ID A0A2U9CRV9_SCOMX Unreviewed; 616 AA.
AC A0A2U9CRV9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Putative cyclin-dependent serine/threonine-protein kinase DDB G0272797/DDB G0274007 {ECO:0000313|EMBL:AWP18456.1};
GN ORFNames=SMAX5B_006408 {ECO:0000313|EMBL:AWP18456.1};
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:AWP18456.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP18456.1, 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; CP026261; AWP18456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CRV9; -.
DR STRING; 52904.ENSSMAP00000003321; -.
DR Proteomes; UP000246464; Chromosome 19.
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 GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:AWP18456.1};
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};
KW Transferase {ECO:0000313|EMBL:AWP18456.1}.
FT DOMAIN 26..76
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 93..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 68359 MW; B1002136F0CCFFA0 CRC64;
MGRLIKPKLS MSGRRKREFI SDEKKDACYW EKRRKNNEAA KRSREKRRLN DMVLENRVIA
LNDENVRLRT ELLQLKLRFG LISTASYIEK SQQIGGGNNA GNGGSSSSSS SSTQYYSSGY
SSGSQVMMNS DSSETEQSGR SEGHRQLVKY SPRGSLSDMS DASSRDSPEP MPFEIKQEGD
RLEMDIADGT TTQIMFNIHR GLASVPTHHQ IQQHSQEMEA AYHSQQRQEQ QQQQLHLHQQ
QQPHQEPVAT INTVSQPAPH PPSAQRSVIL YGSSSASYPV DTLTRPRDMD LLEAQKQSSG
GSQTSVSRLP QSITGSPAET LAEVTKQLER KTLDSPSYEL SESHNEAGEI QVYRVCPLPQ
KHQQETDSSA ELLHQQAEEV NQSHLYHHLQ QSQNLYLSAH DEEPPVLTYE GGPRNEVYYR
GQSSSSSKDT SSSDGDPRSS DKDASTDDEE SPSSSCSDMG SYHNRHLTSL HHPASPLPAS
QGCAQAQGRD HQGEVKGTAL PHKLRLKHRA MSTGSCSGSG GNCSGHESPT TPPSATPPPL
PQHPYIALTL PQDIKRESPG RRQIGVDKTR AKKQEQKNTS DFQRVHWTSY AKRKGEIDPP
QFIAAAIFNV TRHART
//
