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Reviewed, UniProtKB/Swiss-Prot Q5UCB8 (POLG_DEN4S)

Last modified February 9, 2010. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Genome polyprotein
Cleaved into the following 14 chains:
    1- Recommended name:
            Protein C
        Alternative name(s):
            Core protein
            Capsid protein
    2- Recommended name:
            prM
    3- Recommended name:
            Peptide pr
    4- Recommended name:
            Small envelope protein M
        Alternative name(s):
            Matrix protein
    5- Recommended name:
            Envelope protein E
    6- Recommended name:
            Non-structural protein 1
                Short name=NS1
    7- Recommended name:
            Non-structural protein 2A
                Short name=NS2A
    8- Recommended name:
            Non-structural protein 2A-alpha
    9- Recommended name:
            Serine protease subunit NS2B
        Alternative name(s):
            Non-structural protein 2B
            Flavivirin protease NS2B regulatory subunit
    10- Recommended name:
            Serine protease/NTPase/helicase NS3
              EC=3.4.21.91
              EC=3.6.1.15
              EC=3.6.1.-
        Alternative name(s):
            Flavivirin protease NS3 catalytic subunit
            Non-structural protein 3
    11- Recommended name:
            Non-structural protein 4A
                Short name=NS4A
    12- Recommended name:
            Peptide 2k
    13- Recommended name:
            Non-structural protein 4B
                Short name=NS4B
    14- Recommended name:
            Methyltransferase/RNA-directed RNA polymerase NS5
              EC=2.7.7.48
              EC=2.1.1.56
              EC=2.1.1.57
        Alternative name(s):
            Non-structural protein 5
OrganismDengue virus type 4 (strain Singapore/8976/1995) (DENV-4) [Complete proteome]
Taxonomic identifier408687 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Dengue virus group
Virus hostAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Culex albopictus) [TaxID: 7160]
Homo sapiens (Human) [TaxID: 9606]
Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700]

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Protein attributes

Sequence length3387 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Protein C packages viral RNA to form a viral nucleocapsid, and promotes virion budding By similarity.

prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated By similarity.

Envelope protein E binds cell surface receptor and is involved in membrane fusion between virion and target cell. Synthesized as an homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes By similarity.

Non-structural protein 1 is slowly secreted from mammalian cells, but not from mosquito cells. Secreted form elicits protective immune response and plays an essential role in RNA replication. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome By similarity.

Non-structural protein 2B is a required cofactor for the serine protease function of NS3 By similarity.

Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction By similarity.

Non-structural protein 4A plays a role in RNA replication. Enhances inhibition of cell antiviral response by non-structural protein 4B By similarity.

Non-structural protein 4B prevent the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways By similarity.

RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions By similarity.

Catalytic activity

Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

NTP + H2O = NDP + phosphate.

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.

S-adenosyl-L-methionine + m7G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA.

Subunit structure

prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. Envelope protein E forms homodimers. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form an heterodimer. NS3 interacts with unphosphorylated NS5 By similarity.

Subcellular location

Protein C: Virion By similarity.

Peptide pr: Secreted By similarity.

Small envelope protein M: Virion membrane; Single-pass type I membrane protein By similarity.

Envelope protein E: Virion membrane; Single-pass type I membrane protein By similarity.

Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity.

Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane By similarity.

Non-structural protein 2A: Host endoplasmic reticulum membrane By similarity.

Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

Serine protease/NTPase/helicase NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

Non-structural protein 4A: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: The C-terminal transmembrane domain of non-structural protein 4B is presumably reoriented after cleavage on the lumenal side By similarity.

Methyltransferase/RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus By similarity.

Domain

Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals By similarity.

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins. The nascent protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3 By similarity.

RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization By similarity.

Envelope protein E and non-structural protein 1 are N-glycosylated By similarity.

Miscellaneous

The virion is assembled in the endoplasmic reticulum lumen, transported by vesicles to the Golgi, then transported again to the cell membrane where it is released outside the cell.

Sequence similarities

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 peptidase S7 domain.

Contains 1 RdRp catalytic domain.

