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Protein

Genome polyprotein

Gene
N/A
Organism
Ilheus virus (ILHV)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Capsid protein C: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.By similarity
Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.By similarity
Peptide pr: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.By similarity
Protein prM: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Small envelope protein M: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.By similarity
Envelope protein E: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Non-structural protein 1: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).By similarity
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response.By similarity
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
Serine protease NS3: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and 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.PROSITE-ProRule annotation
Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.By similarity
Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Non-structural protein 4B: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.By similarity
RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.By similarity

Catalytic activityi

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).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.By similarity
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1548Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1572Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1632Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1954Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1957Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2532mRNA capPROSITE-ProRule annotation1
Binding sitei2535mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2536mRNA capPROSITE-ProRule annotation1
Binding sitei2538mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2543mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei2547mRNA capPROSITE-ProRule annotation1
Binding sitei2575S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2580For 2'-O-MTase activityBy similarity1
Sitei2580Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2605S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2606S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2623S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2624S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2650S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2651S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2665For 2'-O-MTase activityBy similarity1
Sitei2665Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2666S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2669mRNA capPROSITE-ProRule annotation1
Active sitei2700For 2'-O-MTase activityBy similarity1
Sitei2700Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2731mRNA capPROSITE-ProRule annotation1
Binding sitei2733mRNA capPROSITE-ProRule annotation1
Active sitei2736For 2'-O-MTase activityBy similarity1
Sitei2736Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2738S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2958Zinc 1By similarity1
Metal bindingi2962Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2967Zinc 1By similarity1
Metal bindingi2970Zinc 1By similarity1
Metal bindingi3235Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3251Zinc 2By similarity1
Metal bindingi3370Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1691 – 1698ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
Biological processActivation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host STAT2 by virus, mRNA capping, mRNA processing, Transcription, Transcription regulation, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Protein family/group databases

MEROPSiS07.001

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 5
OrganismiIlheus virus (ILHV)
Taxonomic identifieri59563 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusmosquito-borne viruses
Proteomesi
  • UP000149844 Componenti: Genome

Subcellular locationi

Capsid protein C :
  • Virion By similarity
  • Host nucleus By similarity
  • Host cytoplasm By similarity
  • host perinuclear region By similarity
Peptide pr :
  • Secreted By similarity
Small envelope protein M :
  • Virion membrane By similarity; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence analysis
  • Note: ER membrane retention is mediated by the transmembrane domains.By similarity
Envelope protein E :
  • Virion membrane Curated; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence analysis
  • Note: ER membrane retention is mediated by the transmembrane domains.By similarity
Non-structural protein 1 :
  • Secreted By similarity
  • Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.By similarity
Non-structural protein 2A :
Serine protease subunit NS2B :
Serine protease NS3 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Note: Remains non-covalently associated to serine protease subunit NS2B.PROSITE-ProRule annotation
Non-structural protein 4A :
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Note: Located in RE-associated vesicles hosting the replication complex.By similarity
Non-structural protein 4B :
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.By similarity
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Host nucleus By similarity
  • Note: Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 101CytoplasmicSequence analysisAdd BLAST100
Transmembranei102 – 122HelicalSequence analysisAdd BLAST21
Topological domaini123 – 244ExtracellularSequence analysisAdd BLAST122
Transmembranei245 – 265HelicalSequence analysisAdd BLAST21
Topological domaini266 – 270CytoplasmicSequence analysis5
Transmembranei271 – 285HelicalCuratedAdd BLAST15
Topological domaini286 – 738ExtracellularSequence analysisAdd BLAST453
Transmembranei739 – 759HelicalSequence analysisAdd BLAST21
Topological domaini760 – 765CytoplasmicSequence analysis6
Transmembranei766 – 786HelicalSequence analysisAdd BLAST21
Topological domaini787 – 1170ExtracellularSequence analysisAdd BLAST384
Transmembranei1171 – 1191HelicalSequence analysisAdd BLAST21
Topological domaini1192 – 1213CytoplasmicSequence analysisAdd BLAST22
Transmembranei1214 – 1234HelicalSequence analysisAdd BLAST21
Topological domaini1235 – 1276LumenalSequence analysisAdd BLAST42
Transmembranei1277 – 1297HelicalSequence analysisAdd BLAST21
Topological domaini1298 – 1302CytoplasmicSequence analysis5
Transmembranei1303 – 1323HelicalSequence analysisAdd BLAST21
Topological domaini1324 – 1333LumenalSequence analysis10
Transmembranei1334 – 1354HelicalSequence analysisAdd BLAST21
Topological domaini1355 – 1367CytoplasmicSequence analysisAdd BLAST13
Transmembranei1368 – 1388HelicalSequence analysisAdd BLAST21
Topological domaini1389 – 1391LumenalSequence analysis3
Transmembranei1392 – 1412HelicalSequence analysisAdd BLAST21
Topological domaini1413 – 1469CytoplasmicSequence analysisAdd BLAST57
Intramembranei1470 – 1490HelicalSequence analysisAdd BLAST21
Topological domaini1491 – 2167CytoplasmicSequence analysisAdd BLAST677
Transmembranei2168 – 2188HelicalSequence analysisAdd BLAST21
Topological domaini2189 – 2190LumenalSequence analysis2
Intramembranei2191 – 2211HelicalSequence analysisAdd BLAST21
Topological domaini2212 – 2213LumenalSequence analysis2
Transmembranei2214 – 2234HelicalSequence analysisAdd BLAST21
Topological domaini2235 – 2249CytoplasmicSequence analysisAdd BLAST15
Transmembranei2250 – 2264Helical; Note=Signal for NS4BCuratedAdd BLAST15
Topological domaini2265 – 2299LumenalSequence analysisAdd BLAST35
Intramembranei2300 – 2320HelicalSequence analysisAdd BLAST21
Topological domaini2321 – 2342LumenalSequence analysisAdd BLAST22
Transmembranei2343 – 2363HelicalSequence analysisAdd BLAST21
Topological domaini2364 – 2371CytoplasmicSequence analysis8
Transmembranei2372 – 2392HelicalSequence analysisAdd BLAST21
Topological domaini2393 – 2439LumenalSequence analysisAdd BLAST47
Transmembranei2440 – 2460HelicalSequence analysisAdd BLAST21
Topological domaini2461 – 3424CytoplasmicSequence analysisAdd BLAST964

