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Database: UniProt
Entry: W5N6I0_LEPOC
LinkDB: W5N6I0_LEPOC
Original site: W5N6I0_LEPOC 
ID   W5N6I0_LEPOC            Unreviewed;      1079 AA.
AC   W5N6I0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=SECIS binding protein 2 like {ECO:0000313|Ensembl:ENSLOCP00000016239.1};
GN   Name=SECISBP2L {ECO:0000313|Ensembl:ENSLOCP00000016239.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016239.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000016239.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   EMBL; AHAT01026092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015198522.1; XM_015343036.1.
DR   AlphaFoldDB; W5N6I0; -.
DR   STRING; 7918.ENSLOCP00000016239; -.
DR   Ensembl; ENSLOCT00000016269.1; ENSLOCP00000016239.1; ENSLOCG00000013180.1.
DR   GeneID; 102684394; -.
DR   KEGG; loc:102684394; -.
DR   CTD; 9728; -.
DR   eggNOG; ENOG502QUP4; Eukaryota.
DR   GeneTree; ENSGT00490000043356; -.
DR   HOGENOM; CLU_009625_0_0_1; -.
DR   InParanoid; W5N6I0; -.
DR   OMA; DYHSGCQ; -.
DR   OrthoDB; 253192at2759; -.
DR   Proteomes; UP000018468; Linkage group LG3.
DR   Bgee; ENSLOCG00000013180; Expressed in intestine and 13 other cell types or tissues.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR   GO; GO:0035368; F:selenocysteine insertion sequence binding; IBA:GO_Central.
DR   GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR   InterPro; IPR040051; SECISBP2.
DR   PANTHER; PTHR13284; GH01354P; 1.
DR   PANTHER; PTHR13284:SF10; SELENOCYSTEINE INSERTION SEQUENCE-BINDING PROTEIN 2-LIKE; 1.
DR   Pfam; PF01248; Ribosomal_L7Ae; 1.
DR   SUPFAM; SSF55315; L30e-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT   DOMAIN          702..794
FT                   /note="Ribosomal protein eL8/eL30/eS12/Gadd45"
FT                   /evidence="ECO:0000259|Pfam:PF01248"
FT   REGION          180..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          882..1015
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1030..1079
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..928
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..985
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        989..1007
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1045..1059
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1079 AA;  116835 MW;  F2D7ADD350486D25 CRC64;
     MDTSDNKDVK LSAEVEPFVP QKKGLESALV TMSLPGDGAG GSSAGGAEPT AIPSYLITCY
     PFVQENQPNR QLPLYNGDLR WQQPNPGPGG PYLAYPILPS PQPAVSSDYT YYQIMPAPCP
     PMMGFYQPFP APYAAPVPAA GMVSAVAADC GDRPAPPSQA FPAAGQRGRG VIRPAVLPKQ
     LPQPIRSKRP PMRSVAVQKE ISSSGPDGRS KTVLLVDASQ QTDFPGEIAS KSLLERASPL
     PWKSKARRRR ASQPAGESSS EHGASEADID SDSGYCSPKH NQAAGPASRT TDSAATAGGE
     SGVATAVSWV NVASQVTQKN WMDRSSAFLR AGRGTDLRNY TQAGYRGRAP STSCERGPAL
     QTRRPHVNRP PEAAHSAELY FEDEDEFPEL VSGGNALKIR NEQIQPKLPK NILENLPENS
     PISIVQTPIP ITTSVPKRAK SQRKKALAAA LATAQEYSEI SMEQKKLQEA LTKAAGKKSK
     TPVQLDLGDM LAALERQQQA MKARQLTNTK PLSYTVGTTA PFQSKDSGNK MSVIKSQPYT
     PPHNILDSTA PRMKRGKERE IPKVKRPTAL KKIILKEREV KKGKYSLDHS VLGPEEQADG
     ELRFTDDQSH EGVSQEENGL SMPSDASLSP ASQNSPYSIT PVSQGSPASS EIGSPMTALA
     ITKIHSRRFR EYCNQVLSKE IDESVTLLLQ ELVRFQERVY QKDPAKAKAK RRLVMGLREV
     TKHMKLQKIK CVIISPNCEK IQSKGGLDEA LYNVIAMARE QEIPFVFALG RKALGRCVNK
     LVPVSVVGIF NFSGAEGLFN KLVSLTEEAR KAYKDMVSAL EQEQAEEALK NVKKVHNHMG
     HSRNPSAASA ISFCSVISEP ISEVNEKEYE TNWRSMVESS DGLEALESER EPPGKTAGSE
     SVNNAAADAE SQASALSLPS TPTVTSAPPA CQPGKPGVAV LEKEEGRPDD TLEWASQQST
     ETGSLDGSCR DLLSSSITST ASTLVPGMLE EGEDEDEEDE EEDYTPEPIS VEVPLTSRIE
     SWVTEAQKTL ENLQLGKNQD SAEEEEGGPS EEEELESSEQ TDPVLDHKEQ PLEPKSVPC
//
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