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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 1 (strain Nauru/West Pac/1974) (DENV-1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA.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 binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a 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 involved in virus replication and regulation of the innate immune response. 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 2A may be involved viral RNA replication and capsid assembly.Curated
Non-structural protein 2B is a required cofactor for the serine protease function of NS3.PROSITE-ProRule annotation
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 (By similarity).PROSITE-ProRule annotation
Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase.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 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.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. Besides its role in 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).PROSITE-ProRule annotation

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.
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'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1526 – 15261Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1550 – 15501Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1610 – 16101Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Binding sitei2507 – 25071mRNA capPROSITE-ProRule annotation
Binding sitei2510 – 25101mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2511 – 25111mRNA capPROSITE-ProRule annotation
Binding sitei2513 – 25131mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2518 – 25181mRNA cap bindingPROSITE-ProRule annotation
Binding sitei2522 – 25221mRNA capPROSITE-ProRule annotation
Binding sitei2549 – 25491S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei2554 – 25541Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2579 – 25791S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2580 – 25801S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2597 – 25971S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2598 – 25981S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei2624 – 26241S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2625 – 26251S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei2639 – 26391Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation
Sitei2640 – 26401S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Binding sitei2643 – 26431mRNA capPROSITE-ProRule annotation
Sitei2673 – 26731Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2704 – 27041mRNA capPROSITE-ProRule annotation
Binding sitei2706 – 27061mRNA capPROSITE-ProRule annotation
Sitei2709 – 27091Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation
Binding sitei2711 – 27111S-adenosyl-L-methioninePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1669 – 16768ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Transferase

Keywords - Biological processi

Activation 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 STAT2 by virus, Inhibition of host TYK2 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

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 14 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Non-structural protein 2A-alpha
Short name:
NS2A-alpha
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
Alternative name(s):
Non-structural protein 5
OrganismiDengue virus type 1 (strain Nauru/West Pac/1974) (DENV-1)
Taxonomic identifieri11059 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusDengue virus group
Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000002500 Componenti: Genome

Subcellular locationi

Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A-alpha :
Non-structural protein 2A :
Serine protease subunit NS2B :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
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 NS3 protease.PROSITE-ProRule annotation
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Host nucleus By similarity

