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Database: UniProt
Entry: A7S640_NEMVE
LinkDB: A7S640_NEMVE
Original site: A7S640_NEMVE 
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
//
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