ID   G5DZM7_9PIPI            Unreviewed;       200 AA.
AC   G5DZM7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE   Flags: Fragment;
OS   Hymenochirus curtipes (western dwarf clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Pipinae; Hymenochirus.
OX   NCBI_TaxID=8362 {ECO:0000313|EMBL:AEQ17779.1};
RN   [1] {ECO:0000313|EMBL:AEQ17779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:AEQ17779.1};
RA   Chain F.J.J., Evans B.J., Dushoff J.;
RT   "The odds of duplicate gene persistence after polyploidization.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00000780};
CC   -!- SIMILARITY: Belongs to the TFIIB family.
CC       {ECO:0000256|ARBA:ARBA00010857}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JP286591; AEQ17779.1; -; mRNA.
DR   AlphaFoldDB; G5DZM7; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR   CDD; cd20552; CYCLIN_TFIIB_rpt2; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 1.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR000812; TFIIB.
DR   InterPro; IPR023486; TFIIB_CS.
DR   InterPro; IPR013150; TFIIB_cyclin.
DR   InterPro; IPR013137; Znf_TFIIB.
DR   PANTHER; PTHR11618:SF13; TRANSCRIPTION INITIATION FACTOR IIB; 1.
DR   PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 1.
DR   Pfam; PF08271; TF_Zn_Ribbon; 1.
DR   Pfam; PF00382; TFIIB; 1.
DR   PRINTS; PR00685; TIFACTORIIB.
DR   SUPFAM; SSF47954; Cyclin-like; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS00782; TFIIB; 1.
DR   PROSITE; PS51134; ZF_TFIIB; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00469};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00469};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00469}.
FT   DOMAIN          11..42
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
FT   REGION          56..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEQ17779.1"
FT   NON_TER         200
FT                   /evidence="ECO:0000313|EMBL:AEQ17779.1"
SQ   SEQUENCE   200 AA;  21726 MW;  CFC3463D0F72F9FD CRC64;
     MASTSRVDAL PKVTCPNHPD AILVEDYRAG DMICPECGLV VGDRVIDVGS EWRTFSNDKA
     TKDPSRVGDT QNPLLSGGDL TTMIGKGTGT ASFDEFGNSK YQNRRTMSSS DRAMMNTYIA
     RKAVELDLVP GRSPISVAAA AIYMASQASA EKRTQKEIGD IAGVADVTIR QSYRLIYPRA
     PDLFPADFKF DTPVDKLPQL
//