ID E7BKX2_9REOV Unreviewed; 313 AA.
AC E7BKX2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 03-MAY-2023, entry version 22.
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:ADB27996.1};
OS Rotavirus A giraffe/UCD/IRL/2007.
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=705080 {ECO:0000313|EMBL:ADB27996.1};
RN [1] {ECO:0000313|EMBL:ADB27996.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24582453; DOI=10.1016/j.vetmic.2014.01.012;
RA O'Shea H., Mulherin E., Matthijnssens J., McCusker M.P., Collins P.J.,
RA Cashman O., Gunn L., Beltman M.E., Fanning S.;
RT "Complete genomic sequence analyses of the first group A giraffe rotavirus
RT reveals close evolutionary relationship with rotaviruses infecting other
RT members of the Artiodactyla.";
RL Vet. Microbiol. 170:151-156(2014).
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; GQ428138; ADB27996.1; -; Genomic_RNA.
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|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..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; 36390 MW; 51FAD8DA4BAF11FC CRC64;
MLKMESTQQM ASSIINTSFE AAVVAATSTL ELMGIQYDYN EVYTRVKSKF DYIMDDSGVK
NNLLGKAATI DQALNGKFGS AVRNRNWMAD TKTTARLDED VNKLRMMLSS KGIDQKMRVL
NACFSVKRVP GKSSSIIKCT RLMRDKIERG EVEVDDSFVE EKMEVDTIDW KSRYEQLEKR
FESLKQRVNE KYTSWVQKAK KVNENMYSLQ NVISQQQSQI ADLQHYCNKL EVDLQNKISS
LVSSVEWYMK SMELPDEIKT DIEQQLNSID IINPINAIDD FESLIRNIIL DYDRIFLMFK
GLMRQCNYEY TYE
//
