ID   M4GDB_DANRE             Reviewed;         222 AA.
AC   Q5EAQ1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=MIF4G domain-containing protein B;
GN   Name=mif4gdb; ORFNames=zgc:110826;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).
RG   Center for eukaryotic structural genomics (CESG);
RT   "Crystal structure of an EIF4G-like protein from Danio rerio.";
RL   Submitted (AUG-2006) to the PDB data bank.
CC   -!- FUNCTION: Functions in replication-dependent translation of histone
CC       mRNAs which differ from other eukaryotic mRNAs in that they do not end
CC       with a poly-A tail but a stem-loop. May participate in circularizing
CC       those mRNAs specifically enhancing their translation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with eif4g1, eif4g2 and slbp; probably tethered by
CC       SLBP to the 3'-end of mRNAs ending with the histone stem-loop, it also
CC       interacts with eif4g1 which is bound to their 5'-end. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q5EAQ1; Q7ZU28: ddx19; NbExp=2; IntAct=EBI-16419713, EBI-16419754;
CC       Q5EAQ1; Q5EAQ1: mif4gdb; NbExp=2; IntAct=EBI-16419713, EBI-16419713;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MIF4GD family. {ECO:0000305}.
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DR   EMBL; BC090306; AAH90306.1; -; mRNA.
DR   RefSeq; NP_001013302.1; NM_001013284.1.
DR   PDB; 2I2O; X-ray; 1.92 A; A/B=2-222.
DR   PDB; 4JHJ; X-ray; 3.25 A; A/B=1-222.
DR   PDB; 4JHK; X-ray; 2.51 A; A=1-222.
DR   PDBsum; 2I2O; -.
DR   PDBsum; 4JHJ; -.
DR   PDBsum; 4JHK; -.
DR   AlphaFoldDB; Q5EAQ1; -.
DR   SMR; Q5EAQ1; -.
DR   ComplexPortal; CPX-1305; SLBP-SLIP1 complex.
DR   IntAct; Q5EAQ1; 2.
DR   STRING; 7955.ENSDARP00000124808; -.
DR   PaxDb; Q5EAQ1; -.
DR   DNASU; 503596; -.
DR   Ensembl; ENSDART00000168938; ENSDARP00000141567; ENSDARG00000102578.
DR   GeneID; 503596; -.
DR   KEGG; dre:503596; -.
DR   CTD; 503596; -.
DR   ZFIN; ZDB-GENE-050227-7; mif4gdb.
DR   eggNOG; KOG3942; Eukaryota.
DR   GeneTree; ENSGT00940000153432; -.
DR   HOGENOM; CLU_081010_1_0_1; -.
DR   InParanoid; Q5EAQ1; -.
DR   OMA; KVNSQRM; -.
DR   OrthoDB; 1168859at2759; -.
DR   PhylomeDB; Q5EAQ1; -.
DR   EvolutionaryTrace; Q5EAQ1; -.
DR   PRO; PR:Q5EAQ1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 3.
DR   Bgee; ENSDARG00000102578; Expressed in testis and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0062073; C:histone mRNA stem-loop binding complex; IPI:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008494; F:translation activator activity; IBA:GO_Central.
DR   GO; GO:0006446; P:regulation of translational initiation; IBA:GO_Central.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   Pfam; PF02854; MIF4G; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Nucleus; Reference proteome;
KW   Translation regulation.
FT   CHAIN           1..222
FT                   /note="MIF4G domain-containing protein B"
FT                   /id="PRO_0000337092"
FT   DOMAIN          3..205
FT                   /note="MIF4G"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:4JHJ"
FT   HELIX           16..27
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           34..45
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           49..54
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           56..70
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           74..88
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           90..96
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           98..114
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           126..136
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           139..142
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           145..165
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           167..183
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           189..203
FT                   /evidence="ECO:0007829|PDB:2I2O"
FT   HELIX           210..216
FT                   /evidence="ECO:0007829|PDB:2I2O"
SQ   SEQUENCE   222 AA;  25765 MW;  26059435E7469867 CRC64;
     MENSSKEDYK IQSFDLETQK LLKTALKDPG SVDLEKVSSV IVDQSLKDQV FSREAGRICY
     TIVQAEAKQT NGSVFRRNLL NRLQQEFKAR EETRKRSTQE WVCLVSFICN IFDYLKVNNM
     PMVALVHPVY DCLFRLAQSD ALKNEEEVDC LVLQLHRIGD QLEKMNVQLM DELFNLLRDG
     FLLQEDLSSM GRLLLLEILE FRAGGWKLSD TAQKYYYSEV TD