ID F6GYH3_VITVI Unreviewed; 1740 AA.
AC F6GYH3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN OrderedLocusNames=VIT_09s0054g01780 {ECO:0000313|EMBL:CCB45009.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB45009.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- FUNCTION: Acetyltransferase enzyme. Acetylates histones, giving a
CC specific tag for transcriptional activation.
CC {ECO:0000256|ARBA:ARBA00002581}.
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|ARBA:ARBA00000780};
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DR EMBL; FN594972; CCB45009.1; -; Genomic_DNA.
DR STRING; 29760.F6GYH3; -.
DR PaxDb; 29760-VIT_09s0054g01780-t01; -.
DR EnsemblPlants; Vitvi09g01474_t001; Vitvi09g01474_P001; Vitvi09g01474.
DR Gramene; Vitvi09g01474_t001; Vitvi09g01474_P001; Vitvi09g01474.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_002956_2_0_1; -.
DR InParanoid; F6GYH3; -.
DR Proteomes; UP000009183; Chromosome 9.
DR ExpressionAtlas; F6GYH3; baseline and differential.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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 CDD; cd15614; PHD_HAC_like; 1.
DR Gene3D; 3.30.60.90; -; 2.
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; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
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; PF08214; HAT_KAT11; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
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};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 671..752
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 1124..1560
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1442..1505
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1562..1615
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1622..1705
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1740 AA; 195419 MW; 00333D4567F78E92 CRC64;
MSGQVPNQAG SQLPGLPQQN GSSLPSQIQN LGGHRNTGNM DPDIVRARKS MQVKIYEYLT
QRQSSPYDLQ PKKLADIVRR LDDVLFRSAA TKEDYANLDT LESRLHGSIK SLSLSSHNQQ
FPQAVNSSSA VSTMIPTPGM SHSGSSNLMV TSSVDTSMIA ASACNSIAPT TVNTGSLLPA
GGGSSVGIHS SSFNSSDGSL CNGYQQSTSS FSIGSGGNSM MSSMSGQRIT SQMIPTPGFN
SNNNQSYMNS ESSNNGGGFS SVESTMVSQP QQQKQHVGGQ NIRILHNLGS QRGSGIRSGL
QQKTYGFSNG ALNGGFIGNN MQLVNGPSTS DGYLSGTLYG DSSKPLQQQF DQHQRPLIQG
DGYGMNAADP SGSANFYNTV TSAGSMMNTQ NLNPVSLQSM SKTNSTLIPN QSNLHNAQQA
VHMKPQSVSQ SEKVNFQSPL SSRENLLQSH QQQQFQQQPH QFQQQFVPHQ RQQKPPSQQH
QILIKNDAFG QPQLTSDLSS QVKAELGGEH HNEILNSQVS DQFQLSELQN QFQQNSSDDH
SRGAQLHSLP SGTQEMCSSV SQNSQQIQQL LHPQQLIAES QNDFSCLSIG EQSESVLHGQ
WHPQSQGRPQ ISGNLSHDQH VQEEFRQRIT RHDEAQRNNL SSEGSIIGKT VTPRSTGESQ
LSAAACKSAN SNRERQFKNQ QRWLLFLRHA RRCAAPEGKC QDVNCITVQK LWRHMDRCNL
PQCSFPRCQH TRVLLHHHKH CRDPGCPVCI PVKNYLDLQL RARTRPGSDS GLPTPIDGSC
KSHDTVETAR LTSKASSVVE TSEDLQPSSK RMKTEQPSQS LLPESESSAV LVPVITESHV
PQDVQRQEYR HGDVSMPIKS EFTEVKMEVP VNSGQGSPKI SELKKDNLDD IYNQRPDSEP
IIYDESAGFA KEENVKLEKE NDQARQENVT QPSESIGTKS GKPKIKGVSL TELFTPEQIR
AHITGLRQWV GQSKAKAEKN QAMERSMSEN SCQLCAVEKL TFEPPPIYCS PCGARIKRNA
MYYTMGTGDT RHYFCIPCYN EARGDSVVVD GTSLPKARLE KKKNDEETEE WWVQCDKCEA
WQHQICALFN GRRNDGGQAE YTCPNCYITE IERGERKPLP QSAVLGAKDL PRTILSDHIE
QRLFKRLKQE RQERARLQGK GFDEVAGAEA LVIRVVSSVD KKLEVKQRFL EIFQEENYPT
EFPYKSKVIL LFQKIEGVEV CLFGMYVQEF GSECLFPNQR RVYLSYLDSV KYFRPEIKSV
TGEALRTFVY HEILIGYLEY CKKRGFTSCY IWACPPLKGE DYILYCHPEI QKTPKSDKLR
EWYLSMLRKA AKENIVVDLT NLYDHFFVST GECKSKVTAA RLPYFDGDYW PGAAEDMIYQ
LQQEEDGRKL HKKGTTKKTI TKRALKASGQ SDLSGNASKD LLLMHKLGET ISPMKEDFIM
VHLQHACTHC CHLMVSGNRW VCHQCKNFQL CDKCYEAEQK LEERERHPVN HRDKHLLHPV
EINDVPSDTK DKDEILESEF FDTRQAFLSL CQGNHYQYDT LRRAKHSSMM VLYHLHNPTA
PAFVTTCNIC HLDIEAGQGW RCEVCPDYDV CNACYQKDGG IDHPHKLTNH PSMADRDAQN
KEARQLRVLQ LRKMLDLLVH ASQCRSPHCQ YPNCRKVKGL FRHGIQCKTR ASGGCLLCKK
MWYLLQLHAR ACKESECHVP RCRDLKEHLR RLQQQSDSRR RAAVMEMMRQ RAAEVAGNAG
//
