ID A0A2U9CPU6_SCOMX Unreviewed; 2211 AA.
AC A0A2U9CPU6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=SMAX5B_006291 {ECO:0000313|EMBL:AWP18595.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP18595.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP18595.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP026261; AWP18595.1; -; Genomic_DNA.
DR Proteomes; UP000246464; Chromosome 19.
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; 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; 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:SF29; HISTONE ACETYLTRANSFERASE P300; 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; 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:UP000246464};
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, ECO:0000313|EMBL:AWP18595.1};
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 335..421
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 568..647
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1097..1180
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1328..1705
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1707..1755
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1770..1851
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 335..421
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1770..1851
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1872..1973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2000..2020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2149..2211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1607
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1896..1910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2211 AA; 238503 MW; E4DAFE4929B63E0A CRC64;
MADNVLESGP PSAKRPKLSS PALSVSASDG NDFGSFFDLE HDLPDELINS SDLGLTNGGD
VSQLHTSLGG GIGVGGGHDA AAKHKQLSEL LRAGAPAQQG GPTSNNTAPG ASMGMMGGVN
VSPGGPQGMP PQGQQQQPGL MQQVGMVGGV AALNRAAAMM GNQKGNTGQQ GLMGGQVMNG
SPRMGYPGSA GMGNSSNLLA ETLQQQQVGQ PMGPGGQAGM RPQQPGALNK MNMMANAGPY
GGPYGQSAGQ GMPGAGLGPQ LQNKAGMPNN MANQFNMDKK LPPGQGMPGM QQQQQQHQPG
AVGGVSVGGA AAVGGAQVGI NAVGAGPGTA PPTADPEKRK LIQQQLVLLL HAHKCQRREQ
ANGEVRQCNL PHCRTMKNVL NHMTHCQAGK SCQVAHCASS RQIISHWKNC TRHDCPVCLP
LKNAGDKRNQ QSLINSAGVG LGNSLGSGVP GGQSNTPNLN PPNQIDPSSI ERAYAALGLT
YQGNQMPQQQ QQANMPNQGL QGQPGMRTLN TMGGNSMGVN GGVGGQPPNQ QSNLLPDALL
HSMNAQSLMN DVANLGSMPT ATPPSAPGMR KSWHEDITQD LRNHLVHKLV QAIFPTPDPA
ALKDRRMENL VAYARKVEGD MYESANSRAE YYHLLAEKIY KIQKELEEKR RTRLQKQGMM
PGQPGIPSSG LPQGPPSMAH SPMAPGQSPN GPHADPSMAR QAGPNQMVNR MQNPAGMSQF
GQMGMQSMGQ RSTPPLPLNS PMNQMGMGAP RMGQPNATQL QNQYLPQGQF PGSSPGLGSG
PAGMNQPGPQ NAVPQSASSA PGSMGSGSAT GAGPLPSLPP SSTGTPPNSY PHCPSIRTNS
PSPARSLTPQ PYQTPPTLPR SQTPQPQTPN TPQLPPQQQQ QTSQQQQQQQ QQQQHQLPQQ
TLGGGASSGP QAGQASSVPN QNAHVPLQLP QTPLSAKPSL TADCQESSPA SVNSSTGTSS
QLATADGSAP SQEDVKMEVK KEEEEEGPDS HGEGKGKMGK CEPDVKTEEK PEIKKEKVMA
DGCKGEPMDT SSSSVSSSAA TSEDKKPEVK KEPKDEEEGS GSTASNSSPA STQSKKKIFK
PEELRQALMP TLEALYRQDP ESLPFRQPVD PQLLGIPVRI RTSNKTNLDY FDIVKNPMDL
STIKRKLDTG QYQEPWQYVD DIWLMFNNAW LYNRKTSRVY KYCSKLAEVF EAEIDPVMQG
MGYCCGRKFE FSPQTLCCYG KQLCTIQRDA AYFSYQNRYH FCEKCFNEIQ GETVSLGDDP
SQPQTSINKE QFQRKKNDTL DPELLVECID CSRKMHQICV LHHDTIWPSG FVCDNCLKMA
NKTRKENKYA SKRLPQTKLG GYLESRVNDY LKRQNNPESG DITIRVVHVS DRVVEVKPGM
KSRFVDSGEM AESFPYRMKA LFAFEDIDGA DVCFFGMHVQ EYGADCPPPN QRRVYISYLD
SVHFFKPRHL RTAVYHEILL GYLEYVKRQG FTTGHIWACP PSEGDDYIFH CHPSDQKIPK
PKRLQEWYKK MLDKAVSERI VHDYKDIFKQ ATEDRLTSAK ELPYFEGDFW PNVLEESIKE
LEQEEEERKR EENSTSNEST DVTKGDSKNA KKKNNKKTSK NKSSLSRANK KKPGMPNVSN
DLSQKLYATM EKHKEVFFVI RLIACPTANS LPPIVDLDPM MACDLMDGRD AFLTLARDKH
LEFSSLRRSK WSSMCMLVEL HNQSQDRFVY TCNECKHHVE TRFHCTVCED YDLCITCYNI
KGHEHKMDKL GLGLDDDSNN QSAAATQSPG DSRRLSIQRC IQSLVHACQC RNANCSLPSC
QKMKRVVQHT KGCKRKTNGG CPICKQLIAL CCYHAKHCQE NKCPVPFCLN IKQKLRQQQL
QHRLQQAQML RRRMASMQRV GQPAGGPPGG PVGLPSPGNN GNTAPSTPTS VGTQPPTPQT
PTQTMPPAMQ QGMGQGTGVQ QQHVGGQQPP SQPQGQPSLQ QQQQQPSSGP PPAAVEIAMK
IQQVADAQRK MALQRQAAQA AAGLMPPHPH HQQGQGQQMG MGHPGAVGMV GPQGMPTQTA
AVAAARAHME QQQGAPPGMM VGAGGPMQQP PQQGNMPQGQ LPPQVQLQQQ RMGVTLPGAA
GGNIPQAALQ DLLRTLRSPS SPLQQQQVLN ILRSNPQLMA AFIKQRASKY KGGPGGPGTV
PGGPGPTGGP VGNVMTGGGP QLSGMAGLHG PGGSGQDPLG QNMNHNPLDI M
//