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Ontologies

Keywords
   Biological processRNA replication
Transcription
Transcription regulation
   Cellular componentCapsid protein
Envelope protein
Host endoplasmic reticulum
Host membrane
Host nucleus
Membrane
Secreted
Virion
   DomainTransmembrane
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Viral nucleoprotein
   Molecular functionHelicase
Hydrolase
Methyltransferase
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Ribonucleoprotein
Serine protease
Transferase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological processRNA metabolic process

Inferred from electronic annotation. Source: InterPro

methylation

Inferred from electronic annotation. Source: InterPro

regulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, RNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular componentextrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

double-stranded RNA binding

Inferred from electronic annotation. Source: InterPro

mRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9999Protein C
PRO_0000268117
Propeptide100 – 11314ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity
PRO_0000268118
Chain114 – 279166prM
PRO_0000268119
Chain114 – 20491Peptide pr
PRO_0000268120
Chain205 – 27975Small envelope protein M
PRO_0000268121
Chain280 – 774495Envelope protein E
PRO_0000268122
Chain775 – 1126352Non-structural protein 1
PRO_0000268123
Chain1127 – 1344218Non-structural protein 2A
PRO_0000268124
Chain1127 – ?Non-structural protein 2A-alphaPRO_0000304549
Chain1345 – 1474130Serine protease subunit NS2B
PRO_0000268125
Chain1475 – 2092618Serine protease/NTPase/helicase NS3
PRO_0000268126
Chain2093 – 2219127Non-structural protein 4A
PRO_0000268127
Peptide2220 – 224223Peptide 2k
PRO_0000268128
Chain2243 – 2487245Non-structural protein 4B
PRO_0000268129
Chain2488 – 3387900Methyltransferase/RNA-directed RNA polymerase NS5
PRO_0000268130

Regions

Topological domain1 – 100100Cytoplasmic Potential
Transmembrane101 – 12121 Potential
Topological domain122 – 237116Extracellular Potential
Transmembrane238 – 25821 Potential
Topological domain259 – 2646Cytoplasmic Potential
Transmembrane265 – 28521 Potential
Topological domain286 – 724439Extracellular Potential
Transmembrane725 – 74521 Potential
Topological domain746 – 7516Cytoplasmic Potential
Transmembrane752 – 77221 Potential
Topological domain773 – 1155383Extracellular Potential
Transmembrane1156 – 117621 Potential
Topological domain1177 – 1446270Cytoplasmic Potential
Transmembrane1447 – 146721 Potential
Topological domain1468 – 2191724Lumenal Potential
Transmembrane2192 – 221221 Potential
Topological domain2213 – 22197Cytoplasmic Potential
Transmembrane2220 – 223920 Potential
Topological domain2240 – 2343104Lumenal Potential
Transmembrane2344 – 236421 Potential
Topological domain2365 – 240945Cytoplasmic Potential
Transmembrane2410 – 243021 Potential
Topological domain2431 – 245525Lumenal Potential
Transmembrane2456 – 247621 Potential
Topological domain2477 – 3387911Cytoplasmic Potential
Domain1654 – 1810157Helicase ATP-binding
Domain1820 – 1987168Helicase C-terminal
Domain3016 – 3166151RdRp catalytic
Nucleotide binding1667 – 16748ATP Potential
Motif1758 – 17614DEAH box By similarity

Sites

Active site15251Charge relay system; for serine protease NS3 activity By similarity
Active site15491Charge relay system; for serine protease NS3 activity By similarity
Active site16091Charge relay system; for serine protease NS3 activity By similarity
Active site25481For 2'-O-methyltransferase activity By similarity
Active site26331For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity
Active site26681For 2'-O-methyltransferase activity By similarity
Active site27041For 2'-O-methyltransferase activity By similarity
Site99 – 1002Cleavage; by serine protease NS3 By similarity
Site113 – 1142Cleavage; by host signal peptidase By similarity
Site204 – 2052Cleavage; by host furin By similarity
Site279 – 2802Cleavage; by host signal peptidase By similarity
Site774 – 7752Cleavage; by host signal peptidase By similarity
Site1126 – 11272Cleavage; by host By similarity
Site1344 – 13452Cleavage; by serine protease NS3 By similarity
Site1474 – 14752Cleavage; by serine protease NS3 By similarity
Site2092 – 20932Cleavage; by serine protease NS3 By similarity
Site2219 – 22202Cleavage; by host signal peptidase By similarity
Site2242 – 22432Cleavage; by serine protease NS3 By similarity
Site2487 – 24882Cleavage; by serine protease NS3 By similarity