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, Secreted, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004414861 – 3424Genome polyproteinAdd BLAST3424
ChainiPRO_00004414871 – 101Capsid protein CBy similarityAdd BLAST101
PropeptideiPRO_0000441488102 – 118ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST17
ChainiPRO_0000441489119 – 285Protein prMBy similarityAdd BLAST167
ChainiPRO_0000441490119 – 210Peptide prBy similarityAdd BLAST92
ChainiPRO_0000441491211 – 285Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000441492286 – 786Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000441493787 – 1139Non-structural protein 1By similarityAdd BLAST353
ChainiPRO_00004414941140 – 1366Non-structural protein 2ABy similarityAdd BLAST227
ChainiPRO_00004414951367 – 1497Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00004414961498 – 2115Serine protease NS3By similarityAdd BLAST618
ChainiPRO_00004414972116 – 2241Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004414982242 – 2264Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004414992265 – 2519Non-structural protein 4BBy similarityAdd BLAST255
ChainiPRO_00004415002520 – 3424RNA-directed RNA polymerase NS5By similarityAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi133N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi288 ↔ 315By similarity
Disulfide bondi345 ↔ 406By similarity
Disulfide bondi345 ↔ 401By similarity
Disulfide bondi359 ↔ 390By similarity
Disulfide bondi377 ↔ 406By similarity
Disulfide bondi377 ↔ 401By similarity
Disulfide bondi475 ↔ 573By similarity
Disulfide bondi590 ↔ 621By similarity
Disulfide bondi790 ↔ 801By similarity
Disulfide bondi841 ↔ 929By similarity
Glycosylationi916N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi965 ↔ 1009By similarity
Glycosylationi993N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi1067 ↔ 1116By similarity
Disulfide bondi1078 ↔ 1100By similarity
Disulfide bondi1078 ↔ 1099By similarity
Disulfide bondi1099 ↔ 1103By similarity
Disulfide bondi1100 ↔ 1103By similarity
Modified residuei2575PhosphoserineBy similarity1

Post-translational modificationi

Genome polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
Protein prM: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.By similarity
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.By similarity
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei100 – 101Cleavage; by viral protease NS3By similarity2
Sitei118 – 119Cleavage; by host signal peptidaseBy similarity2
Sitei210 – 211Cleavage; by host furinBy similarity2
Sitei285 – 286Cleavage; by host signal peptidaseBy similarity2
Sitei786 – 787Cleavage; by host signal peptidaseBy similarity2
Sitei1139 – 1140Cleavage; by hostBy similarity2
Sitei1366 – 1367Cleavage; by viral protease NS3By similarity2
Sitei1497 – 1498Cleavage; by autolysisBy similarity2
Sitei2115 – 2116Cleavage; by autolysisBy similarity2
Sitei2241 – 2242Cleavage; by viral protease NS3By similarity2
Sitei2264 – 2265Cleavage; by host signal peptidaseBy similarity2
Sitei2519 – 2520Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Interactioni

