ID   B6URJ3_9REOV            Unreviewed;       313 AA.
AC   B6URJ3;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   03-MAY-2023, entry version 28.
DE   RecName: Full=Non-structural protein 3 {ECO:0000256|HAMAP-Rule:MF_04094};
DE            Short=NSP3 {ECO:0000256|HAMAP-Rule:MF_04094};
DE   AltName: Full=NCVP4 {ECO:0000256|HAMAP-Rule:MF_04094};
DE   AltName: Full=Non-structural RNA-binding protein 34 {ECO:0000256|HAMAP-Rule:MF_04094};
DE            Short=NS34 {ECO:0000256|HAMAP-Rule:MF_04094};
OS   Bovine rotavirus.
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10927 {ECO:0000313|EMBL:ACI48280.1};
RN   [1] {ECO:0000313|EMBL:ACI48280.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KJ56-1 {ECO:0000313|EMBL:ACI48280.1};
RA   Park S.I., Park S.H., Cho K.O.;
RT   "Molecular Characterization of G8 and G6 Bovine Rotaviruses Reveals
RT   Multispecies Reassortments in Most of the Genes.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in stimulating the translation of
CC       viral mRNAs. These mRNAs are capped but not polyadenylated, instead
CC       terminating in a conserved sequence 'GACC' at the 3' that is recognized
CC       by NSP3, which competes with host PABPC1 for EIF4G1 binding. The
CC       interaction between NSP3 and host EIF4G1 stabilizes the EIF4E-EIF4G1
CC       interaction, thereby facilitating the initiation of capped mRNA
CC       translation. {ECO:0000256|HAMAP-Rule:MF_04094}.
CC   -!- SUBUNIT: Homodimer. Interacts (via the coiled-coil region) with host
CC       ZC3H7B (via LD motif). Interacts with host EIF4G1. {ECO:0000256|HAMAP-
CC       Rule:MF_04094}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04094}.
CC   -!- SIMILARITY: Belongs to the rotavirus A NSP3 protein family.
CC       {ECO:0000256|HAMAP-Rule:MF_04094}.
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DR   EMBL; FJ206177; ACI48280.1; -; Genomic_RNA.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-UniRule.
DR   CDD; cd20714; NSP3_rotavirus; 1.
DR   Gene3D; 3.30.70.1610; -; 1.
DR   Gene3D; 1.20.5.970; Nonstructural RNA-binding protein; 1.
DR   Gene3D; 6.10.280.20; Rotavirus non-structural protein NSP3, N-terminal domain; 1.
DR   HAMAP; MF_04094; ROTA_A_NSP3; 1.
DR   HAMAP; MF_04090; ROTA_NSP3; 1.
DR   InterPro; IPR042519; NSP3_N_rotavirus.
DR   InterPro; IPR036082; NSP3_sf.
DR   InterPro; IPR002873; Rotavirus_NSP3.
DR   Pfam; PF01665; Rota_NSP3; 1.
DR   SUPFAM; SSF69903; NSP3 homodimer; 1.
DR   SUPFAM; SSF58030; Rotavirus nonstructural proteins; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW   Rule:MF_04094}; Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04094};
KW   Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04094};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_04094};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW   Rule:MF_04094}.
FT   REGION          1..149
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT   REGION          150..206
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT   REGION          170..234
FT                   /note="Interaction with host ZC3H7B"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT   REGION          208..313
FT                   /note="Interaction with host EIF4G1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT   COILED          166..237
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
SQ   SEQUENCE   313 AA;  36176 MW;  D633A13004435A72 CRC64;
     MLKMESTQQM VSSIINTSFE AAVVADTSTL ELMGIQYDYN EIFTRVKSKF DYVMDDSGVK
     NNLLGKAATI DQALNGKFGS TIRNRNWMTD SKTVAKLDED VNKLRMILSS KGIDQKMRVL
     NACFSVKRIP GKSSSVIKCT RLMKDKIERG EVEVDDSFVD EKMEIDTIDW KARYDQLEKR
     FESLKQRVNE KYNSWVQKAK KVNENMYSLQ NVISQQQNQI ADLQQYCNKL EVDLQSKISS
     LVSSVEWYLR SMELSDDVKT DIEQQLNSID AINPINAIDD LESLIRNLIQ DYDRTFLMLK
     GLVRQCNYEC TYE
//