ID A0A077Z5Q9_TRITR Unreviewed; 1042 AA.
AC A0A077Z5Q9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=TTRE_0000228901 {ECO:0000313|EMBL:CDW54020.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW54020.1};
RN [1] {ECO:0000313|EMBL:CDW54020.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW54020.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; HG805877; CDW54020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077Z5Q9; -.
DR STRING; 36087.A0A077Z5Q9; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; 1.
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; IPR036388; WH-like_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:SF102; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT TRANSMEM 1004..1027
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..266
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 536..787
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 714
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1042 AA; 115914 MW; 99880971B2D433B7 CRC64;
MNAHGSAQAG RSEDNGVDSD APPDMEIVSQ LLTVIASIKY HRQQVSLERL KSKSRVLGLN
SSVIEKQLEL AVKHGLILKL LGVNGLWSYA DPNNVNIGRF RTLQVDEKTD LARIVQRVVR
DIDNCNGSNL SEIEVYVRDY YDMRVKGDLT LCQLLRDAVT KAVDQGLLVP VNGDRYQLPY
KGAASSSSNG AKHSSSMSKK KSGTTLTRCY LCKGSKRWNQ DGLSEGLLTC CSCRKRAHPS
CLHLTPELAD RLFATSSWHC STCKVCTLCR KPVHATSLRC DGCDKGYHKA CLSSLTKEKA
DSNKAGACKA DRDKVREKKI IREAARNVKS RYKKSRGRPF AGKREEAEQP SAMTPTSFDD
LDRDEGRGAL SPIDCLDSNL PQICAPTNKC GTFVQPDVSG CPQPFVDEKG VSVAPKICAD
LNVTKDNWSE PTVQPFGDTA KLSSPAKWSA RLRPRLPPEN GLDAHSSVGN DRCRSRTCKS
LISQLRAATR GRYVRRSHRQ PKLVSFEDLV TKEDEVLFKE CQRKASHNFS LCKLDVKLPY
PRAIVIGKWV IDSWFSAPYP QEYARLNKLY VCEFCLKYMK SNDVLTRHIV LKKCKLFHPP
GDEIYRKDSL SFFEVDGCKA KIYCQNLCLL AKVYLDHKTL YYDVEPFLFY VLTMNDAYGC
HLVGYFSKEK YSSQKFNVSC IVTLPPYQNK GFGRLQIAFS YLLSRKEGEV GTPEKPLSEL
GRFSYTSYWK SAIFEFFDKN RDMKACNIKQ ISETTGMTPV DIVETMQSLN MILLQGNSLK
FVIDWDAIDS YMKRARNDPK RSLLACSLPK EEEVAASADS SSQLLRQEDH SNASIDASAA
DRLVPPCSSE SATLNGPPSL REQDEEEQAN QTYATPTTPT TKKGGGRRRK RRKGKIRSEV
QSRDLTLESF DSDSDSSHVR TRARKRQSCH EAVRHRSFGG SSPDSSDSSK QMGPSKKVDG
TGKLSGAQTS ASANSASKST NKARGGSTQC RVAKAPQEQG SRTVMFLVGK GLLLPVVASF
LVVFVCLDST TLIPQGADAW KR
//