ID A7S640_NEMVE Unreviewed; 1451 AA.
AC A7S640;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE Flags: Fragment;
GN ORFNames=NEMVEDRAFT_v1g106064 {ECO:0000313|EMBL:EDO40753.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO40753.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO40753.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS469586; EDO40753.1; -; Genomic_DNA.
DR RefSeq; XP_001632816.1; XM_001632766.1.
DR STRING; 45351.A7S640; -.
DR EnsemblMetazoa; EDO40753; EDO40753; NEMVEDRAFT_v1g106064.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_000162_4_0_1; -.
DR InParanoid; A7S640; -.
DR OMA; HCTESKC; -.
DR PhylomeDB; A7S640; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd15802; RING_CBP-p300; 1.
DR CDD; cd02337; ZZ_CBP; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF1; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF06001; RING_CBP-p300; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 2..90
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 211..292
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 683..755
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 905..1275
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1277..1325
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1344..1425
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 2..90
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1344..1425
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 338..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1181
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDO40753.1"
FT NON_TER 1451
FT /evidence="ECO:0000313|EMBL:EDO40753.1"
SQ SEQUENCE 1451 AA; 165467 MW; E51DB3C26333B160 CRC64;
ADPEKRRLIQ QQLVLLLHAH KCQRREQQAA NGEMKSCNLP HCRTMKNVLN HMTTCTAGKT
CQVAHCASSR QIISHWKNCM RQDCPVCLPL KHASDRRISQ GRAPKLLLLF LLQGHLIAET
TRNNLFMGCK SHQLFSQKKE KKLLSMRRNG KKDTRMGGNR SFGETTSGTS RYFCCATINT
GQMLLVIPPV LFLVSVLMID LFPSTGSAAN RGPKEWHSHV TQDLRTHLVH KLVTAIFPTP
VNDPTAMRDK RMCNLLNYAR KVEGDMYETA NCKEEYYHLL AEKIYKIQKE LEEKRQRRLL
AQMRTTAAPQ VGQNQGDNPV KSSYFGFVLA PFHQMNGDPS ASQTLRSAQV AAVEAAQQHR
QQPQTQAQSN FSDLLSQLSP QPPCSMAGMP TASAPQLQSS MSSQQQQPQQ HQISAQQQLQ
QQQHQQQQLL QQQQQQQSQM PPQSSQSMTG GQNNTQSLTG QGQGKNQMPS PATPQSMSSE
KPSYPQSPKP STGKGAVPSP SPQRPASSMG KPDTIEKQGI TPVSESASST SQPQKNQKSV
SFCHASMYSD PSQAQSSPSP AQGTAQPVVK TEEDVKPVIT MAPASQAVTQ SASPHTTSSP
ALPIAGTVRF PFRKGGFLRH LMIKMTMGEL PFFCRLDEKT MLLAYSFLHN YLEFKSVSCL
EIALFLPEEL RLALMPTLEK LYKQEPESLP FRSPVDPKLL GCLDYFEIVR NPMDLSTIKR
KLDNGQYKNP WEYCDDVWLM FDNAWLYNRK TSRVYKYCTK LSEVFESEID PVMKLLGYCC
GRKYVFHPQV LCCFGKQLCT ITRDTAYYTY QNRQEIVTFP KCFNEIQGDM VNLGEDPTLQ
QSLIPKDQFV KLKNDHLDVE PFVECIDCGR KVHQICVLHH DLIWPTGYQC DACLNKRGVK
KKENKYTARR LQHTRLGEKI ETRVNTFLQK QGCPAEVTIR VVSSVQKQAE IKPGMKTRYE
GSGQLPEYFP YQAKALFAFE EIDGTDVCFF GMHVQEYGSD CQQPNTRRVY VSYLDSVHFF
QPRQLRTAVY HEILIGYLEH VGQIGFQMAH IWACPPSEGD DYIFHCHPPE QKIPKHKRLV
DWYKKMLDKA IMDKVVIEYK DILKQASDDG LTNPKELPYF DGDFWPNALE DSIRELDQEE
EERKANAAAA EASGKEGSKV KGNSKRSNSK KGTKSKAGSR KLSKKINGPS MELCDLSQRL
YSTMEKHREV FFVIRLNGRK TPDTSDPDPM MTCDLMDGRD AFLTLARDKH YEFSSNRRAQ
FSTMAMLVEL HNQGNDRFVY TCNLCKRPVE TRYHCNECED YDLCVPCYDE KGHEHKMERL
GFDLDVEQQS QPSKDGQPQK MNAQEERRLK IQRCIQSLVH ATHCRDINCT MLSCAKMKRV
VEHTKSCRKK TSGGCRICQE LIHLCCYHAK HCMERECVVP FCRHIKAKLR QQQLQQRFNQ
QQTLRRRMAL M
//