ID A0A267FWU1_9PLAT Unreviewed; 1605 AA.
AC A0A267FWU1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=BOX15_Mlig032580g2 {ECO:0000313|EMBL:PAA78288.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA78288.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA78288.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA78288.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA78288.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PAA78288.1}.
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DR EMBL; NIVC01000696; PAA78288.1; -; Genomic_DNA.
DR STRING; 282301.A0A267FWU1; -.
DR Proteomes; UP000215902; 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; cd15557; PHD_CBP_p300; 1.
DR CDD; cd15802; RING_CBP-p300; 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; 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; 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 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:UP000215902};
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:PRU00228}.
FT DOMAIN 31..108
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 263..342
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 540..612
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 772..1161
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1164..1213
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1226..1307
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 31..108
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1226..1307
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 227..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1542..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1058
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1542..1560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1605 AA; 181647 MW; 5EEC1099603E1AD6 CRC64;
MRPMGAPGQS AQLPAGLQLG GQPPPGGVSG DPDKRKLIQQ QLVLLLHAHK CKQNCTLAHC
ETMRNVLHHM QQCTEGKSCP TPHCASSRQI LNHWKNCTNP SCPVCEPLKS QNRTQVQPSL
PQQQVVVPPS AQPPFRPQQP AQAIPQPASM QVHPIRPPGQ PMPLTNQGLV QSNSVPAPGY
GAIVHWQQPT TQQPQVIRMA APIPPGRTIN MTPTVPQIPN HIQQVVQPAP VPKQSPQQPQ
VQARTQPLQP PSQAVVTTSS STSAGGGWQV EVTNDMRHHL VRRIVQTIFP SPDPEAYKDP
RMTNLIEYAR KVEREMYSSA RNKEEYFHLL AEKCFKIHKE LEEKRRSRST GQTGGNAQRP
TGTGANSVQP STSQTGTPAT VSNQVPVSAT SISDGMLTMP RTTSATTVPT DCVGVGDDNT
LSAVDVAERN FIQAIKKFEN SSSGSVDVTM REEQPKGAEV VKSEVKSELD ESSVSDGRSN
ETVSLTTPVK VEVKQEDIKQ DPSEASTSQR IQPKVPRDPK RWSREELMRA FHPVYEKLYS
SEPDSFPFQR PVDPIQLGIP DYPSIVKNPM DLSTISKKLQ DGSYKDPWEV VGDFWLMFNN
AWLYNKKSSK VYRYCSTLNS IFVEEADKVM KDLGFCCATE YVFEPKVLYC FSPNSCTIQK
DQTYYTFVKK DRAAYPGLSC DKYHFCESCF VKSVEFVDIY EDISSQQPVR VPKSEFEQKK
NNIKDMEKFC QCRECGRKWH CICALHMDEI YPSGFVCPTC ISSKKIVKRE NRFTAKKLSP
CILSEFLEKR VNDFLKKKET NAGAVHIRVL SNVDKQCEVK PLMRSRFTDA GSFPESFTFR
SKAIFAFQDQ DGVDVCFFGL HVQEYGSNCP QPNCRRVYVA YLDSVHYFQP RKYRTDVYHE
ILIGYLDYVK KLGYAFAHIW SCPPSEGDDY IFHCHPADQK IPKPKRLTDW YRRMLDKALI
ERIVVDYKDI LAYALENSIV SPTDLPYFEG DFWPGSLEEL IKELDEQKKK MEEEQQQMDN
DDDDVEEGGD GSKSSKKNPK SSKNNNKRKA KSKITSTSKR KKSSYLATSG TSPDHDDLIS
KLYEGLERHR DVFFAIRLHG PQSVANLGPI DDPDTEVHLD LQDGRDNFLS MARDRHLEFS
SLRRTKYSTM VMLYELHSEA RKESFCFNCN KCQAQIETRY HCTECDDFDL CQKCYQENND
HPHELVKKTG LLVEADGPGA VDANSPEPRR VSIERCIKSL VHACTCRDAN CCQQTCMKMK
RVLYHTKVCQ KKTSNSCSLC KQLIALCCYH AKFCSEVKCA VPFCQNIKQR LKQQQLQQRL
HQAQMLRRRM NITRKGQGPP PSTAPTASSL VLQPQTSVPA VSQPAPQIPL QIMPTHLQQS
QQPPTSVYAT QPVIRQQLPA QSYATVPAGQ PAQQMWASVP GQRMPMQQPQ GQTQGQPQQQ
QLTGAARMPG QAPSPANYPR PALSAQDQAK LDNVWSQVMQ KINNPNCSQQ ERDSAKQYAE
MMRRDPHFFL QRLHTSEQRR LQQQQQQQQQ VVQAQQPQPQ VRFQQQQQQP LQQQQTYYPQ
MARMPGIAQR PPGEQLLMGQ SPSVQDPQQQ IHVQAERLGQ FADKL
//