Amino acid modifications

Glycosylation1821N-linked (GlcNAc...); by host Potential
Glycosylation3461N-linked (GlcNAc...); by host Potential
Glycosylation4321N-linked (GlcNAc...); by host Potential
Glycosylation9811N-linked (GlcNAc...); by host Potential
Glycosylation22971N-linked (GlcNAc...); by host Potential
Glycosylation23011N-linked (GlcNAc...); by host Potential
Glycosylation24531N-linked (GlcNAc...); by host Potential
Disulfide bond282 ↔ 309 By similarity
Disulfide bond339 ↔ 400 By similarity
Disulfide bond353 ↔ 384 By similarity
Disulfide bond371 ↔ 395 By similarity
Disulfide bond464 ↔ 564 By similarity
Disulfide bond581 ↔ 612 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5UCB8-1 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: E2B3ABCE29A6A857

FASTA3,387378,484
        10         20         30         40         50         60 
MNQRKKVVRP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI TFLRVLSIPP 

        70         80         90        100        110        120 
TAGILKRWGQ LKKNKAIKIL IGFRKEIGRM LNILNGRKRS TMTLLCLIPT VMAFHLSTRD 

       130        140        150        160        170        180 
GEPLMIVAKH ERGRPLLFKT TEGINKCTLI AMDLGEMCED TVTYKCPLLV NTEPEDIDCW 

       190        200        210        220        230        240 
CNLTSTWVMY GTCTQSGERR REKRSVALTP HSGMGLETRA ETWMSSEGAW KHAQRVESWI 

       250        260        270        280        290        300 
LRNPGFALLA GFMAYMIGQT GIQRTVFFVL MMLVAPSYGM RCVGVGNRDF VEGVSGGAWV 

       310        320        330        340        350        360 
DLVLEHGGCV TTMAQGKPTL DFELTKTTAK EVALLRTYCI EASISNITTA TRCPTQGEPY 

       370        380        390        400        410        420 
LKEEQDQQYI CRRDVVDRGW GNGCGLFGKG GVVTCAKFSC SGKITGNLVQ IENLEYTVVV 

       430        440        450        460        470        480 
TVHNGDTHAV GNDTSNHGVT ATITPRSPSV EVKLPDYGEL TLDCEPRSGI DFNEMILMEM 

       490        500        510        520        530        540 
KKKTWLVHKQ WFLDLPLPWT AGADTSEVHW NYKERMVTFK VPHAKRQDVT VLGSQEGAMH 

       550        560        570        580        590        600 
SALAGATEVD SGDGNHMFAG HLKCKVRMEK LRIKGMSYTM CSGKFSIDKE MAETQHGTTV 

       610        620        630        640        650        660 
VKVKYEGAGA PCKVPIEIRD VNKEKVVGRV ISSTPLAENT NSVTNIELEP PFGDSYIVIG 

       670        680        690        700        710        720 
VGNSALTLHW FRKGSSIGKM FESTYRGAKR MAILGETAWD FGSVGGLFTS LGKAVHQVFG 

       730        740        750        760        770        780 
SVYTTMFGGV SWMVRILIGF LVLWIGTNSR NTSMAMTCIA VGGITLFLGF TVQADMGCVV 

       790        800        810        820        830        840 
SWSGKELKCG SGIFVADNVH TWTEQYKFQP ESPARLASAI LNAHKDGVCG IRSTTRLENV 

       850        860        870        880        890        900 
MWKQITNELN YVLWEGGHDL TVVAGDVKGV LTKGKRALTP PVNDLKYSWK TWGKAKIFTP 

       910        920        930        940        950        960 
EARNSTFLID GPDTSECPNE RRAWNFLEVE DYGFGMFTTN IWMKFREGSS EVCDHRLMSA 

       970        980        990       1000       1010       1020 
AIKDQKAVHA DMGYWIESSK NQTWQIEKAS LIEVKTCLWP KTHTLWSNGV LESQMLIPKS 

      1030       1040       1050       1060       1070       1080 
YAGPFSQHNY RQGYATQTVG PWHLGKLEID FGECPGTTVT IQEDCDHRGP SLRTTTASGK 

      1090       1100       1110       1120       1130       1140 
LVTQWCCRSC TMPPLRFLGE DGCWYGMEIR PLSEKEENMV KSQVTAGQGT SETFSMGLLC 