  • Note: Located in RE-associated vesicles hosting the replication complex.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 101101CytoplasmicSequence analysisAdd
BLAST
Transmembranei102 – 11918HelicalSequence analysisAdd
BLAST
Topological domaini120 – 242123ExtracellularSequence analysisAdd
BLAST
Transmembranei243 – 26018HelicalSequence analysisAdd
BLAST
Topological domaini261 – 2611CytoplasmicSequence analysis
Transmembranei262 – 28019HelicalSequence analysisAdd
BLAST
Topological domaini281 – 725445ExtracellularSequence analysisAdd
BLAST
Intramembranei726 – 74621HelicalSequence analysisAdd
BLAST
Topological domaini747 – 7526ExtracellularSequence analysis
Intramembranei753 – 77523HelicalSequence analysisAdd
BLAST
Topological domaini776 – 1125350ExtracellularSequence analysisAdd
BLAST
Transmembranei1126 – 114621HelicalSequence analysisAdd
BLAST
Topological domaini1147 – 115711CytoplasmicSequence analysisAdd
BLAST
Transmembranei1158 – 117821HelicalSequence analysisAdd
BLAST
Topological domaini1179 – 119921LumenalSequence analysisAdd
BLAST
Transmembranei1200 – 122021HelicalSequence analysisAdd
BLAST
Topological domaini1221 – 128969CytoplasmicSequence analysisAdd
BLAST
Transmembranei1290 – 131021HelicalSequence analysisAdd
BLAST
Topological domaini1311 – 13155LumenalSequence analysis
Transmembranei1316 – 133621HelicalSequence analysisAdd
BLAST
Topological domaini1337 – 134610CytoplasmicSequence analysis
Transmembranei1347 – 136721HelicalSequence analysisAdd
BLAST
Topological domaini1368 – 13703LumenalSequence analysis
Transmembranei1371 – 139121HelicalSequence analysisAdd
BLAST
Topological domaini1392 – 144756CytoplasmicSequence analysisAdd
BLAST
Intramembranei1448 – 146821HelicalSequence analysisAdd
BLAST
Topological domaini1469 – 2148680CytoplasmicSequence analysisAdd
BLAST
Transmembranei2149 – 216921HelicalSequence analysisAdd
BLAST
Topological domaini2170 – 21712LumenalSequence analysis
Intramembranei2172 – 219221HelicalSequence analysisAdd
BLAST
Topological domaini2193 – 21931LumenalSequence analysis
Transmembranei2194 – 221421HelicalSequence analysisAdd
BLAST
Topological domaini2215 – 222915CytoplasmicSequence analysisAdd
BLAST
Transmembranei2230 – 225021Helical; Note=Signal for NS4BSequence analysisAdd
BLAST
Topological domaini2251 – 227626LumenalSequence analysisAdd
BLAST
Intramembranei2277 – 229721HelicalSequence analysisAdd
BLAST
Topological domaini2298 – 234952LumenalSequence analysisAdd
BLAST
Transmembranei2350 – 237021HelicalSequence analysisAdd
BLAST
Topological domaini2371 – 241545CytoplasmicSequence analysisAdd
BLAST
Transmembranei2416 – 243621HelicalSequence analysisAdd
BLAST
Topological domaini2437 – 246125LumenalSequence analysisAdd
BLAST
Transmembranei2462 – 248221HelicalSequence analysisAdd
BLAST
Topological domaini2483 – 3392910CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 33923392Genome polyproteinPRO_0000405207Add
BLAST
Chaini1 – 100100Capsid protein CBy similarityPRO_0000264658Add
BLAST
Propeptidei101 – 11414ER anchor for the protein C, removed in mature form by serine protease NS3By similarityPRO_0000264659Add
BLAST
Chaini115 – 280166prMBy similarityPRO_0000264660Add
BLAST
Chaini115 – 20591Peptide prBy similarityPRO_0000264661Add
BLAST
Chaini206 – 28075Small envelope protein MBy similarityPRO_0000264662Add
BLAST
Chaini281 – 775495Envelope protein EBy similarityPRO_0000264663Add
BLAST
Chaini776 – 1127352Non-structural protein 1By similarityPRO_0000264664Add
BLAST
Chaini1128 – 1345218Non-structural protein 2ABy similarityPRO_0000264666Add
BLAST
Chaini1128 – 1315188Non-structural protein 2A-alphaBy similarityPRO_0000264665Add
BLAST
Chaini1346 – 1475130Serine protease subunit NS2BBy similarityPRO_0000264667Add
BLAST
Chaini1476 – 2094619Serine protease NS3By similarityPRO_0000264668Add
BLAST
Chaini2095 – 2221127Non-structural protein 4ABy similarityPRO_0000264669Add
BLAST
Peptidei2222 – 224423Peptide 2kBy similarityPRO_0000264670Add
BLAST
Chaini2245 – 2493249Non-structural protein 4BBy similarityPRO_0000264671Add
BLAST
Chaini2494 – 3392899RNA-directed RNA polymerase NS5By similarityPRO_0000264672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi183 – 1831N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi283 ↔ 310By similarity
Disulfide bondi340 ↔ 401By similarity
Glycosylationi347 – 3471N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi354 ↔ 385By similarity
Disulfide bondi372 ↔ 396By similarity
Glycosylationi433 – 4331N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi465 ↔ 565By similarity
Disulfide bondi582 ↔ 613By similarity
Glycosylationi982 – 9821N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2303 – 23031N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2307 – 23071N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2459 – 24591N-linked (GlcNAc...); by hostSequence analysis

Post-translational modificationi

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. Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei100 – 1012Cleavage; by viral protease NS3Sequence analysis
Sitei114 – 1152Cleavage; by host signal peptidaseBy similarity
Sitei205 – 2062Cleavage; by host furinSequence analysis
Sitei280 – 2812Cleavage; by host signal peptidaseSequence analysis
Sitei775 – 7762Cleavage; by host signal peptidaseSequence analysis
Sitei1127 – 11282Cleavage; by hostBy similarity
Sitei1345 – 13462Cleavage; by viral protease NS3Sequence analysis
Sitei1475 – 14762Cleavage; by autolysisSequence analysis
Sitei2094 – 20952Cleavage; by autolysisSequence analysis
Sitei2221 – 22222Cleavage; by viral protease NS3Sequence analysis
Sitei2244 – 22452Cleavage; by host signal peptidaseSequence analysis
Sitei2493 – 24942Cleavage; by viral protease NS3Sequence analysis

