ID E3MHJ8_CAERE Unreviewed; 1212 AA.
AC E3MHJ8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE Flags: Fragment;
GN Name=Cre-lsy-12 {ECO:0000313|EMBL:EFP01989.1};
GN ORFNames=CRE_22791 {ECO:0000313|EMBL:EFP01989.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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; DS268445; EFP01989.1; -; Genomic_DNA.
DR RefSeq; XP_003104388.1; XM_003104340.1.
DR AlphaFoldDB; E3MHJ8; -.
DR STRING; 31234.E3MHJ8; -.
DR EnsemblMetazoa; CRE22791.1; CRE22791.1; WBGene00062912.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_269680_0_0_1; -.
DR InParanoid; E3MHJ8; -.
DR OrthoDB; 2883913at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
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; 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 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 PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF210; HISTONE ACETYLTRANSFERASE KAT7; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 244..507
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..920
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 420
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
FT NON_TER 1212
FT /evidence="ECO:0000313|EMBL:EFP01989.1"
SQ SEQUENCE 1212 AA; 135341 MW; 2E10F53F2100DDD0 CRC64;
MSSTATKRRN TNNSRCASLL MASTTPTVTR KSALVDSDDD DDDDEMSSNG ESSELAAHRS
RTPRGRYSPM LDERNRRTNS RMSALSIDTH RNTDLNADGS APSSSSAASS AFLTPDINRP
PPPTVSHKKR APHSTGRRKK MRNYPSSSAQ NSQGETELDS DDEDQRDTDN MSICNDDDSY
KIFVAIALYR TWERCSVERA CNKVHESEVP SNNRKKFQES QITVQGECEF SKSEIAEIFK
KGDQQARLPE RIQIGTVIMK TWYGSPFPAE FINVRQLYIC EFCFFYARSD LIMQNHAKRC
KLRAPPGVEI YRKDDVSVFE VDGRRQKSYC QTLCLISRMF LESKTVFYDT EPFFFYVATK
NDAHGCHFTG YFSKEKYEPD VNNLSCIMTL PCYQDQGYGR FLIDLSYALS RREGWNGGPE
QPLSDLGKKA YGGYWKNTIA VSLVKMKDRI EYGGRGICIG GEQNVRNIAN DTGINSHDVL
SVVCSLGWAK IVDPKNGGKV CTLEWDVDWD VCHAIDEQRR KAGGGGKTQF DEKCLDTSKL
QFRHSTDMRN LRLARILISS APRESNPCGN TKDIHKETGV ETAKNEATHG RISRIDERGD
RRRRATPSEK SSEDTDSHDG GNGGGDADEF ELSDWIREKK TCDRSVIDDV IDDELRSRGH
NRTTAGRNLK LELTRKVKVP TEVREITDDD ETQRVEDKKS HKKRKSFTRC ADDVPDPQKR
HEGTPDDDDQ PGPSTSKSLG RRPRSTREQV ESTASASSEQ KTPNGRGRYR RRRGGKAEDS
DDEPTEDEAV STDEEAELTT TPRPHQAPEK GKPRGRKPGK KRKSVSGKKF PPNFGVREDK
KTTEVVESEE EKVEKKQEEA ELEKTTAGSE AEEIDLLHDA IDEDMMKNYN IGTPESYHSN
SPSPAPPPEM PPPQEPPVEE DPPLLISEVN NLTVAEPVEP MDEGQPTAPP PLIADTFGDD
DDDDDDVPPN LSPQYEKNEV HEEEVEMAQV APQAPPPQQH QTPNQHSHNS HNGIHQEESY
HDSMSVAGTS SIHVTPQMMP GEMSHHYSQP NSHQQVTTPG SGGIPSCGGP ATTVPQSTYS
TPEQQTQQFM SPQMAGMPAS VSSVHSVHNN NSMEMVGGPA SLQQHTPQQQ YDIMGQMPQQ
DNNGMVVNNV SAMDQMMQQH AFNSPPMPMV VPQQPPQQPS QQQVPPQQQQ QPQVQQQQAP
QVPPTIPAPA TT
//
