ID   NSP3_ROTSH              Reviewed;         315 AA.
AC   A2T3N5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-MAY-2023, entry version 50.
DE   RecName: Full=Non-structural protein 3 {ECO:0000255|HAMAP-Rule:MF_04094};
DE            Short=NSP3 {ECO:0000255|HAMAP-Rule:MF_04094};
DE   AltName: Full=NCVP4 {ECO:0000255|HAMAP-Rule:MF_04094};
DE   AltName: Full=Non-structural RNA-binding protein 34 {ECO:0000255|HAMAP-Rule:MF_04094};
DE            Short=NS34 {ECO:0000255|HAMAP-Rule:MF_04094};
OS   Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A)
OS   (Simian Agent 11 (isolate SI/South Africa/H96/58)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=450149;
OH   NCBI_TaxID=60710; Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=17059839; DOI=10.1016/j.virol.2006.09.024;
RA   Small C., Barro M., Brown T.L., Patton J.T.;
RT   "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O'
RT   agent.";
RL   Virology 359:415-424(2007).
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:0000255|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:0000255|HAMAP-
CC       Rule:MF_04094}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04094}.
CC   -!- SIMILARITY: Belongs to the rotavirus NSP3 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04094}.
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DR   EMBL; DQ838610; ABG75784.1; -; Genomic_RNA.
DR   RefSeq; YP_002302220.1; NC_011501.2.
DR   SMR; A2T3N5; -.
DR   GeneID; 7011355; -.
DR   KEGG; vg:7011355; -.
DR   Proteomes; UP000001119; Genome.
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; Host cytoplasm; Host-virus interaction; Reference proteome;
KW   RNA-binding; Translation regulation.
FT   CHAIN           1..315
FT                   /note="Non-structural protein 3"
FT                   /id="PRO_0000369445"
FT   REGION          1..149
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT   REGION          150..206
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT   REGION          170..234
FT                   /note="Interaction with host ZC3H7B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT   REGION          208..315
FT                   /note="Interaction with host EIF4G1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
FT   COILED          166..237
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04094"
SQ   SEQUENCE   315 AA;  36425 MW;  71029C07B95D4D21 CRC64;
     MLKMESTQQM AVSIINSSFE AAVVAATSAL ENMGIEYDYQ DIYSRVKNKF DFVMDDSGVK
     NNLIGKAITI DQALNNKFGS AIRNRNWLAD TSRAAKLDED VNKLRMMLSS KGIDQKMRVL
     NACFSVKRIP GKSSSIIKCT KLMRDKLERG EVEVDDSFVD EKMEVDTIDW KSRYEQLEQR
     FESLKSRVNE KYNNWVLKAR KMNENMHSLQ NVISQQQAHI AELQVYNNKL ERDLQNKIGS
     LTSSIEWYLR SMELDPEIKA DIEQQINSID AINPLHAFDD LESVIRNLIS DYDKLFLMFK
     GLIQRCNYQY SFGCE
//