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Database: UniProt
Entry: A0A077Z5Q9_TRITR
LinkDB: A0A077Z5Q9_TRITR
Original site: A0A077Z5Q9_TRITR 
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
//
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