Keywords - PTMi

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

Interactioni

Subunit structurei

Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity. NS5 interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation.By similarity

Structurei

Secondary structure

1
3392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi288 – 2903Combined sources
Beta strandi291 – 2933Combined sources
Beta strandi295 – 30814Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi321 – 33212Combined sources
Beta strandi334 – 35219Combined sources
Helixi363 – 3664Combined sources
Beta strandi370 – 37910Combined sources
Helixi381 – 3833Combined sources
Beta strandi389 – 40921Combined sources
Helixi412 – 4143Combined sources
Beta strandi415 – 4239Combined sources
Beta strandi440 – 4445Combined sources
Beta strandi450 – 4556Combined sources
Turni456 – 4583Combined sources
Beta strandi459 – 4679Combined sources
Turni473 – 4753Combined sources
Beta strandi476 – 4816Combined sources
Beta strandi484 – 4896Combined sources
Helixi490 – 4945Combined sources
Beta strandi500 – 5045Combined sources
Helixi514 – 5163Combined sources
Beta strandi518 – 5203Combined sources
Beta strandi530 – 5323Combined sources
Helixi537 – 5437Combined sources
Turni544 – 5463Combined sources
Beta strandi547 – 5537Combined sources
Beta strandi556 – 5594Combined sources
Beta strandi562 – 57110Combined sources
Beta strandi586 – 5905Combined sources
Beta strandi596 – 5983Combined sources
Beta strandi600 – 6067Combined sources
Beta strandi612 – 6143Combined sources
Beta strandi617 – 6204Combined sources
Beta strandi633 – 6353Combined sources
Beta strandi637 – 6393Combined sources
Beta strandi645 – 6495Combined sources
Beta strandi653 – 66311Combined sources
Beta strandi667 – 6737Combined sources
Turni956 – 9583Combined sources
Beta strandi960 – 9645Combined sources
Beta strandi967 – 9715Combined sources
Beta strandi973 – 99422Combined sources
Helixi1002 – 10043Combined sources
Helixi1013 – 10153Combined sources
Helixi1020 – 10223Combined sources
Helixi1028 – 10303Combined sources
Helixi1043 – 10453Combined sources
Beta strandi1046 – 10538Combined sources
Beta strandi1059 – 10624Combined sources
Beta strandi1073 – 10764Combined sources
Beta strandi1085 – 10906Combined sources
Beta strandi1096 – 10994Combined sources
Beta strandi1104 – 11063Combined sources
Beta strandi1111 – 11144Combined sources
Beta strandi1496 – 15049Combined sources
Beta strandi1507 – 151711Combined sources
Beta strandi1520 – 15234Combined sources
Helixi1525 – 15284Combined sources
Beta strandi1533 – 15353Combined sources
Beta strandi1538 – 15403Combined sources
Beta strandi1542 – 15465Combined sources
Turni1547 – 15504Combined sources
Beta strandi1551 – 15577Combined sources
Beta strandi1570 – 15745Combined sources
Beta strandi1582 – 15865Combined sources
Beta strandi1589 – 15935Combined sources
Beta strandi1596 – 16016Combined sources
Beta strandi1613 – 16153Combined sources
Beta strandi1621 – 16255Combined sources
Beta strandi1628 – 16303Combined sources
Beta strandi1636 – 16394Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L6PX-ray2.20A1476-1648[»]
3LKWX-ray2.00A1476-1657[»]
4AL8X-ray1.66C575-675[»]
4GSXX-ray1.90A/B281-691[»]
4GT0X-ray2.57A/B281-701[»]
4LCYX-ray1.60C/J1741-1749[»]
4OIGX-ray2.69A/B/D/E947-1127[»]
ProteinModelPortaliP17763.
SMRiP17763. Positions 21-100, 115-195, 281-674, 1495-2094, 2500-2760, 2766-3375.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17763.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1476 – 1653178Peptidase S7PROSITE-ProRule annotationAdd
BLAST
Domaini1656 – 1812157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1822 – 1988167Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2495 – 2756262mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
BLAST
Domaini3020 – 3169150RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 7442Hydrophobic; homodimerization of capsid protein CBy similarityAdd
BLAST
Regioni1398 – 143740Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1760 – 17634DEAH box

