ID A0A3Q3WL57_MOLML Unreviewed; 2221 AA.
AC A0A3Q3WL57;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000018446.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000018446.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR STRING; 94237.ENSMMOP00000018446; -.
DR Ensembl; ENSMMOT00000018746.1; ENSMMOP00000018446.1; ENSMMOG00000013964.1.
DR OMA; MEYTCNK; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:UniProt.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR CDD; cd15647; PHD_CBP; 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; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking 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; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_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:SF34; CREB-BINDING PROTEIN; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 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; SSF69125; Nuclear receptor coactivator interlocking domain; 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 Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
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 311..416
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 491..570
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 985..1057
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1205..1582
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1584..1632
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1647..1728
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 311..416
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1647..1728
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 118..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1755..1876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..2212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..833
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1484
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1860..1876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1992..2031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2062..2125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2126..2149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2150..2167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2177..2199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2221 AA; 242940 MW; FB3C6690BC95BFAA CRC64;
MCWLAVCSVV IGKKGLLIDG NQFLFPSFSF LFLDLVSLFD LENDLPDELI PNGDLGMTSN
GGPAGGGPGL SSIVPDAAAK HKQLSELLRP GSSSILGGGI QQGGMVGAQL GAVLGKSPLG
QSSTNHQSPQ VQKGGVATGQ GNGSTGMGFN QTMLNSGQSH GVMGQAGQVM NGTLGPAGRG
RPGMQYQGQG MQASQGPGVG GSVLAETLTQ GGTQLGTHNA LNAQQAGNIN KMGMTGAPFS
QQYGQAGVKQ MGAAGVNGQQ LQNKTALSNN LPQFPAELKG AGCVPNLMQQ QVASVGIMPG
AGGVSPGPTA DPEKRKLIQQ QLVLLLHAHK CQRREQANGE VRACALPHCR TMKNVLNHMT
HCQAGKSCQA MLGSPGAGLQ NAINTVGPGQ PSATAINSAT HIDPSSMQRA YAALGLPYGN
QSPSQVQGQS PIQQNLQGAQ HQQLRNMNPL GTEQMKIRSF FASVFSQLMP DGSVGGGMGN
LPTATPLSAA GVRKAWHEHV TQDLRTHLVH KLVQAIFPTP DPAALKDRRM ENLVAYARKV
EGDMYESANS RDEYYHFLAE KIYKIQKELE EKRRSRLQKQ PGMVGNAGPQ QPVMAQSNTM
DGPVSMPNMP NQIMNRMQVS QGINQFNPMA MQNAQMSQAP MGARAPSPMN HPQQMNMSSV
PAMGMSPSRM PQTQGMMGSH PNNMVAQPAN QSQFLPQGQF PVAAGGAVNV NVSLGQPITQ
PAVTQVRILY NSNLPVNALG SLGSQLPCGP AAQTNLRATP PPNSSANLQP QQQHHHASAQ
AQGPPRTPTP ASVGGPSTTP THAPSSLPGP PPAISTTPEP SLPPTPQQPQ TEPPSQMQQP
TSVKAQHPST PLSQAAASLD NRVPSPAFVA ELSSQQALPD MSSTETKLQV KDEEDDSNFA
KKQLDIKMED DETKPPLVKE EPDTVEPKQE KMEMEEKKPE IKAEPKEEEE SGANTTSATS
QNRKKIFKPE ELRQALMPTL EALYRQDPES LPFRQPVDPM LLGIPDYFDI VKNPIDLSTI
KRKLDTGQYQ EPWQYVDDVW LMFNNAWLYN RKTSRVYKHC TKLAEVFEAE IDPVMQGLGY
CCGRKYEFSP QTLCCYGKQL CTISRDGTYY SYQNRYHFCE KCFNEIQGNS VTLGDDPAQS
QTMISKEQFE KKKNDMLDSE PFVECKDCGR KMHQICVLHY EVIWPSGFIC DSCLKKSGKT
RKENKFSARR LQSTRLGTYI EDRVNKYLKR QNHPEAGEVF VRVVASSDKT VEIKPGMKSR
FVDSGEMMES FPYRTKALFA FEEIDGVDVC FFGMHVQEYG SECPFPNTRR VYISYLDSIH
FFKPRMLRTA VYHEILIGYL EYVKKLGYVT GHIWACPPSE GDDYIFHCHP PDQKIPKPKR
LQEWYRKMLD KAFAERIIHD YKDIFKQATE DRLTSANELP YFEGDFWPNV LEESIKELEQ
EEEERKKEEN TASSETTEGP HADSKNAKKK NNKKTNKNKS SISRANKKKP GMPNVANDLS
QKLYATMEKH KEVFFVIHLH AGPVINTLPP IMDPDPLLTC DLMDGRDAFL TLARDKHWEF
SSLRRCKWST MCMLVELHNQ GQDRFVYTCN ECKHHVETRW HCTVCEDYDL CINCYNSKGH
EHQMVKWGLG IDDDSNGQGG EASKSPQESR RLSIQRCIQS LVHACQCRNA NCSLPSCQKM
KRVVQHTKGC KRKTNGGCPV CKQLIALCCY HAKHCQENKC PVPFCLNIKH KLRQQQLQHR
LQQAQMMRRR MATMAGRGMP MPSPPTSAAP DTPNSVQQPN TPQTPQPMAN QPQQQPPPNP
TNIAQGFPNN GRGSQPPTPI SQVMQAMQQG QWGPGMQNPM RNTQGHQQQG PPQPGPMGPQ
QVQGTPMAQQ GQLMQRPMMP QQQGLQMPGV MPPQGPSQQG MTPQQQNMPR GLPGNIAPSA
LQELLRTLKS PSSPQQQQQV LTILKSNPHL MAAFIKQRTA GDGASTAVSS AGSGPGNGSH
GPPRADDECW SKRQSSNVPQ TAGGMPQGHG QFPQQQPGPA SYSQLRMQQQ MAMQGGGGPM
GQLPPTSQMG QPGMGIDGPQ NLLQQRMLQQ QQQQQQMLKQ QMGSPAQANS MSPQPHMLQG
QAQGGAHLPG QTMASTLGNQ VRSPAPVQSP RPPSQQPPHS SPSPRIQPQP SPQHSTLHSS
SPHPSLGGPM SGSMEQGRMG TPEQSAMLPQ LNTPNRGGLS NDMGMVGDTT GDTLEKFVEG
L
//
