ID   C6ZNX8_9REOV            Unreviewed;       533 AA.
AC   C6ZNX8;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   03-MAY-2023, entry version 29.
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};
GN   Name=NSP3 {ECO:0000313|EMBL:ACL36363.1};
OS   Simian rotavirus.
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10922 {ECO:0000313|EMBL:ACL36363.1};
RN   [1] {ECO:0000313|EMBL:ACL36363.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SA11-4F {ECO:0000313|EMBL:ACL36363.1};
RA   Small Brownback C., Taraporewala Z.F., Barro M., Patton J.T.;
RT   "Rotavirus Variant Encoding a Defective NSP3 Fails to Induce Nuclear
RT   Accumulation of Poly(A)-Binding Protein.";
RL   Submitted (JUL-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_04094}.
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DR   EMBL; EU934821; ACL36363.1; -; mRNA.
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; 2.
DR   Gene3D; 3.30.70.1610; -; 2.
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; 2.
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; 2.
DR   SUPFAM; SSF69903; NSP3 homodimer; 2.
DR   SUPFAM; SSF58030; Rotavirus nonstructural proteins; 2.
PE   2: Evidence at transcript level;
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..146
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT   REGION          426..533
FT                   /note="Interaction with host EIF4G1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT   COILED          171..230
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          392..451
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   533 AA;  61603 MW;  170D3D9B822A093E CRC64;
     MESTQQMAVS IINSSFEAAV VAATSALENM GIEYDYQDIY SRVKNKFDFV MDDSGVKNNL
     IGKAITIDQA LNNKFGSAIR NRNWLADTSR AAKLDEDVNK LRMMLSSKGI DQKMRVLNAC
     FSVKRIPGKS SSIIKCTKLM RDKLERGEVE VDDSFVDEKM EVDTIDWKSR YEQLEQRFES
     LKSRVNEKYN NWVLKARKMN ENMHSLQNVI SQQQAHIAEL QVYNNKLERD LQNKIGSLTS
     SIDATSALEN MGIEYDYQDI YSRVKNKFDF VMDDSGVKNN LIGKAITIDQ ALNNKFGSAI
     RNRNWLADTS RAAKLDEDVN KLRMMLSSKG IDQKMRVLNA CFSVKRIPGK SSSIIKCTKL
     MRDKLERGEV EVDDSFVDEK MEVDTIDWKS RYEQLEQRFE SLKSRVNEKY NNWVLKARKM
     NENMHSLQNV ISQQQAHIAE LQVYNNKLER DLQNKIGSLT SSIEWYLRSM ELDPEIKADI
     EQQINSIDAI NPLHAFDDLE SVIRNLISDY DKLFLMFKGL IQRCNYQYSF GCE
//