Domaini

Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals.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
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 mRNA cap 0-1 NS5-type MT domain.PROSITE-ProRule annotation
Contains 1 peptidase S7 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR026470. Flavi_E_Stem/Anchor_dom.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR001850. Flavivirus_NS3_S7.
IPR027287. Flavovir_Ig-like.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
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.
[Graphical view]
PfamiPF01003. 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.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. 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.
PROSITEiPS51527. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P17763-1 [UniParc]FASTAAdd to basket

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        10         20         30         40         50
MNNQRKKTGR PSFNMLKRAR NRVSTVSQLA KRFSKGLLSG QGPMKLVMAF
60 70 80 90 100
IAFLRFLAIP PTAGILARWG SFKKNGAIKV LRGFKKEISN MLNIMNRRKR
110 120 130 140 150
SVTMLLMLLP TALAFHLTTR GGEPHMIVSK QERGKSLLFK TSAGVNMCTL
160 170 180 190 200
IAMDLGELCE DTMTYKCPRI TETEPDDVDC WCNATETWVT YGTCSQTGEH
210 220 230 240 250
RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQKVETW ALRHPGFTVI
260 270 280 290 300
ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW
310 320 330 340 350
VDVVLEHGSC VTTMAKDKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT
360 370 380 390 400
DSRCPTQGEA TLVEEQDTNF VCRRTFVDRG WGNGCGLFGK GSLITCAKFK
410 420 430 440 450
CVTKLEGKIV QYENLKYSVI VTVHTGDQHQ VGNETTEHGT TATITPQAPT
460 470 480 490 500
SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT MEKKSWLVHK QWFLDLPLPW
510 520 530 540 550
TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM HTALTGATEI
560 570 580 590 600
QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV
610 620 630 640 650
LVQVKYEGTD APCKIPFSSQ DEKGVTQNGR LITANPIVTD KEKPVNIEAE
660 670 680 690 700
PPFGESYIVV GAGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW
710 720 730 740 750
DFGSIGGVFT SVGKLIHQIF GTAYGVLFSG VSWTMKIGIG ILLTWLGLNS
760 770 780 790 800
RSTSLSMTCI AVGMVTLYLG VMVQADSGCV INWKGRELKC GSGIFVTNEV
810 820 830 840 850
HTWTEQYKFQ ADSPKRLSAA IGKAWEEGVC GIRSATRLEN IMWKQISNEL
860 870 880 890 900
NHILLENDMK FTVVVGDVSG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG
910 920 930 940 950
ADVQNTTFII DGPNTPECPD NQRAWNIWEV EDYGFGIFTT NIWLKLRDSY
960 970 980 990 1000
TQVCDHRLMS AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCIW
1010 1020 1030 1040 1050
PKSHTLWSNG VLESEMIIPK IYGGPISQHN YRPGYFTQTA GPWHLGKLEL
1060 1070 1080 1090 1100
DFDLCEGTTV VVDEHCGNRG PSLRTTTVTG KTIHEWCCRS CTLPPLRFKG
1110 1120 1130 1140 1150
EDGCWYGMEI RPVKEKEENL VKSMVSAGSG EVDSFSLGLL CISIMIEEVM
1160 1170 1180 1190 1200
RSRWSRKMLM TGTLAVFLLL TMGQLTWNDL IRLCIMVGAN ASDKMGMGTT
1210 1220 1230 1240 1250
YLALMATFRM RPMFAVGLLF RRLTSREVLL LTVGLSLVAS VELPNSLEEL
1260 1270 1280 1290 1300
GDGLAMGIMM LKLLTDFQSH QLWATLLSLT FVKTTFSLHY AWKTMAMILS
