GenomeNet

Database: UniProt
Entry: A8B3I1_9FLAV
LinkDB: A8B3I1_9FLAV
Original site: A8B3I1_9FLAV 
ID   A8B3I1_9FLAV            Unreviewed;      1167 AA.
AC   A8B3I1;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   Flags: Fragment;
GN   Name=E {ECO:0000313|EMBL:ABM65593.1};
OS   Murray Valley encephalitis virus.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus murrayense.
OX   NCBI_TaxID=11079 {ECO:0000313|EMBL:ABM65593.1};
RN   [1] {ECO:0000313|EMBL:ABM65593.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MK6684 {ECO:0000313|EMBL:ABM65593.1};
RA   Mackenzie J.S., Hall R.A., Poidinger M., Khromykh T.I., Johansen C.A.;
RT   "Murray Valley encephalitis virus in Papua New Guinea.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC         the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC         EC=3.4.21.91; Evidence={ECO:0000256|ARBA:ARBA00024468};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00001491};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004367}; Lumenal side
CC       {ECO:0000256|ARBA:ARBA00004367}. Host endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00023443}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00023443}; Lumenal side
CC       {ECO:0000256|ARBA:ARBA00023443}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Secreted
CC       {ECO:0000256|ARBA:ARBA00004613}. Virion membrane
CC       {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004385}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF015075; ABM65593.1; -; Genomic_RNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd12149; Flavi_E_C; 1.
DR   CDD; cd17038; Flavi_M; 1.
DR   Gene3D; 1.20.1280.260; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 1.10.8.970; Flavivirus envelope glycoprotein M-like; 1.
DR   Gene3D; 2.60.260.50; Flavivirus polyprotein propeptide domain; 1.
DR   Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 1.
DR   Gene3D; 3.30.67.10; Viral Envelope Glycoprotein, domain 2; 1.
DR   Gene3D; 3.30.387.10; Viral Envelope Glycoprotein, domain 3; 1.
DR   InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR   InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR   InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR   InterPro; IPR027287; Flavi_E_Ig-like.
DR   InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR   InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR   InterPro; IPR011998; Flavi_Glycoprot_E_cen/dimer.
DR   InterPro; IPR001157; Flavi_NS1.
DR   InterPro; IPR000752; Flavi_NS2A.
DR   InterPro; IPR002535; Flavi_propep.
DR   InterPro; IPR038688; Flavi_propep_sf.
DR   InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR   InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR   InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR   InterPro; IPR014756; Ig_E-set.
DR   NCBIfam; TIGR04240; flavi_E_stem; 1.
DR   Pfam; PF21659; Flavi_E_stem; 1.
DR   Pfam; PF02832; Flavi_glycop_C; 1.
DR   Pfam; PF00869; Flavi_glycoprot; 1.
DR   Pfam; PF01004; Flavi_M; 1.
DR   Pfam; PF00948; Flavi_NS1; 1.
DR   Pfam; PF01005; Flavi_NS2A; 1.
DR   Pfam; PF01570; Flavi_propep; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|ARBA:ARBA00022510};
KW   Fusion of virus membrane with host membrane
KW   {ECO:0000256|ARBA:ARBA00022506};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Viral envelope protein {ECO:0000313|EMBL:ABM65593.1};
KW   Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW   Virion {ECO:0000256|ARBA:ARBA00022844};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   TRANSMEM        628..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        655..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..99
FT                   /note="Flavivirus polyprotein propeptide"
FT                   /evidence="ECO:0000259|Pfam:PF01570"
FT   DOMAIN          102..175
FT                   /note="Envelope glycoprotein M flavivirus"
FT                   /evidence="ECO:0000259|Pfam:PF01004"
FT   DOMAIN          178..474
FT                   /note="Envelope glycoprotein E central and dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00869"
FT   DOMAIN          477..574
FT                   /note="Glycoprotein E immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF02832"
FT   DOMAIN          577..671
FT                   /note="Flavivirus envelope glycoprotein E Stem/Anchor"
FT                   /evidence="ECO:0000259|Pfam:PF21659"
FT   DOMAIN          679..1028
FT                   /note="Non-structural protein NS1 flavivirus"
FT                   /evidence="ECO:0000259|Pfam:PF00948"
FT   DOMAIN          1040..1143
FT                   /note="Flavivirus non-structural protein NS2A"
FT                   /evidence="ECO:0000259|Pfam:PF01005"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABM65593.1"
FT   NON_TER         1167
FT                   /evidence="ECO:0000313|EMBL:ABM65593.1"
SQ   SEQUENCE   1167 AA;  127788 MW;  51F7CC7FFB6E8BDE CRC64;
     MLIGLSAALK LSTFQGKIMM TVNATDIADV IAIPTPKGPN QCWIRAIDIG FMCDDTITYE
     CPKLESGNDP EDIDCWCDKQ AVYVNYGRCT RARHSKRSRR SITVQTHGES TLVNKKDAWL
     DSTKATRYLT KTENWIIRNP GYALVAVVLG WMLGSNTGQK VIFTVLLLLV APAYSFNCLG
     MSSRDFIEGA SGATWVDLVL EGDSCITIMA ADKPTLDIRM MNIEATNLAL VRNYCYAAIV
     SDVSTVSNCP TTGESHNTKR ADHNYLCKRG VTDRGWGNGC GLFGKGSIDT CAKFTCSSSA
     AGRLILPENI KYEVGIFVHG STDSTSHGNY STQIGANQAA RFTISPNAPA ITAKMGDYGE
     VTVECEPRSG LNTEAYYVMT IGTKHFLVHR EWFNDLLLPW TSPSSTEWRN REILMEFEEP
     HATKQSVVAL GSQEGALHQA LAGAIPVEFA SSTLKLTSGH LKCRVKMEKL KLKGTTYGMC
     TEKFTFSKNP ADTGHGTVVL ELQYTGSDGP CKIPISSVAS LNDMTPVGRM VTANPYVASS
     TANAKVLVEI EPPFGDSYIV VGRGDKQINH HWHKEGSSIG KAFSTTLKGA QRLAALGDTA
     WDFGSVGGVF NSIGKAVHQV FGGAFRTLFG GMSWISQGLL GALLLWMGVN ARDKSIALAF
     LATGGVLLFL ATNVHADTGC AIDITRRELK CGSGIFIHND VEAWIDRYKY LPETPKQLAK
     VVENAHKSGI CGIRSVNRFE HQMWESVRDE LNALLKENAI DLSVVVEKQK GMYRAAPNRL
     KLTVEELDIG WKAWGKSLLF AAELANSTFV VDGPETAECP NSKRAWNSFE IEDFGFGITS
     TRVWLKLREE NTSECDSTII GTAVKGNHAV HSDLSYWIES GLNGTWKLER AIFGEVKSCT
     WPETHTLWGD AVEETELIIP VTLAGPRSKH NRREGYKVQV QGPWDEEDIK LDFDYCPGTT
     VTVSEHCGKR GPSVRTTTDS GKLVTDWCCR SCTLPPLRFT TASGCWYGME IRPMKHDEST
     LVKSRVQALN GDMIDPFQLG LLVMFLATQE VLRKRWTARL TLPAAVGALL VLLLGGITYT
     DLVRYLILVG SAFAESNNGG DVIHLALIAV FKVQPAFLVA SLTRSRWTNQ ENLVLVLGAA
     FFQMAASDLE LSIPGLLNSA ATAWMVL
//
DBGET integrated database retrieval system