Entry sw:SHUT_ADES1

ID   SHUT_ADES1              Reviewed;         679 AA.
AC   A9CB91;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   30-NOV-2016, entry version 32.
DE   RecName: Full=Shutoff protein;
DE   AltName: Full=100 kDa protein;
DE            Short=p100K;
DE   AltName: Full=100K-chaperone protein;
DE   AltName: Full=L4-100K;
DE   AltName: Full=Shutoff protein 100K;
OS   Snake adenovirus serotype 1 (SnAdV-1).
OC   Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Atadenovirus.
OX   NCBI_TaxID=189830;
OH   NCBI_TaxID=94885; Pantherophis guttatus (Corn snake) (Elaphe guttata).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12237421;
RA   Farkas S.L., Benko M., Elo P.T., Ursu K., Dan A., Ahne W., Harrach B.;
RT   "Genetic analysis of an adenovirus isolated from corn snake (Elaphe
RT   guttata) implies common origin with the members of the proposed new
RT   genus Atadenovirus.";
RL   J. Gen. Virol. 83:2403-2410(2002).
CC   -!- FUNCTION: Protein that inhibits host translation while promoting
CC       late viral translation by ribosome shunting. Blocks host cap-
CC       dependent translation. Binds to the bipartite leader sequence of
CC       viral late mRNAs and allows ribosome shunting and efficient
CC       translation of late viral mRNAs even though conventional
CC       translation via ribosome scanning from the cap has been shut off
CC       in the host cell. During assembly, acts as a chaperone protein
CC       that helps hexon proteins assembly into trimers (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with hexon protein;
CC       this interaction allows chaperoning and trimerization of hexon
CC       proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative
CC       cycle.
CC   -!- PTM: Phosphorylated. Tyrosine phosphorylation enhances
CC       preferential binding to bipartite leader mRNAs and allows ribosome
CC       shunting (By similarity). {ECO:0000250}.
CC   -!- PTM: Might be cleaved by the viral protease. {ECO:0000250}.
CC   -!- MISCELLANEOUS: All late proteins expressed from the major late
CC       promoter are produced by alternative splicing and alternative
CC       polyadenylation of the same gene giving rise to non-overlapping
CC       ORFs. A leader sequence is present in the N-terminus of all these
CC       mRNAs and is recognized by the viral shutoff protein to provide
CC       expression although conventional translation via ribosome scanning
CC       from the cap has been shut off in the host cell (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenoviridae shutoff protein family.
CC       {ECO:0000305}.
DR   EMBL; DQ106414; ABA47241.1; -; Genomic_DNA.
DR   RefSeq; YP_001552258.1; NC_009989.1.
DR   GeneID; 10973872; -.
DR   KEGG; vg:10973872; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019060; P:intracellular transport of viral protein in host cell; IEA:InterPro.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0039704; P:viral translational shunt; ISS:UniProtKB.
DR   InterPro; IPR003381; Adeno_100.
DR   Pfam; PF02438; Adeno_100; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus; Host cytoplasm;
KW   Host gene expression shutoff by virus; Host-virus interaction;
KW   Inhibition of eukaryotic host translation factors by virus;
KW   Late protein; Phosphoprotein; RNA-binding; Translational shunt;
KW   Transport.
FT   CHAIN         1    679       Shutoff protein.
FT                                /FTId=PRO_0000425937.
FT   MOD_RES     564    564       Phosphotyrosine; by host. {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        11    573       ipfam:Adeno_100 [T]
SQ   SEQUENCE   679 AA;  76109 MW;  DAB506228A31602E CRC64;
     MAAEGERQNL LSKHLERQVK ILQSICKNDS EACNLLDLGY ILEKNLFAPA DSRKADSGPD
     PQLNFFPPFL TPECLALHYP FFLTTSIPPS CKGNRSGTDT YSQFCSRSSC LEDIPDPSEW
     DDSLGNVSLM AELKENQKLA PLEEDSPRTT AVDESKCSSK QSYSYPALTF PPQVQKILFD
     YLIGESQDPN DLDSEYKLAF TDEDLPQEGQ AEKTKQRETL GAVATFGAVL LSIQRLFTHP
     VVIKNTQESL HYTFLHGFVR MVHLLTEVNL SEFVTFHGLT HRNRLNNPVQ HRQLEGADRF
     DYILDTIYLY LVFAWQTAMD IWSQTIDEET ERNLRERVKS LKPELAGANY AEACSLVSNT
     VFPPLLREAL VVNIPDFVNQ TQLANFRLFI NNKSNVPASV CPALPSDFIP LTYEESHPVL
     WAHVMLLRLA AFLLNHGQYV QAPDESSISL PLCDCNLCAP HRMPCYNPML LNEILSIGKF
     EVRGPDTEGK GFSLTPQVFA NAYMEKFYSE DFHPHQVVLY KDDKAQFKTE PTAAVIREPK
     LLALIRESQT RREKSILKRG GGRYLDPQTG EVLGESSHGI GEELQDGPSY GEKPSHDLPS
     YGKQNPVAGR GLQAAGERVR RDAGSPSQPT EQLGRRTPQR GGTGRDKRGR GRGGRSATPD
     PRQETAEKES LQGTRRESS
//