1310 1320 1330 1340 1350
IVSLFPLCLS TTSQKTTWLP VLLGSLGCKP LTMFLITENK IWGRKSWPLN
1360 1370 1380 1390 1400
EGIMAVGIVS ILLSSLLKND VPLAGPLIAG GMLIACYVIS GSSADLSLEK
1410 1420 1430 1440 1450
AAEVSWEEEA EHSGASHNIL VEVQDDGTMK IKDEERDDTL TILLKATLLA
1460 1470 1480 1490 1500
ISGVYPMSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI
1510 1520 1530 1540 1550
LQRGLLGRSQ VGVGVFQEGV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD
1560 1570 1580 1590 1600
LISYGGGWRF QGSWNAGEEV QVIAVEPGKN PKNVQTAPGT FKTPEGEVGA
1610 1620 1630 1640 1650
IALDFKPGTS GSPIVNREGK IVGLYGNGVV TTSGTYVSAI AQAKASQEGP
1660 1670 1680 1690 1700
LPEIEDEVFR KRNLTIMDLH PGSGKTRRYL PAIVREAIRR NVRTLVLAPT
1710 1720 1730 1740 1750
RVVASEMAEA LKGMPIRYQT TAVKSEHTGK EIVDLMCHAT FTMRLLSPVR
1760 1770 1780 1790 1800
VPNYNMIIMD EAHFTDPASI AARGYISTRV GMGEAAAIFM TATPPGSVEA
1810 1820 1830 1840 1850
FPQSNAVIQD EERDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC
1860 1870 1880 1890 1900
LRKNGKRVVQ LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID
1910 1920 1930 1940 1950
PRRCLKPVIL KDGPERVILA GPMPVTVASA AQRRGRIGRN QNKEGDQYIY
1960 1970 1980 1990 2000
MGQPLNNDED HAHWTEAKML LDNINTPEGI IPALFEPERE KSAAIDGEYR
2010 2020 2030 2040 2050
LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF DGERNNQVLE
2060 2070 2080 2090 2100
ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL
2110 2120 2130 2140 2150
ILEIGKLPQH LTQRAQNALD NLVMLHNSEQ GGKAYRHAME ELPDTIETLM
2160 2170 2180 2190 2200
LLALIAVLTG GVTLFFLSGR GLGKTSIGLL CVIASSALLW MASVEPHWIA
2210 2220 2230 2240 2250
ASIILEFFLM VLLIPEPDRQ RTPQDNQLAY VVIGLLFMIL TAAANEMGLL
2260 2270 2280 2290 2300
ETTKKDLGIG HAAAENHHHA AMLDVDLHPA SAWTLYAVAT TIITPMMRHT
2310 2320 2330 2340 2350
IENTTANISL TAIANQAAIL MGLDKGWPIS KMDIGVPLLA LGCYSQVNPL
2360 2370 2380 2390 2400
TLTAAVFMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL
2410 2420 2430 2440 2450
DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW
2460 2470 2480 2490 2500
EGSPGKFWNT TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE
2510 2520 2530 2540 2550
TLGEKWKRQL NQLSKSEFNT YKRSGIIEVD RSEAKEGLKR GEPTKHAVSR
2560 2570 2580 2590 2600
GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW SYYCAGLKKV TEVKGYTKGG
2610 2620 2630 2640 2650
PGHEEPIPMA TYGWNLVKLY SGKDVFFTPP EKCDTLLCDI GESSPNPTIE
2660 2670 2680 2690 2700
EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN
2710 2720 2730 2740 2750
PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL
2760 2770 2780 2790 2800
GAGTRHVAVE PEVANLDIIG QRIENIKNGH KSTWHYDEDN PYKTWAYHGS
2810 2820 2830 2840 2850
YEVKPSGSAS SMVNGVVRLL TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK
2860 2870 2880 2890 2900
VDTRTPKAKR GTAQIMEVTA RWLWGFLSRN KKPRICTREE FTRKVRSNAA
2910 2920 2930 2940 2950
IGAVFVDENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA TCVYNMMGKR
2960 2970 2980 2990 3000
EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE
3010 3020 3030 3040 3050
GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLQ NEAKITDIME
3060 3070 3080 3090 3100
PEHALLATSI FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG
