ID H9LJA6_9REOV Unreviewed; 310 AA.
AC H9LJA6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 03-MAY-2023, entry version 23.
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; Sedoreoviridae; Rotavirus.
OX NCBI_TaxID=28875 {ECO:0000313|EMBL:AEF80033.1, ECO:0000313|Proteomes:UP000101672};
RN [1] {ECO:0000313|EMBL:AEF80033.1, ECO:0000313|Proteomes:UP000101672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RVA/human-tc/USA-DC/G2275/1980/G9P[8]
RC {ECO:0000313|EMBL:AEF80033.1};
RX PubMed=18234798; DOI=10.1128/JVI.02537-07;
RA Cao D., Santos N., Jones R.W., Tatsumi M., Gentsch J.R., Hoshino Y.;
RT "The VP7 genes of two G9 rotaviruses isolated in 1980 from diarrheal stool
RT samples collected in Washington, DC, are unique molecularly and
RT serotypically.";
RL J. Virol. 82:4175-4179(2008).
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; JF521478; AEF80033.1; -; Genomic_RNA.
DR Proteomes; UP000101672; 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 {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..146
FT /note="RNA-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT REGION 147..203
FT /note="Dimerization"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT REGION 167..231
FT /note="Interaction with host ZC3H7B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT REGION 205..310
FT /note="Interaction with host EIF4G1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
FT COILED 163..234
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04094"
SQ SEQUENCE 310 AA; 35840 MW; 5326947F00BFD8E0 CRC64;
MESTQQMVGS IINTSFEAAV VAATSTLELM GIQYDYNEVF TRVKSKFDYV MDDSGVKNNL
VGKAITIDQA LNGKFGSVAR NRNWMTDSRT VAKLDEDVNK LRMMLSSKGI DQKMRVLSAC
FSVKRIPGKS SSIIKCTRLM RDKMERGEVE VDDSFVDEKM EIDTIDWKSR YDQLEKRFES
LKQRVSEKYN NWVQKAKKVN ENMYSLQNVI SQQQNQITDL QQYCNKLETD LQNKISSLVS
SVEWYLRSME LSDDIKTDIE QQLNSIDAIN PINAIDDLES LIRNLIQDYD KTFLMLKGLV
RQCNYECTYE
//