      1150       1160       1170       1180       1190       1200 
LTLFMEECLR RRVTRKHMIL VVVITLCAII LGGLTWMDLL RALIMLGDTM SGRIGGQVHL 

      1210       1220       1230       1240       1250       1260 
AIMAVFKMSP GYVLGVFLRK LTSRETALMV IGMAMTTVLS IPHDLMELID GISLGLILLK 

      1270       1280       1290       1300       1310       1320 
IVTQFDNTQV GTLALSLTFI RSTMPLVMAW RTIMAVLFVV TLIPLCRTSC LQKQSHWVEI 

      1330       1340       1350       1360       1370       1380 
TALILGAQAL PVYLMTLMKG ASRRSWPLNE GIMAVGLVSL LGSALLKNDV PLAGPMVAGG 

      1390       1400       1410       1420       1430       1440 
LLLAAYVMSG SSADLSLEKA ANVQWDEMAD ITGSSPIIEV KQDEDGSFSI RDVEETNMIT 

      1450       1460       1470       1480       1490       1500 
LLVKLALITV SGLYPLAIPV TMTLWYMWQV KTQRSGALWD VPSPAATQKA ALSEGVYRIM 

      1510       1520       1530       1540       1550       1560 
QRGLFGKTQV GVGIHIEGVF HTMWHVTRGS VICHETGRLE PSWADVRNDM ISYGGGWRLG 

      1570       1580       1590       1600       1610       1620 
DKWDKEEDVQ VLAIEPGKNP KHVQTKPGLF KTLTGEIGAV TLDFKPGTSG SPIINRKGKV 

      1630       1640       1650       1660       1670       1680 
IGLYGNGVVT KSGDYVSAIT QAERIGEPDY EVDEDIFRKK RLTIMDLHPG AGKTKRILPS 

      1690       1700       1710       1720       1730       1740 
IVREALKRRL RTLILAPTRV VAAEMEEALR GLPIRYQTPA VKSEHTGREI VDLMCHATFT 

      1750       1760       1770       1780       1790       1800 
TRLLSSTRVP NYNLIVMDEA HFTDPSSVAA RGYISTRVEM GEAAAIFMTA TPPGTTDPFP 

      1810       1820       1830       1840       1850       1860 
QSNSPIEDIE REIPERSWNT GFDWITDYQG KTVWFVPSIK AGNDIANCLR KSGKKVIQLS 

      1870       1880       1890       1900       1910       1920 
RKTFDTEYPK TKLTDWDFVV TTDISEMGAN FRAGRVIDPR RCLKPVILPD GPERVILAGP 

      1930       1940       1950       1960       1970       1980 
IPVTPASAAQ RRGRIGRNPA QEDDQYVFSG DPLKNDEDHA HWTEAKMLLD NIYTPEGIIP 

      1990       2000       2010       2020       2030       2040 
TLFGPEREKT QAIDGEFRLR GEQRKTFVEL MRRGDLPVWL SYKVASAGIS YKDREWCFTG 

      2050       2060       2070       2080       2090       2100 
ERNNQILEEN MEVEIWTREG EKKKLRPKWL DARVYADPMA LKDFKEFASG RKSITLDILT 

      2110       2120       2130       2140       2150       2160 
EIASLPTYLS SRAKLALDNI VMLHTTEKGG RAYQHALNEL PESLETLMLV ALLGAMTAGT 

      2170       2180       2190       2200       2210       2220 
FLFFMQGKGI GKLSMGLITI AVASGLLWVA ELQPQWIAAS IILEFFLMVL LIPEPEKQRT 

      2230       2240       2250       2260       2270       2280 
PQDNQLIYVI LTILTIIGLI AANEMGLIEK TKTDFGFYQV KTETTILDVD LRPASAWTLY 

      2290       2300       2310       2320       2330       2340 
AVATTILTPM LRHTIENTSA NLSLAAIANQ AAVLMGLGKG WPLHRVDLGV PLLAMGCYSQ 

      2350       2360       2370       2380       2390       2400 
VNPTTLTASL VMLLVHYAII GPGLQAKATR EAQKRTAAGI MKNPTVDGIT VIDLEPISYD 

      2410       2420       2430       2440       2450       2460 
PKFEKQLGQV MLLVLCAGQL LLMRTTWAFC EVLTLATGPI LTLWEGNPGR FWNTTIAVST 

