ID   POLG_JAEVN              Reviewed;        1440 AA.
AC   P14403; P08769;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   19-JAN-2010, entry version 77.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Protein C;
DE     AltName: Full=Core protein;
DE     AltName: Full=Capsid protein;
DE   Contains:
DE     RecName: Full=Small envelope protein M;
DE     AltName: Full=Matrix protein;
DE   Contains:
DE     RecName: Full=Envelope protein E;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=NS1;
DE   Contains:
DE     RecName: Full=Non-structural protein 2A;
DE              Short=NS2A;
DE   Contains:
DE     RecName: Full=Serine protease subunit NS2B;
DE     AltName: Full=Non-structural protein 2B;
DE     AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE   Contains:
DE     RecName: Full=Serine protease/NTPase/helicase NS3;
DE              EC=3.4.21.91;
DE              EC=3.6.1.15;
DE              EC=3.6.1.-;
DE     AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE     AltName: Full=Non-structural protein 3;
DE   Flags: Fragment;
OS   Japanese encephalitis virus (strain Nakayama).
OC   Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae;
OC   Flavivirus; Japanese encephalitis virus group.
OX   NCBI_TaxID=11076;
OH   NCBI_TaxID=8899; Ardeidae (herons).
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=308713; Culex gelidus.
OH   NCBI_TaxID=7178; Culex tritaeniorhynchus (Mosquito).
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=87236200; PubMed=3035787; DOI=10.1016/0042-6822(87)90207-8;
RA   McAda P.C., Mason P.W., Schmaljohn C.S., Dalrymple J.M., Mason T.L.,
RA   Fournier M.J.;
RT   "Partial nucleotide sequence of the Japanese encephalitis virus
RT   genome.";
RL   Virology 158:348-360(1987).
CC   -!- FUNCTION: The small proteins NS2A, NS4A and NS4B are hydrophobic,
CC       suggesting a possible membrane-related function (By similarity).
CC   -!- FUNCTION: Non-structural protein 2B is a required cofactor for the
CC       serine protease function of NS3 (By similarity).
CC   -!- FUNCTION: Serine protease NS3 displays three enzymatic activities:
CC       serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC       association with NS2B, cleaves the polyprotein (By similarity).
CC   -!- FUNCTION: RNA-directed RNA polymerase NS5 replicates the viral (+)
CC       and (-) genome, and performs the capping of genomes in the
CC       cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
CC       2'-O positions (By similarity).
CC   -!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
CC       in which each of the Xaa can be either Arg or Lys and Yaa can be
CC       either Ser or Ala.
CC   -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
CC   -!- SUBUNIT: NS3 and NS2B form a heterodimer. NS3 is the catalytic
CC       subunit, whereas NS2B strongly stimulates the latter (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Protein C: Virion (Potential). Host
CC       membrane; Single-pass membrane protein (Potential).
CC   -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion
CC       (Potential). Host membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SUBCELLULAR LOCATION: Envelope protein E: Virion (Potential). Host
CC       membrane; Multi-pass membrane protein (Potential).
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins
CC       (By similarity).
CC   -!- MISCELLANEOUS: The virion of this virus is a nucleocapsid covered
CC       by a lipoprotein envelope. The envelope contains two proteins: the
CC       protein M and glycoprotein E. The nucleocapsid is a complex of
CC       protein C and mRNA. In immature particles, there are 60
CC       icosaedrally organized trimeric spikes on the surface. Each spike
CC       consists of three heterodimers of envelope protein M precursor
CC       (prM) and envelope protein E (By similarity).
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DR   EMBL; M16574; AAA46251.1; -; Genomic_RNA.
DR   PIR; A27844; GNWVJF.
DR   SMR; P14403; 54-136, 223-621, 1351-1393.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0019058; P:viral infectious cycle; IEA:InterPro.
DR   InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR   InterPro; IPR013756; Flav_glyE_cen_dom_subdom2.
DR   InterPro; IPR013754; Flav_glyE_dim.
DR   InterPro; IPR001122; Flavi_capsidC.
DR   InterPro; IPR001157; Flavi_NS1.
DR   InterPro; IPR000752; Flavi_NS2A.
DR   InterPro; IPR000487; Flavi_NS2B.
DR   InterPro; IPR002535; Flavi_propep.
DR   InterPro; IPR000336; Flv_glyE_Ig-like.
DR   InterPro; IPR011999; GlycoprotE_cen/dimer_Flavivir.
DR   InterPro; IPR011998; GlycoprotE_cen/dimer_vir.
DR   InterPro; IPR014756; Ig_E-set.
DR   Gene3D; G3DSA:3.30.67.10; Flav_glyE_cen_2; 1.
DR   Gene3D; G3DSA:2.60.98.10; Flav_glyE_dim; 1.
DR   Gene3D; G3DSA:2.60.40.350; Flv_glyE_Ig-like; 1.
DR   Pfam; PF01003; Flavi_capsid; 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; PF01002; Flavi_NS2B; 1.
DR   Pfam; PF01570; Flavi_propep; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Capsid protein; Cleavage on pair of basic residues;
KW   Core protein; Disulfide bond; Envelope protein; Glycoprotein;
KW   Helicase; Host membrane; Hydrolase; Membrane; Nucleotide-binding;
KW   Transmembrane; Virion.
FT   CHAIN        <1     53       Protein C.
FT                                /FTId=PRO_0000037869.
FT   PROPEP       54    146
FT                                /FTId=PRO_0000037870.
FT   CHAIN       147    222       Small envelope protein M.
