ID A0A0V0US58_9BILA Unreviewed; 1289 AA.
AC A0A0V0US58;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=T09_1639 {ECO:0000313|EMBL:KRX54104.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX54104.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX54104.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX54104.1};
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 -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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:KRX54104.1}.
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DR EMBL; JYDN01000181; KRX54104.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; 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); 2.
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; IPR001841; Znf_RING.
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; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRX54104.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 95..156
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 156..219
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 302..574
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 577..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..859
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 478
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1289 AA; 145014 MW; 363291954DE5FC6C CRC64;
MNEQESGITC PDPDPTILEQ ILIAISKIKR ERQRCTLERI IHKMENAGIE AKKIEHQVNL
ACRKGLIVET PPTGDRACSY HDACLMRMPA RKVQSNRCVF CKTVRKQHKD GSVDIVLTCK
ECKKSGHASC WKVSVELAKK VIDSGENWHC EKCKSCSICE KDEQETVTLE IVRNFLLFNH
FFLQLMRIVC NSCGKGYHWN CLPTNLQSTK TLATCPACEK KSKKPSKRKA STCTVKVAKT
RGKGKAQPIV VSSDDNASPS RSMTPTLDGL PDGIISQADI ELYKLVHNEA LKCYDSLPEM
ATDRVCPPEI CVSGFYMKSW YSSPYPQEYA CLKTLYLCDF CLKYLKTQQM RFSHQHKCRL
FHPPGDEIYR QGNLSFFEVD GNKSKAYCQN LCLLAKLFID HKTLLYDVEP FLFYVLTLRD
KTGFHLVGYF SKEKFNVQKF NVSCIMTLPA FQKKGYGRFL IDFSYLLSKR EGILGTPERP
LSELGRISYE SYWRYVIMKY LSEHRNEMTL SCKDISDSTG MQMYDVFQTL QNLDMVRTQG
KKVIYLVNMN KVDKYMETHQ VHFKLDEARL RWVPPKQEAK IPEEPPNKVN QTQVELPKES
PVKSQNERSQ RRRKNQPVVP PPTIKLRKRT VRKACNEEDA SRDEQLNDEK QPEQQQPIKR
RGRRKKINVE VTNNIVTRQA TLNEIFQSTP KRKLRHRRVP EILESNNAEK EISNDNMQGC
SENAESLSRT DNNEESLMDV FESESWETNL ERLIETNQCD ENENDLKAVE NEDSSTFLLA
DSAELLSTDE KAGPSDSNFW TGSLSISTLN DEEIEAEAKQ EQLQDVNQKE EIEKGDEQRE
EVEDKEEDEI DDDDDDEKAD ESLKISAADE ESDVDTDTEI QQLTIGSMEK LSEDGPPVLL
PMTYDSCPST PHDNSASQQL TMPLLKASDN ASVNRDDSSE EALEIGNNDS PISSKLKELN
SSEQAVSEKQ PGQRKKPLSK RSSETLRNSA KSSPLEESQS VSYTPSSSVH FPTFTDYATD
STSKVTTPGS YFGQSKYPLA EEDNCINRSS DYESYTKLCS FSGELFDHHH QQQQQQQQQQ
QYSLTALNSF QSTSSAAEMQ QIMGANNPSV SMASYNPSSF TLQHGSNNNA NNSNNNSNAN
LQYSAGTLSS YYYYPSVTSN VCQPVDGDLG LSTAGLNSNF YVNPYMPFGG SSTVGYFQPN
STAATATGAS AASMTAPSNN ASPMELGVMG LPQEAHSAAV SGFQQTSAEN NLVATAAGSV
QANPTTIAGE NNLFYNNLSQ TALMSDSRR
//