Subunit structurei

Capsid protein C: Homodimer. Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway. Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi. Interacts with protein prM. Interacts with non-structural protein 1. Non-structural protein 1: Homodimer; Homohexamer when secreted. NS1 interacts with NS4B. Interacts with host complement protein CFH; this interaction leads to the degradation of C3. Non-structural protein 2A: Interacts (via N-terminus) with serine protease NS3. Non-structural protein 2B: Forms a heterodimer with serine protease NS3. May form homooligomers. Serine protease NS3: Forms a heterodimer with NS2B. Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity. Non-structural protein 4B: Interacts with serine protease NS3. RNA-directed RNA polymerase NS5: Homodimer. Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation. Interacts with serine protease NS3.By similarity

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliQ32ZD7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1498 – 1675Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1678 – 1834Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1845 – 2009Helicase C-terminalPROSITE-ProRule annotationAdd BLAST165
Domaini2520 – 2784mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3048 – 3200RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 15Interaction with host EXOC1By similarityAdd BLAST14
Regioni35 – 70Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni383 – 396Fusion peptideBy similarityAdd BLAST14
Regioni1420 – 1459Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1682 – 1685Important for RNA-bindingBy similarity4
Regioni2160 – 2164Regulates the ATPase activity of NS3 helicaseBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1782 – 1785DEAH boxPROSITE-ProRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2380 – 2383Poly-LeuSequence analysis4