FT                                /FTId=PRO_0000037871.
FT   CHAIN       223    794       Envelope protein E.
FT                                /FTId=PRO_0000037872.
FT   CHAIN       795   1136       Non-structural protein 1.
FT                                /FTId=PRO_0000037873.
FT   CHAIN      1137   1301       Non-structural protein 2A.
FT                                /FTId=PRO_0000037874.
FT   CHAIN      1302   1432       Serine protease subunit NS2B.
FT                                /FTId=PRO_0000037875.
FT   CHAIN      1433  >1440       Serine protease/NTPase/helicase NS3.
FT                                /FTId=PRO_0000037876.
FT   TRANSMEM     36     56       Potential.
FT   TRANSMEM    181    201       Potential.
FT   TRANSMEM    208    224       Potential.
FT   TRANSMEM    675    695       Potential.
FT   TRANSMEM    702    722       Potential.
FT   TRANSMEM   1106   1126       Potential.
FT   TRANSMEM   1148   1168       Potential.
FT   TRANSMEM   1179   1199       Potential.
FT   TRANSMEM   1201   1221       Potential.
FT   TRANSMEM   1238   1258       Potential.
FT   TRANSMEM   1270   1290       Potential.
FT   TRANSMEM   1303   1323       Potential.
FT   TRANSMEM   1327   1347       Potential.
FT   TRANSMEM   1405   1425       Potential.
FT   CARBOHYD     68     68       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    376    376       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    852    852       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    929    929       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   DISULFID    225    252       By similarity.
FT   DISULFID    282    338       By similarity.
FT   DISULFID    296    327       By similarity.
FT   DISULFID    314    343       By similarity.
FT   DISULFID    412    509       By similarity.
FT   DISULFID    526    557       By similarity.
FT   NON_TER       1      1
FT   NON_TER    1440   1440
SQ   SEQUENCE   1440 AA;  158185 MW;  4D489A365A3C2E6E CRC64;
     SVAMKHLTSF KRELGTLIDA VNKRGRKQNK RGGNEGSIMW LASLAVVIAC AGAMKLSNFQ
     GKLLMTVNNT DIADVIVIPN PSKGENRCWV RAIDVGYMCE DTITYECPKL TMGNDPEDVD
     CWCDNQEVYV QYGRCTRTRH SKRSRRSVSV QTHGESSLVN KKEAWLDSTK ATRYLMKTEN
     WIVRNPGYAF LAAILGWMLG SNNGQRRWYF TILLLLVAPA YSFNCLGMGN RDFIEGASGA
     TWVDLVLEGD SCLTIMANDK PTLDVRMINI EAVQLAEVRS YCYHASVTDI STVARCPTTG
     EAHNEKRADS SYVCKQGFTD RGWGNGCGLF GKGSIDTCAK FSCTSKAIGR TIQPENIKYE
     VGIFVHGTTT SENHGNYSAQ VGASQAAKFT VTPNAPSITL KLGDYGEVTL DCEPRSGLNT
     EAFYVMTVGS KSFLVHREWF HDLALPWTPP SSTAWRNREL LMEFEEAHAT KQSVVALGSQ
     EGGLHQALAG AIVVEYSSSV KLTSGHLKCR LKMDKLALKG TTYGMCTEKF SFAKNPADTG
     HGTVVIELSY SGSDGPCKIP IVSVASLNDM TPVGRLVTVN PFVATSSANS KVLVEMEPPF
     GDSYIVVGRG DKQINHHWHK AGSTLGKAFS TTLKGAQRLA ALGDTAWDFG SIGGVFNSIG
     KAVHQVFGGA FRTLFGGMSW ITQGLMGALL LWMGVNARDR SIALAFLATG GVLVFLATNV
     HADTGCAIDI TRKEMRCGSG IFVHNDVEAW VDRYKYLPET PRSLAKIVHK AHKEGVCGVR
     SVTRLEHQMW EAVRDELNVL LKENAVDLSV VVNKPVGRYR SAPKRLSMTQ EKFEMGWKAW
     GKSILFAPEL ANSTFVVDGP ETKECPDEHR AWNSIEIEDF GFGITSTRVW LKIREESTDE
     CDGAIIGTAV KGHVAVHSDL SYWIESRYND TWKLERAVFG EVKSCTWPET HTLWGDGVEE
     SELIIPHTIA GPKSKHNRRE GYKTQNQGPW DENGIVLDFD YCPGTKVTIT EDCGKRGPSV
     RTTTDSGKLI TDWCCRSCSL PPLRFRTENG CWYGMEIRPV RHDETTLVRS QVDAFNGEMV
     DPFQLGLLVM FLATQEVLRK RWTARLTIPA VLGALLVLML GGITYTDLAR YVVLVAAAFA
     EANSGGDVLH LALIAVFKIQ PAFLVMNMLS TRWTNQENVV LVLGAAFFHL ASVDLQIGVH
     GILNAAAIAW MIVRAITFPT TSSVTMPVLA LLTPGMRALY LDTYRIILLV IGICSLLQER
     KKTMAKKKGA VLLGLALTST GWFSPTTIAA GLMVCNPNKK RGWPATEFLS AVGLMFAIVG
     GLAELDIESM SIPFMLAGLM AVSYVVSGKA TDMWLERAAD ISWEMDAAIT GSSRRLDVKL
     DDDGDFHLID DPGVPWKVWV LRMSCIGLAA LTPWAIVPAA FGYWLTLKTT KRGGVFWDTP
//