ID A0A2A2JPG5_9BILA Unreviewed; 2166 AA.
AC A0A2A2JPG5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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};
GN ORFNames=WR25_07690 {ECO:0000313|EMBL:PAV63531.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV63531.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV63531.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV63531.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV63531.1}.
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DR EMBL; LIAE01010301; PAV63529.1; -; Genomic_DNA.
DR EMBL; LIAE01010301; PAV63531.1; -; Genomic_DNA.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0003712; F:transcription coregulator 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 CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd15557; PHD_CBP_p300; 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; 1.20.1020.10; 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; 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; 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; 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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
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 Reference proteome {ECO:0000313|Proteomes:UP000218231};
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, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00203}.
FT DOMAIN 480..573
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 712..791
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1061..1133
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1292..1671
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1727..1808
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 480..573
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1727..1808
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1533..1582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1852..2091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..249
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1575
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1852..1868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1883..1928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1946..1989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2020..2063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2077..2091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2166 AA; 236074 MW; 09F40D0CCEC3748E CRC64;
MDEPAVKKAR LDSEFDSGDG LDGLSELEKM EPLPQAGSDA ESTAPGTSKS QPMTNGSTAP
PTQSVTSTQP LGMGGPQNQP PTSGNFGPSA VPPTSSSAGS GGSSVLQELL MNQGPATSTI
NSSPRPPPQQ FGAPGSQQPP QPAFNTRSPM TSHSGPASMM SPPNSMAGPN QQVMGTQAGP
MRPPGPGNMY PGVPDQGMGP QMTGPQGGPP QQYGAGPPMM GARPPPMGYP NQGYPPQQPG
YPPPQGRGQP MQPGRGAMMN GAPPQMARGA MAGPPQRVMP PQMINGPGGG MMRHPMEQPS
YPGAPFPGPH QPRPDQYSNY PMGRGQGNYV MMPQHGGPMM MPMDPNQNGP GMGRGPMQPQ
GGPGGQMMPN MTNGGGPNMP PNQMVPGQNA PPQMGQPPSM PPTGRGQQQQ QPLVGGPNSG
MMSGPGQPVQ APQQQQQPPM GQPQGGPPQG QAPGQMPPAS SQQGPSSNQG LGGPPPGAQD
PEKRKLIQQQ LVLLLHAHKC QQREREQGGG ADGPNGRCVC SLPHCSTMKD VLQHMTTCNN
GRQCPYAHCA SSRQIIAHWK NCNREDCPVC KPLKNIQNPP HGGPGQKGLG STPGDLFTDM
NTLLGPGSVG PGSVGPRSVD LGIPAFSSPP NAGGMGQGPP SQQHINLLEG YNPGAHQNPM
SDFRQPNPPM RGQGGMIHPG AGNMGQPNLP PSMQRQPTDM HTLSFPAPEM PNVVKDWHQH
VTKDLRNHLV GKLVKAIFPS PDPNAIYDQR IKDLITYARK VEKEMFESAN DREEYYHLLA
EKIYKIQKEL QEKKNSRLVR PDGSGPGAGQ PGTSQQHSGG SSLGSDLDNI MDVHMGIQSA
SSANQQPGQQ NRPNMSAQGQ HMQGQSNWGN NNMGEMHMQG QHNQGGFNQM GGQQANQNQP
KFGTPSTQGQ NNQSMTPQIK NEPSFDESHS RAPSNASAMS NGPTSSSSLP NGMPPRQASD
AGEKRLNVKD EPMSDLTRSS TPSSSNGNNT QTASQASSAA ASQSTSSLKQ ELTAPKKEAA
AASAPKQPEV KREPTPPPGE DNVWSPDELR QFLRPVWDKL EQSEDAIPFR LPVDPHVLNI
PDYFDIIKHP MDLQTIAQRL DQGQYRNPWA FCDDIWLMFD NAWLYNRKNS KVYKYCTKLS
ELFVVLMDPV MKEMGYCCSR KLSFTPLALF CYGANLCTIA RDQPYYVYES SSTQYGVTVS
ERYTYCLKCF EGLPKEGISL SDNPGDTSNW APKEKFQLTK NNIIDPEWFE TCKYCHRKWH
RICGLYDKKV FPEGFICDTC RREKNYPKGD NRFSAKKLPH NTLSKFLEDR VNGFIRNQLK
AAADQYQVVI RTLCVQDKEV EVKPLMKAKY GPEGFPEKFP YRTKAVFAFE MIDGAEVCFF
GLHVQEYGSN CKGPNARRVY IAYLDSVHFF QPRELRTDVY HEILLGYLDY VKRLGYTMAH
IWACPPSEGD DYIFHCHPPE QKIPKPKRLQ DWYKKMLEKG VLEKTVIEFK DIYKQARDDN
LTTPMMLPYF EGDFWPNIIE DCIREANTEE AQRVKVEADE GDGEEDETGQ GTEGGKKKSS
KSKKNNLKKS NKMNKKKQGS LTGNEVADKL YSQFEKHKEV FFTIRLVTQQ NQLSIQNQPI
EDPDPLMPSE MMDGRDTFLT RARDEHWEFS SLRRAKYSTL CLCHALHESD SNKVDYTCNK
CSGQAKWHCG TCDDFDLCDA CYKLVQHEHK MEPIKSIIGD SGAESSTSNR FESIQRCIQS
LVHACQCRDA NCRRMSCHKM KRVVQHTKMC KKRVNASCPV CKQLIALCCY HAKHCSRDPC
SVPFCMNIRQ KLAEQKRSLA RRADMMMRRR MEGLHSGFSV AAAGAAAAAT STSQSGASTP
SVSTPPAYPN ASAHPPSLQG HVKGGFSQPS HSSSMGHNQM GGPSTSMPNN QMGGHDMGQG
QRYNMSSKPM MGSGRPGMGP GPMTGHQSGG QLQGQHGAGP AQQQQQQPPT MFGIRQGGPQ
QNQMGPMGMM QGQSGIGPNM GAGQRGQAPP PYGAGPGNNP NQRGGYSQMG GPNPNGPGGS
QSQPMSGSMA PPMQRNPSFG QYTPDSHMPG PGSMGGMGGP QQQQQQQGMI STNDPALNSA
IQKISQKLKT SKSSEERQTV FNDLKKSPAL FSAFLKMKGV EVWKRILRLV ISRKKQDNMT
KLAYRT
//
