ID   C5IAV4_9REOV            Unreviewed;       313 AA.
AC   C5IAV4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   18-SEP-2019, entry version 25.
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; 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
CC       of viral mRNAs. These mRNAs are capped but not polyadenylated,
CC       instead terminating in a conserved sequence 'GACC' at the 3' that
CC       is recognized by NSP3, which competes with host PABPC1 for EIF4G1
CC       binding. The interaction between NSP3 and host EIF4G1 stabilizes
CC       the EIF4E-EIF4G1 interaction, thereby facilitating the initiation
CC       of capped mRNA translation. {ECO:0000256|HAMAP-Rule:MF_04094}.
CC   -!- SUBUNIT: Homodimer. Interacts (via the coiled-coil region) with
CC       host ZC3H7B (via LD motif). Interacts with host EIF4G1.
CC       {ECO:0000256|HAMAP-Rule:MF_04094}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-
CC       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-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.550; -; 1.
DR   HAMAP; MF_04094; ROTA_A_NSP3; 1.
DR   HAMAP; MF_04090; ROTA_NSP3; 1.
DR   InterPro; IPR042519; NSP3_N.
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   Complete proteome {ECO:0000313|Proteomes:UP000145116};
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|HAMAP-Rule:MF_04094}.
FT   REGION        1    149       RNA-binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_04094}.
FT   REGION      150    206       Dimerization. {ECO:0000256|HAMAP-Rule:
FT                                MF_04094}.
FT   REGION      170    234       Interaction with host ZC3H7B.
FT                                {ECO:0000256|HAMAP-Rule:MF_04094}.
FT   REGION      208    313       Interaction with host EIF4G1.
FT                                {ECO:0000256|HAMAP-Rule:MF_04094}.
FT   COILED      166    237       {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
//