      2470       2480       2490       2500       2510       2520 
ANIFRGSYLA GAGLAFSLIK NAQTPRRGTG TTGETLGEKW KRQLNSLDRK EFEEYKRSGI 

      2530       2540       2550       2560       2570       2580 
IEVDRTEAKS ALKDGSKIKH AVSRGSSKIR WIVERGMVKP KGKVVDLGCG RGGWSYYMAT 

      2590       2600       2610       2620       2630       2640 
LKNVTEVRGF TKGGPGHEEP IPMATYGWNL VKLHSGVDVF YKPTEQVDTL LCDIGESSSN 

      2650       2660       2670       2680       2690       2700 
PTIEEGRTLR VLKMVEPWLS SKPEFCIKVL NPYMPTVIEE LEKLQRKHGG NLVRCPLSRN 

      2710       2720       2730       2740       2750       2760 
STHEMYWVSG ASGNIVSSVN TTSKMLLNRF TTRHRKPTYE KDVDLGAGTR SVSTETEKPD 

      2770       2780       2790       2800       2810       2820 
MTIIGRRLQR LQEEHKETWH YDQENPYRTW AYHGSYEAPS TGSASSMVNG VVKLLTKPWD 

      2830       2840       2850       2860       2870       2880 
VIPMVTQLAM TDTTPFGQQR VFKEKVDTRT PQPKPGTRMV MTTTANWLWT LLGKKKNPRL 

      2890       2900       2910       2920       2930       2940 
CTREEFISKV RSNAAIGAVF QEEQGWTSAS EAVNDSRFWE LVDKERALHQ EGRCESCVYN 

      2950       2960       2970       2980       2990       3000 
MMGKREKKLG EFGRAKGSRA IWYMWLGARF LEFEALGFLN EDHWFGRENS WSGVEGEGLH 

      3010       3020       3030       3040       3050       3060 
RLGYILEDID KKDGDLMYAD DTAGWDTRIT EDDLQNEELI TEQMAPHHKI LAKAIFKLTY 

      3070       3080       3090       3100       3110       3120 
QNKVVKVLRP TPRGAVMDII SRKDQRGSGQ VGTYGLNTFT NMEVQLIRQM EAEGVITQDD 

      3130       3140       3150       3160       3170       3180 
MQNPKGLKER VEKWLKECGV DRLKRMAISG DDCVVKPLDE RFSTSLLFLN DMGKVRKDIP 

      3190       3200       3210       3220       3230       3240 
QWEPSKGWKN WQEVPFCSHH FHKIFMKDGR SLVVPCRNQD ELIGRARISQ GAGWSLRETA 

      3250       3260       3270       3280       3290       3300 
CLGKAYAQMW SLMYFHRRDL RLASMAICSA VPTEWFPTSR TTWSIHAHHQ WMTTEDMLKV 

      3310       3320       3330       3340       3350       3360 
WNRVWIEDNP NMTDKTPVHS WEDVPYLGKR EDLWCGSLIG LSSRATWAKN IHTAITQVRN 

      3370       3380 
LIGKEEYVDY MPVMKRYSAP SESEGVL

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References

[1]"Dengue virus type 4 strain Singapore 8976/95, complete genome."
Yoong L.F., Tan T., Anwar A., August T.J., Too H.P.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY762085 Genomic RNA. Translation: AAV31422.1.

3D structure databases

HSSPHSSP built from PDB template 2BHR based on UniProtKB Q91H74.
ModBaseSearch...

Family and domain databases

InterProIPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR000069. Env_glycoprot_M_flavivir.
IPR013754. Flav_glyE_dim.
IPR001122. Flavi_capsidC.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flv_glyE_Ig-like.
IPR014412. Gen_Poly_FLV.
IPR011999. GlycoprotE_cen/dimer_Flavivir.
IPR011998. GlycoprotE_cen/dimer_vir.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR014756. Ig_E-set.
IPR001850. Peptidase_S7.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_RrmJ/FtsJ.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]
Gene3DG3DSA:2.60.98.10. Flav_glyE_dim. 1 hit.
G3DSA:2.60.40.350. Flv_glyE_Ig-like. 1 hit.
PfamPF01003. Flavi_capsid. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
PIRSFPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTSM00487. DEXDc. 1 hit.
[Graphical view]
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. False negative.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePOLG_DEN4S
AccessionPrimary (citable) accession number: Q5UCB8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 7, 2004
Last modified: February 9, 2010
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents