ID A0A2U9BRG8_SCOMX Unreviewed; 441 AA.
AC A0A2U9BRG8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN ORFNames=SMAX5B_002028 {ECO:0000313|EMBL:AWP06206.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP06206.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP06206.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bZIP family. NFIL3 subfamily.
CC {ECO:0000256|ARBA:ARBA00006079}.
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DR EMBL; CP026250; AWP06206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BRG8; -.
DR STRING; 52904.ENSSMAP00000012905; -.
DR Proteomes; UP000246464; Chromosome 8.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd14694; bZIP_NFIL3; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR047229; NFIL3-like.
DR InterPro; IPR047106; NFIL3-like_bZIP.
DR PANTHER; PTHR15284:SF4; E4 BINDING PROTEIN 4-2-RELATED; 1.
DR PANTHER; PTHR15284; NUCLEAR FACTOR INTERLEUKIN-3-REGULATED PROTEIN; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 49..99
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 48650 MW; 969D02FDAE572574 CRC64;
MKREPGTESG SLPSPVPESG GRASRQAKGS KNNLSSRRKR EFISDEKKDA SYWEKRRKNN
EAAKRSREKR RLNDMVLENR VMALNEENVR LKTELLQLKL RFGLISTASY MEKSQQISNS
SAAMCSAAGN DGTPNSNTYL SSSGYSSASQ ATSAQRSVIL YRSSSGCYPM ESQRSEEQHP
SASKFSDCTV SVTEVAEKLE RTKTLDSPQY EYANGHAESA EELQEKYNPA AQQHRDSHHH
YSYEDQEDSR QHQNPFAPNL IHNTEEGKSS FAQHNSYLNT LDEEPPVLTY EGGPRAEGFY
QENSSAKDTS SSDGDPRSSD KEASTDDESP SSSSSDTSSY HQKAAGATGS HGECHAEVKG
TALPHKLRLK YRAMSNGAAG AQVEGLFNTS MSPSPTLPQH PYLALPSNPH SGQANGESKE
NEYADVFRPP VSERAETDNY Y
//
