ID   C5IAV4_9REOV            Unreviewed;       313 AA.
AC   C5IAV4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   29-SEP-2021, entry version 34.
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   Rotavirus A.
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=28875 {ECO:0000313|EMBL:ACR56744.1, ECO:0000313|Proteomes:UP000145116};
RN   [1] {ECO:0000313|Proteomes:UP000145116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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: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; FJ816613; ACR56744.1; -; Genomic_RNA.
DR   Proteomes; UP000145116; 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   Gene3D; 6.10.280.20; -; 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; SSF69903; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_04094};
KW   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;  36262 MW;  9DECF22F4233F5D1 CRC64;
     MLKMESTQQM ASSIINSSFE AAVVAATSTL ELMGTQYDYN EVYTRVKSKF DFVMDDSGVK
     NNLMGKAVTI DQALNGKFGS AIRNRNWMID SRTVAKLDED VNKLRMMLSS KGIDQKMRVL
     NACFSVKRVP GKSSSIVKCT RLMKDKLERG EVEVDDSFVE EKMEIDTIDW KSRYEQLEKR
     FESLKHRVNE KYNNWVLKAR KVNENMNSLQ NVISQQQAHI NDLQMYNNKL ERDLQSKIGS
     VVSSIEWYLR SMELSDDVKS DIEQQLNSID QLNPVNAMDD FESILRNLIS DYDRLFIMFK
     GLLQQCNYTC TYE
//