Domaini

The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.By similarity

Sequence similaritiesi

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
cd00079 HELICc, 1 hit
Gene3Di1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR001122 Flavi_capsidC
IPR037172 Flavi_capsidC_sf
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR000208 RNA-dir_pol_flavivirus
IPR007094 RNA-dir_pol_PSvirus
IPR002877 rRNA_MeTrfase_FtsJ_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF01003 Flavi_capsid, 1 hit
PF07652 Flavi_DEAD, 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
PIRSFiPIRSF003817 Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF101257 SSF101257, 1 hit
SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
SSF53335 SSF53335, 1 hit
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit
TIGRFAMsiTIGR04240 flavi_E_stem, 1 hit
PROSITEiView protein in PROSITE
PS51527 FLAVIVIRUS_NS2B, 1 hit
PS51528 FLAVIVIRUS_NS3PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51591 RNA_CAP01_NS5_MT, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q32ZD7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKPGKSAA KRTVNMLKRL ASVSPSRGRR TIRRMLDVRG APRLILALMA
60 70 80 90 100
FFRFAAIKPT LGLKKRWRSV NKTVAVKHLT NFKKELTTML DSVNKRKEKK
110 120 130 140 150
KSFSTALLWI TMITAVAGLK ISSHRDRPLL MVNKTDVSDA IPVPSVKGTN
160 170 180 190 200
MCTIRALDVG YTCAYDTTYE CPHLEVTMDP EDIDCWCTLE SVYVNYGLCK
210 220 230 240 250
QNHHVRRGRR AINIPHHGES HLENRATPWM DTTKTTKYLT KVENWVIRNP
260 270 280 290 300
GYALVALATA WMLGSNTPQR VVFMIMMMLI APAYSLNCLG ISNRDFVEGL
310 320 330 340 350
SGGTWVDIVL EGGSCVTVMA KDKPTLDIKL IRMEAKDLAT VRSYCYQATV
360 370 380 390 400
TDSSTEARCP TMGEAHNSKS LDASYVCKSS YVDRGWGNGC GLFGKGSIQT
410 420 430 440 450
CVKFSCPGKA TGKSIQRENL NYDVAVYVHG PISAAAHGNY TAQLTGKYAA
460 470 480 490 500
KFSITPSAPT YTANLGEYGE ATMECEPRAA LDIDNYYVMS LNNKHWLVNR
510 520 530 540 550
DWFHDLDLPW TGPATESWKN RESLIEFEEP HATRQTVVAL GNQEGALHTA
560 570 580 590 600
LAGAIPVEVS STTLTLNSGH LKCRLKLDKL KIKGTTYAMC KGTFAFAQTP
610 620 630 640 650
VDTGHGTIVA ELTYTGTDGP CKIPISMTAD LRDMTPIGRL VTVNPIIPSS
660 670 680 690 700
AKSQKILVEL EPPFGSSFIL VGQENNQIKY QWHKTGSTIG NALKTTWKGA
710 720 730 740 750
QRFAVLGDTA WDFGSVGGIF NSIGKTIHGV FGTAFRSLFG GMSWVTQALM
760 770 780 790 800
GALLLWLGIS ARERTVSLIM LSVGGILLFL AVNVHADTGC AIDMARRELK
810 820 830 840 850
CGSGIFIHND VETWRNNYKY HPLTPRGFAK VIQMSKDKGV CGIRSVGRLE
860 870 880 890 900
HEMWEAIAPE LNAIFEDNGV DLSVVVKGQT GIYKRAPKRL TETKDEMSFG
910 920 930 940 950
WKNWGKSFIF STETANSTFI VDGPESKECP TSDRAWNSLE LEDFGFGIIS
960 970 980 990 1000
TKIFLKVNEQ RGNSCDSAVI GTAVKGNEAV HSDLGFWIQS TKNESWQLER
1010 1020 1030 1040 1050
AVLGEVKSCT WPESHTLWGD GVEESDLIIP ITLAGPKSHH NMRPGYKTQT
1060 1070 1080 1090 1100
KGPWHEETPL VIEFAECPGT TVTQEESCGG RGPSIRTTTA SGRTIRNWCC
1110 1120 1130 1140 1150
KNCTLPPLRF MAGENCWYGV EVRPKRENEE TLIKSKVSAG NGQTIEPFQL
1160 1170 1180 1190 1200
GILMAFVFTQ EVLRRRWTAN LALPTSALLM ACFIFGGFTY LDLFRYFILV
1210 1220 1230 1240 1250
GAAFAEANSG GDVVHLAMIA AFNIQPVALV TTFFRKNWTN RENMILIIAA
1260 1270 1280 1290 1300
ACTQMACMEL KIELFHVMNS LSLAWMILKA LTTGTTSTLA MPFLAALSPP
1310 1320 1330 1340 1350
MNWLGLDVVR CLLIMAGVAA LISERRESLA KKKGALLISA ALALTGAFSP
1360 1370 1380 1390 1400
LVLQGALMFT QSLGKRGWPA SEVLTAVGMT FALAGSVARL DGGTMAIPLA
1410 1420 1430 1440 1450
TMAILAVAYV LSGKSTDMWL ERCADISWIN EAEITGTSPR LDVELDSNGD
1460 1470 1480 1490 1500
FKMINDPGVP MWMWTCRMGL MAMAAYNPVL IPVSMAGYWM TVKIHKRGGV
1510 1520 1530 1540 1550
MWDVPAPKQF GKTELKPGVY RVMTMGILGR YQSGVGVMWD GVFHTMWHVT
1560 1570 1580 1590 1600
QGAALRNGEG RLNPTWGSVR DDLISYGGKW KLSATWNGSE EVQMIAVEPG
