ID A0A0V1D9T2_TRIBR Unreviewed; 768 AA.
AC A0A0V1D9T2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Histone acetyltransferase {ECO:0000256|RuleBase:RU361211};
DE EC=2.3.1.48 {ECO:0000256|RuleBase:RU361211};
DE Flags: Fragment;
GN Name=KAT8 {ECO:0000313|EMBL:KRY58168.1};
GN ORFNames=T03_10452 {ECO:0000313|EMBL:KRY58168.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY58168.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY58168.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY58168.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361211};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|RuleBase:RU361211}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY58168.1}.
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DR EMBL; JYDI01000023; KRY58168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1D9T2; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|RuleBase:RU361211};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transferase {ECO:0000313|EMBL:KRY58168.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 484..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 605..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 138..385
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY58168.1"
SQ SEQUENCE 768 AA; 88296 MW; 837AC20BF722585E CRC64;
LISSTAMEDK SITQYQDRDE SEALNLQKKL DYDVNLPALK AVYYVTRSNG EKRRGKVLSI
RSANSPEDTL ECYVHYLRES SRMDEWVTLD RIGELYGMSK ATGVTDSSGL KTRSKLKHDT
LNGDISSCEE DNDERENSMV RNIDYIQMGN FRIKAWYSSR YPLQYCEKLL FICDRCAKYM
LLAKSLKEHM KRCSQRPLPG KQVYRKDNLV VIEVDGDKNK LYCQFLALLG KLFIYHKAVC
FLVQEFFFYV LYELDEENGY HMAGFYSKEK NSECNNLACI SVFPQYQKKS YGLLCHFNSN
WNPSWTRTST FRSWQTSLPI LFCMGDYSDV RQKTAIRLED IQETLQEMNI TYYYGGRHGV
FVSDELLAKC VSSPGFHEPK LKLDPLSRCA SRFLNKGCAE KILISRCLTS LPVRCVAYRH
LKTDSSSESS DILDFLNETS SDSTDGEVME SFELCNIFGD DSFVGFRWYS QLLNFVQSTL
DVPWWIAIAT TATLLRLAMF PFITVSNQRM HAAFHNATPE MVAHHRRIAQ ARKKIDLKSI
FETEADYAEY CALRNLPTIG SQLFNIIISV SIFSTQFFAL KHIAAKHCVG FETGGVYFFE
NLTDQSALLA LITSFTYFTW MFIRMEQSTS VGGKGTVTST VGRILVTTLS SGSLFIFANM
PSTTLCFCTT DFAINTALAS LYWTRWYRNV FSIPHPVIFL NSEREAFADM PLQLSEGIES
ARGKIRAVRR ANISRLRSEG NSFLLYDADE ISDMFKRWFR KLTRRKDK
//
