYMN QSPGAQYASM QMGMMGTQPY PQQPMQAPPH
SNMYSSAGQH GYMTNTGPMS KQTLKGPFIR R
//
