GenomeNet

Database: UniProt
Entry: Q6DD22_XENLA
LinkDB: Q6DD22_XENLA
Original site: Q6DD22_XENLA 
ID   Q6DD22_XENLA            Unreviewed;       540 AA.
AC   Q6DD22;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   22-FEB-2023, entry version 38.
DE   SubName: Full=LOC446224 protein {ECO:0000313|EMBL:AAH77807.1};
DE   Flags: Fragment;
GN   Name=LOC446224 {ECO:0000313|EMBL:AAH77807.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH77807.1};
RN   [1] {ECO:0000313|EMBL:AAH77807.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH77807.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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; BC077807; AAH77807.1; -; mRNA.
DR   AlphaFoldDB; Q6DD22; -.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR006565; BTP.
DR   InterPro; IPR009072; Histone-fold.
DR   PANTHER; PTHR46452; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 3; 1.
DR   PANTHER; PTHR46452:SF1; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 3; 1.
DR   Pfam; PF07524; Bromo_TP; 1.
DR   SMART; SM00576; BTP; 1.
PE   2: Evidence at transcript level;
FT   DOMAIN          3..79
FT                   /note="Bromodomain associated"
FT                   /evidence="ECO:0000259|SMART:SM00576"
FT   REGION          134..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..174
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         540
FT                   /evidence="ECO:0000313|EMBL:AAH77807.1"
SQ   SEQUENCE   540 AA;  58701 MW;  9A299B5F68A44AA5 CRC64;
     MCESYSRSLL RVSVAQICQA LGWDSVQVTA CDLLTDVLQR YLQQLCRGAH RYSELYGRTD
     PVLDDVGQAF KLMGVNINEL EDYIHNIEPV TFPHPIPSFP VSKNNALQFP PPGSKDAEDR
     KAYIPDYLPL IISSQEEEEE EQVPTDGGTS AEAMQVPLEE EEEEEGEMED EETVNDENYL
     SKRPLDSPET MEMPFAKRTR LMNNKGDILD GSLEPREPLS SINSQKVPSV LSPAHKLDSQ
     DLDVSSSDQI MLSPVSKSPV PPTKPSDSKS LISKTKSKGG SPGQKIKSPK ATPISSVLGS
     PIRSPKSGPK ERKSPGRAKS PKSPKSPKVP LAASLPAVKA ETPNRTPLAT LSEKIGRENI
     QVKQNQTPLD SDQLNLEIPS NKPSIADNTI EDSIDAVIAR ACAEQEPDPF EFSSGSESEG
     EVFTSPKRLS ISEPTTPKVS ASGINLGKSS STPVPASGGT SSSDISWTMD DSINEVIRKV
     SQETPANTPA NNPPCFSSPS ASPPTPEPLL KAFEDKVKLP SPVELKKKTK KEQRTKKKKK
//
DBGET integrated database retrieval system