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Database: UniProt
Entry: R1CGH7_EMIHU
LinkDB: R1CGH7_EMIHU
Original site: R1CGH7_EMIHU 
ID   R1CGH7_EMIHU            Unreviewed;      1179 AA.
AC   R1CGH7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=EMIHUDRAFT_469732 {ECO:0000313|EMBL:EOD21888.1};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD21888.1};
RN   [1] {ECO:0000313|EMBL:EOD21888.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD21888.1};
RG   DOE Joint Genome Institute;
RA   Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA   Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA   Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA   Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA   Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA   Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA   Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA   Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA   Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA   Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA   Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA   Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA   Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT   "Genome variability drives Emilianias global distribution.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000013827}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX   PubMed=23760476; DOI=10.1038/nature12221;
RA   Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA   Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA   Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA   Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA   Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA   Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA   Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA   Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA   Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA   Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA   Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA   Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA   Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA   van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA   Wurch L.L.;
RT   "Pan genome of the phytoplankton Emiliania underpins its global
RT   distribution.";
RL   Nature 499:209-213(2013).
RN   [3] {ECO:0000313|EnsemblProtists:EOD21888}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; KB865803; EOD21888.1; -; Genomic_DNA.
DR   RefSeq; XP_005774317.1; XM_005774260.1.
DR   STRING; 2903.R1CGH7; -.
DR   PaxDb; 2903-EOD21888; -.
DR   EnsemblProtists; EOD21888; EOD21888; EMIHUDRAFT_469732.
DR   GeneID; 17267433; -.
DR   KEGG; ehx:EMIHUDRAFT_469732; -.
DR   eggNOG; KOG1778; Eukaryota.
DR   HOGENOM; CLU_273251_0_0_1; -.
DR   OMA; CAPKHER; -.
DR   Proteomes; UP000013827; 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   CDD; cd15517; PHD_TCF19_like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR031162; CBP_P300_HAT.
DR   InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
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   SMART; SM01250; KAT11; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   PROSITE; PS51727; CBP_P300_HAT; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013827};
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:PRU00146}.
FT   DOMAIN          779..1113
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51727"
FT   DOMAIN          1112..1166
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          92..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..162
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1179 AA;  130343 MW;  00DEDEA99B995D43 CRC64;
     MGRKSVFSKR SRFGGSDLIT RIPRSDRSSS QTRHFTFFLS RYTGGGSRLD GPLAGAAQPA
     REPLQLELRS VAGRDALRQA LLAMVPQIDE LQKKRELMKR SGPPPQRPTP MGMPQQGQLP
     PGTVQPLAQP TTVQGHVLPN QPGPPPLPQP PPPIPKPVIG PVPPQRSHSQ VGLAESAVSG
     SAMLEPKMGL PPVAHPPEYK PNLGQHGGQH GMGGVNQNRK STLPVQALVH AFHCNEAGCK
     QKSCVETKQV PSGGHPGATG AAAPRRMSVP SPPDGRVSGG APRLGGVHSN NEAVRQKLRQ
     LDPAQVKRML LQHVRSCQNK QCHTCHKLRE RIKASRANNT GGGGSSHDPL QRPFGGGGIP
     PLQRPGSIGG MTAGGMEGSS NILMGGGFGG GGGFGGFPGL DGGPGLLGAG TGVGFGLQGS
     SPWVPSAQSG LQRKTKVKQR GRENIQPGLA WSSRQGDQRT ALAEGTRFSR IRLKLKGVAP
     TLAPSRSRDR KKKARADDDD GGRGEKADIK RLRRQISQKS TQDEEEEMAQ AGMDQYRVAP
     GRPASLELNK FEVGSWVEHR EDASTWRLAI VRSQQQAGGQ LQYTIQLEPV EQNRHKQTGV
     PHADLRMACS HPECKKHALH LAALPLFCDR CRKALMSTPQ QRVYFQEKEA VESGQSLRLC
     STCVGSLRAE LKSKGQAGLD AEVQKFTRDL PQGADRQSLV LETLEETALP QRAENSDAPI
     LSTDIDTRWA QCAGCFKWWH WVCAMYVETQ YKNGRPFYCR GCAPKHERLS DELQSLLENN
     DATKLTQIPM GEFIEEQVRS DLEEAKIDCT PITIRIVSSL LMNSYTPERL VEHQQALGES
     YPREFPYKSK ALLAFQKRDG LDVCLFALYV QEYGSDCPEP NKNRVYISYL DSVRYFESEP
     MGHRSTVYHS ILVAYLQWTR MLGFKYVHIW VEPPKSGDEY IFFARSDQQR KPMKREKLRE
     WYKGMLDKAK AKNVVEHYGT MHDMFNGLKS LAEIPLFHGD QWEITVPSLL GLDDEEYVSA
     PKSNKLVRMD SKDVVQKAQQ EMQHLKRHFL VAVLRDPDLS PMKDNDPVIS TDLTDSRQTF
     LGQCQMCHWQ FNTLRHAQYS TRMILNHIHN KPSYCVEDCQ RGRVEDGSFM VGCDVCDNWY
     HGDCVGISKD EANTMDSYLC ARCRALDESG GLDEGGGGS
//
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