ID A0A2D0T1T1_ICTPU Unreviewed; 2391 AA.
AC A0A2D0T1T1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=crebbpb {ECO:0000313|RefSeq:XP_017348869.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017348869.1};
RN [1] {ECO:0000313|RefSeq:XP_017348869.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017348869.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_017348869.1; XM_017493380.3.
DR GeneID; 108279275; -.
DR KEGG; ipu:108279275; -.
DR CTD; 567111; -.
DR OrthoDB; 5490807at2759; -.
DR Proteomes; UP000221080; Chromosome 2.
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:SF1; HISTONE ACETYLTRANSFERASE; 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 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 318..404
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 557..636
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1033..1105
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1263..1640
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1642..1690
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1705..1786
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 318..404
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1705..1786
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1496..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1816..1913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..2006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2131..2154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2170..2200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2239..2348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1542
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1818..1841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1850..1891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1908
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1990..2006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2239..2295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2296..2319
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2391 AA; 263240 MW; E50F0D2840D84592 CRC64;
MADNIMDMGP PNAKRPKLNS PALSSSDGPD LGSLFDLEND LPDELIPNGE AVLPSMPTNG
DGGVAGRMGA IMADAATKHK QLSQLLQSGS GGQPGMGSQL STLCKSPLGQ ASPSHSSQPQ
KSVAASSGPG NSGSPGMSIN TGFNQTVLNS GQSHGLMGQN MAQQGQMLNG MMGPGGRGRM
APGMQYQGQT MQGAPVGGGG APGVTGVSMA GGVLAETLTQ GAPQMGVHNS ISPQQGGNMN
KMGLGATNGP FGQQYAQGAV QQITSAGVNV QLQSKAALSN SLQPTLKGAS SVQNLLHQQV
PAVNMMPGQG APAAPTADPE KRKLIQQQLV LLLHAHKCQR REQANGEVRS CALPHCRTMK
NVLNHMTHCQ AGKSCQVAHC ASSRQIISHW KNCTRQDCPV CLPLKTASDK RNQQPMLNPT
NAGLQVPVGI STMGPSQPSA QISNTTNIDP SSMKRAYAAL GLPYGNHSAT QTQAQVLGQQ
TPQTQPHQQP LRPMNSLGTN QMNLGGNGMS VPTSDQTNLH TDSPLPSSLN NNQLMPDGSG
ASGMGNLPST AVPSMPGMKK AWHEHVTQDL RNHLVHKLVQ AIFPTPDPAA LKDRRMENLV
AYARKVEGDM YESANSRDEY YHFLAEKIYK IQKELEEKRK SRLQKQPPLG TQGVQQTGIP
QPNAMGPAQA TRTANGSVPM SSVSNQMVNR MKVPQGMNQF NPMAMQNVPM SQSPVGSRAA
SPMNHLPQLN MSSVSPMVMS PSRMMQAQGM MEGHANNMVG QTPNQNQFMN QTHFPTSTGG
LNVNFAQQAG QAGGTQPQQQ NSNLSLNALG SLAPQPAMCS TPPPPASTPV GPNLQHMAQP
STPVSAGNQA STTHIPHPPS RLCSSPNPSQ PLPSLPHPEP PIQIQQPRSE KAQHPATPLD
QAAANMDNRV LTPASVAEMH SQPEFTVAVS KAVPEEDDLD LENGKKLPKL KTEDEDVKPV
SIKKEEPENV EPKQEPMETE DKKPEVKIEA KQEENGDATS TTSSTQSSQT FKKIFKPEEL
RQALMPTLES LYRQDPESLP FRQPVDPMLL GIPDYFDIVK NPIDLSTIKR KLDTGQYQEP
WQYVDDIWLM FNNAWLYNRK TSRVYKYCSK LAEVFEQEID PVMQGLGYCC GRKYEFSPQT
LCCYGKQLCT ISRDGTYYSY QNSSPKYGLL ADRYHFCEKC FNEIQGDNVT LGDDPAQSQT
MISKDQFEKK KNDMLDPEPF VECKDCGRKM HQICVLHYDV IWPSGFFCDN CLKKSGKTRK
ENKFSAKRLQ ITRLGTYIED RVNKYLKRQN HPDAGEVFVR VVASSDKMVD VKPGMKSRFV
DSGEMAENFP YRTKALFAFE EVDGVDVCFF GMHVQEYGSD CPFPNTRRVY ISYLDSIHFF
RPRLLRTAVY HEILIGYLEY VKKLGYVTGH IWACPPSEGD DYIFHCHPPD QKIPKPKRLQ
EWYRKMLDKA FAERILHDYK DIFKQATEDR IKSAYELPYF EGDFWPNVLE ESIKELEQEE
EERKKEESTA SSETVEGTQA DSKNAKKKNN KKTNKNKSSM SRANKKKPGM PNVANDLSQK
LYATMEKHKE VFFVIHLYAG PVINTLPPIM DPDPLLTCDL MDGRDAFLTL ARDKHWEFSS
LRRCKWSTMC MLVELHNQGQ DRFVYTCNEC KHHVETRWHC TVCEDFDLCI NCYNSKGHEH
QMVKWGLGLD DDNSNQNSEA SKSPQESRRL SIQRCIQSLV HACQCRNANC SLPSCQKMKR
VVQHTKGCKR KTNGGCPVCK QLIALCCYHA KHCPENKCPV PFCLNIKHKL RQQQLQQRLQ
QAQLMRRRMA LMQGRTMQKP LPSPSSGAPG TPNSQQQQPS TPQTPQPLPN QPQVSNQNMA
AMPQAFANNG RSSQPPTPGS QGKQGPQSSP RHQQPSPLPM PPQPTTPQQQ PTLAALQVAR
SIEMTTKSKQ QPQPDFRVNI NGMPMNQSRM VAPMQMMGPR GPQQGMQSGS WGAGMQGPMQ
NPQAPQPQQV PTQPSTMVSQ QPQVTQSPQQ SPLMQRAMIQ QQQPRPIQGV MPLQPVPPQA
PQQIDVAQRG AGSSIAPGAL QELLRKLKSP SSPQQQQQVL NILKLNPHLM AAFIKQRTAK
YQASQPQQAQ QQQNPQAMIG VQTGLQNMSA MQSAPVMRPG MQPQQALGPQ GQLMNAAHNG
NQQLYRRQLM RQMQQQQQQG ALAPGQGRFP QPQSTASYSQ IRMQQQLTMG SGPMMQGVAQ
IGQPGMNMDP TQNMMQQRML QQQLPQQMLK QQIGSPPQAT SMSPQPHMLP GQQQGSHLPG
QTMVNALSNQ VRSPAPVQSP RPPSQQPPHS SPSPRMQPQP SPQHTSLHSS SPHPALIGPM
TGSMEQGHLC TPEQSTMLSQ LNTPNHRGLT NDLSMVGDTT GDTLEKFVEG L
//