1610 1620 1630 1640 1650
KAAKNYQTKP GVFKTPAGEI GAITLDFPKG TSGSPIINKA GEITGLYGNG
1660 1670 1680 1690 1700
IVLERGAYVS AITQGERQEE ETPEAFTPDM LKKRRLTILD LHPGAGKTRR
1710 1720 1730 1740 1750
VIPQIVRECV KARLRTVILV PTRVVAAEMA EALRGLPIRY QTSAVKAEHS
1760 1770 1780 1790 1800
GNEIVDAMRH ATLTQRLLTP AKVPNYNVFV MDEAHFTDPA SIAARGYIST
1810 1820 1830 1840 1850
KVELGEAAAI FMTATPPGTT DPFPDSNAPI IDQEAEIPDR AWNSGFEWIT
1860 1870 1880 1890 1900
EYTGKTVWFV PSVRMGNEIA MCLTKAGKKV IQLNRKSYDS EYQKCKGNDW
1910 1920 1930 1940 1950
DFVITTDISE MGANFGAHRV IDSRKCVKPV ILDGDDRVLM NGPAPITPAS
1960 1970 1980 1990 2000
AAQRRGRIGR DPTQSGDEYF YGGPTTTDDT GHAHWIEAKI LLDNIQLQNG
2010 2020 2030 2040 2050
LVAQLYGPER DKVFTTDGEY RLRSEQKKNF VEFLRTGDLP VWLSYKVAEA
2060 2070 2080 2090 2100
GYAYTDRRWC FDGPANNTIL EVRGDPEVWT RQGEKRILRP RWSDARVYCD
2110 2120 2130 2140 2150
NQALRSFKEF AAGKRSAGSV MEVMGRMPDY FWTKTLNAAD NLYVLATANK
2160 2170 2180 2190 2200
GGRAHQAALE ELPDTVETIL LMTMMCVASL GMFTLMVHRR GLGKTGLGTL
2210 2220 2230 2240 2250
VLATVTVLLW ISDVPAPKIA GVLLIAFLLM IVLIPEPEKQ RSQTDNHLAI
2260 2270 2280 2290 2300
FLVCVLLLIG AVSANEMGWL ETTKKDIGKL FRSSGDTQEQ STWQSWAPEV
2310 2320 2330 2340 2350
RAATAWAGYA GLTVFLTPLF RHLITTQYVS FSLTAITAQA SALFGLSAGY
2360 2370 2380 2390 2400
PFVGIDLAVG FLLLGCYGQY NLPTAVATGL LLLAHYGYMI PGWQAEAMRA
2410 2420 2430 2440 2450
AQKRTAAGVM KNAVVDGIVA TDIPEVDTAT PITEKKLGQI LLILLCGASL
2460 2470 2480 2490 2500
LVKFDTMVLV EAGVLTTSAM ATLIEGNANT VWNSTVAVGV CHLMRGAWLA
2510 2520 2530 2540 2550
GPSIGWTIVR NLENPKLKRG GGSAPTLGEI WKAQLNQLTR EEFMAYRRDG
2560 2570 2580 2590 2600
ILEVDRTQAR RARQSGITTG GHPVSRGTAK LRWMVERGFV RPIGKVVDLG
2610 2620 2630 2640 2650
CGRGGWSYYC ATLRHVQEVR GYTKGGPGHE EPVMMQSYGW NIVTMKSGVD
2660 2670 2680 2690 2700
VFYKPTESCD TLLCDIGESS SSVGVEEART LRVLDMVEPW LRAANSFCIK
2710 2720 2730 2740 2750
VLCPYTPKVI ERLERLQRAY GGGLVRVPLS RNSTHEMYWV SGASSNIINA
2760 2770 2780 2790 2800
VTVTSQILVQ RMNKGCRHGP RYEEDVCLGS GTRAVATQAS PSDHTKIKHR
2810 2820 2830 2840 2850
LERLRKEFSA TWHIDLEHPY RTWHYHGSYE VQPTGSANSM VNGVVRLLSK
2860 2870 2880 2890 2900
PWDAITSVVT MAMTDTTPFG QQRVFKEKVD TRAPDPAVGV AQALDITTGW
2910 2920 2930 2940 2950
LWTFLARSKK PRMCTREEFI AKVNSNAALG AVFDEQNQWS TAREAVEDPA
2960 2970 2980 2990 3000
FWNLVDEERK AHLAGRCETC IYNMMGKREK KLGEFGKAKG SRAIWYMWLG
3010 3020 3030 3040 3050
ARFLEFEALG FLNEDHWMSR ENSLGGVEGQ GLQKLGYILR DISHLEGGNM
3060 3070 3080 3090 3100
FADDTAGWDT RITRADLENE AKVMNMMDGE HKQLAKAIIE LTYRHKVVKV
3110 3120 3130 3140 3150
MRPARGGKTV MDIISREDQR GSGQVVTYAL NTFTNLAAQL VRCMEGEELL
3160 3170 3180 3190 3200
TESDVHGLSP KKKQAVRNWL IQNGRERLSR MAVSGDDCVV KPIDDRFASA
3210 3220 3230 3240 3250
LHFLNGMAKI RKDTQEWKPS VGWSNWQEVP FGSHHFNELL MKDGRTIVVP
3260 3270 3280 3290 3300
CRSQDELVGR ARVSPGSGWS LRETACLSKA YAQMWLLMYF HRRDLRLMAN
3310 3320 3330 3340 3350
AICSAVPVDW VPTGRTTWSI HGKGEWMTTE DMLQVWNRVW IEDNEHMEDK
3360 3370 3380 3390 3400
TPITSWTDIP YIGKREDQWC GSLIGTRQRA TWAENIYTPI MQIRNLIGDE
3410 3420
KYVDCMVSQH RFETPSPVLF TGAI
Length:3,424
Mass (Da):379,057
Last modified:December 6, 2005 - v1
Checksum:i314D2282C5FF6CBA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY632539 Genomic RNA Translation: AAV34155.1
RefSeqiYP_001040006.1, NC_009028.2

Genome annotation databases

GeneIDi5075856
KEGGivg:5075856

Similar proteinsi

Entry informationi

Entry nameiPOLG_ILHV
AccessioniPrimary (citable) accession number: Q32ZD7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2017
Last sequence update: December 6, 2005
Last modified: May 23, 2018
This is version 113 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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