ID A0A2U9CYJ9_SCOMX Unreviewed; 1385 AA.
AC A0A2U9CYJ9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative DNA-binding protein RFX5 {ECO:0000313|EMBL:AWP21213.1};
GN ORFNames=SMAX5B_003141 {ECO:0000313|EMBL:AWP21213.1};
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:AWP21213.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP21213.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CP026264; AWP21213.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000025791; -.
DR Proteomes; UP000246464; Chromosome 22.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR CDD; cd03760; proteasome_beta_type_4; 1.
DR Gene3D; 2.40.128.20; -; 2.
DR Gene3D; 6.10.140.1290; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR003150; DNA-bd_RFX.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR016295; Proteasome_beta4.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR InterPro; IPR039779; RFX-like.
DR InterPro; IPR040889; RFX5_N.
DR InterPro; IPR047009; RFX5_N_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12619:SF18; DNA-BINDING PROTEIN RFX5; 1.
DR PANTHER; PTHR12619; RFX TRANSCRIPTION FACTOR FAMILY; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF18326; RFX5_N; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:AWP21213.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1385
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015917451"
FT DOMAIN 825..926
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000259|PROSITE:PS51526"
FT REGION 325..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1385 AA; 150157 MW; 245D63BF974002D0 CRC64;
MTLWLSAHFL VAGLILCSSA PMPTPEECEP LLTPSSLDKM FGRWNVLVGF TGGELFSNIL
KITESSYVTF SNGSTGLVMS EENRMGGKCF SSVTNVTIDN NMATVSVVNV TSVFHVLPSS
DDCLVLSINS TLGNLENLLK FLNVSGGPAA EGSTMRSLYL MGRESTVKDS DLQMFKNQAS
CLGIPVEPGF YYDPKTDQGV FGFSRMTCAV KLLLLVAAVA IGSNTEIGSD LVDGSNSIPV
AKECDGLNKT LPRDELHQIV GDWVLVWSVT DNEKYWDDYS NISTSHVEMR LRPDNTTIWF
HERNLFLDKS CVTFILNMSS SDPAPSDPAL NMSSSDPAPS DPALNMSASD PDPAHHTLYT
ISATMEKAGV VEPYDDSGVV DVYESSSDAL VLVYTNKDGR YLLIYRREGH HSDMEQLKAA
HSDHEKRGEC LGFPVNRTLT YDGVAAGGGE APVCDVTRLL KKTLCRHFLH IFNMECGLKL
SFWEDGPRPG QFHSFPGGSS SSGPGTACGP VRHTLNPMVT GTSVLGVKFT GGVMIAADML
GSYGSLARFR NISRLMKVNN NTILGASGDY ADYQHLKQVI EQMVIDEELL GDGHSYSPKA
VHSWLTRVMY NRRSKMNPLW NTVVIGGFYN GESFLGYVDK LGVAYEAPTV ATGFGAYLAQ
PLMREVVENK VEITKQEARE LLERCLKVLY YRDARSYNKH EIAIVTEEGV EIIGPLSSET
NWDIAHLLVR MSEDQQHQRA DAPRRSEGSL EAVEGDTEPS MLLQKLKNNI SKSVQTKVDQ
ILQDVQRFSD NDKLYLYLQL PSGPGAADKS VGDSSLFNTA DQLHTCNWIR SHLEEHSDTC
LPKQDVYETY RRHCDNLQHR PLSAANFGKI IRDIFPNIKA RRLGGRGHVL MPQPSASLCT
VAVVTGVEFH NLWTDTYCYS GIRRKTVLNM PLLPNLDLKS DPAELTELVQ TYKQEVTEAA
CELICDWAQK ILKRSFDTVV EIARYLIQEH IVNPRCSQAE LVTSATLAGG PAKPHKVMKK
VAVPSRVEAD PADQKVLACV SVHFLLEGTR RLAEGSTRRQ VEAFMKQLPR ILPRSSIPDK
TQLSVRSSPP SLAPKDASGV GGASGPGGPA AAVAASGGGV KVIAMATLPQ QQGGPVPVMI
LPQGCLSYER EKVAPPPAPP PAQQQHAAAA PTSVVQKARG NIKRPLELLT SGGAAGVSAG
SANAPPVKRK RGRPRKPRPE DALPAPPLPP QAPPPAPPCH PPIITSLTGG VIQKASSSSS
SSSQPVLELV LSQLPAVSEQ RGMVVQCQPG GAVERDRHAR PLLLLQTSGN PSWELAAAAG
RTPMVETSGN PSWELAAAAG RTPMVEEERH VNLPTPPSPS SSTVVKSEED AGPEISSTSS
KREGH
//