3110 3120 3130 3140 3150
LNTFTNMEAQ LIRQMESEGI FSPSELETPN LAERVLDWLK KHGTERLKRM
3160 3170 3180 3190 3200
AISGDDCVVK PIDDRFATAL TALNDMGKVR KDIPQWEPSK GWNDWQQVPF
3210 3220 3230 3240 3250
CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL RETACLGKSY
3260 3270 3280 3290 3300
AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED
3310 3320 3330 3340 3350
MLSVWNRVWI EENPWMEDKT HVSSWEDVPY LGKREDRWCG SLIGLTARAT
3360 3370 3380 3390
WATNIQVAIN QVRRLIGNEN YLDFMTSMKR FKNESDPEGA LW
Length:3,392
Mass (Da):378,702
Last modified:December 12, 2006 - v2
Checksum:i3A7C57D3054D2972
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti125 – 1262HM → TL in strain: Isolate Philippines/836-1/1984.
Natural varianti142 – 1421S → P in strain: Isolate Philippines/836-1/1984.
Natural varianti171 – 1733TET → AEA in strain: Isolate Philippines/836-1/1984.
Natural varianti186 – 1861E → D in strain: Isolate Philippines/836-1/1984.
Natural varianti210 – 2101A → D in strain: Isolate Philippines/836-1/1984.
Natural varianti251 – 2511A → G in strain: Isolate Philippines/836-1/1984.
Natural varianti441 – 4411T → I in strain: Isolate Philippines/836-1/1984.
Natural varianti475 – 4751E → R in strain: Isolate Philippines/836-1/1984.
Natural varianti482 – 4821E → K in strain: Isolate 45AZ5.
Natural varianti573 – 5731T → I in strain: Isolate 45AZ5.
Natural varianti677 – 6771S → T in strain: Isolate Philippines/836-1/1984.
Natural varianti786 – 7861R → K in strain: Isolate Philippines/836-1/1984.
Natural varianti1689 – 16924RRNV → KRKL in strain: Isolate 45AZ5.
Natural varianti2242 – 22421A → V in strain: Isolate 45AZ5.
Natural varianti2357 – 23571F → L in strain: Isolate 45AZ5.
Natural varianti2543 – 25431P → T in strain: Isolate 45AZ5.
Natural varianti2779 – 27791G → E in strain: Isolate 45AZ5.
Natural varianti3337 – 33371R → Q in strain: Isolate 45AZ5.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88535 Genomic RNA. Translation: AAB70694.1.
U88536 Genomic RNA. Translation: AAB70695.1.
M23027 Genomic RNA. Translation: AAA42940.1.
D00503 Genomic RNA. Translation: BAA00395.1.
PIRiA27032. GNWVWP.
RefSeqiNP_059433.1. NC_001477.1.

Genome annotation databases

GeneIDi5075725.
KEGGivg:5075725.

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88535 Genomic RNA. Translation: AAB70694.1.
U88536 Genomic RNA. Translation: AAB70695.1.
M23027 Genomic RNA. Translation: AAA42940.1.
D00503 Genomic RNA. Translation: BAA00395.1.
PIRiA27032. GNWVWP.
RefSeqiNP_059433.1. NC_001477.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L6PX-ray2.20A1476-1648[»]
3LKWX-ray2.00A1476-1657[»]
4AL8X-ray1.66C575-675[»]
4GSXX-ray1.90A/B281-691[»]
4GT0X-ray2.57A/B281-701[»]
4LCYX-ray1.60C/J1741-1749[»]
4OIGX-ray2.69A/B/D/E947-1127[»]
ProteinModelPortaliP17763.
SMRiP17763. Positions 21-100, 115-195, 281-674, 1495-2094, 2500-2760, 2766-3375.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5075725.
KEGGivg:5075725.

Miscellaneous databases

EvolutionaryTraceiP17763.
PROiP17763.

Family and domain databases

Gene3Di2.60.40.350. 1 hit.
2.60.98.10. 2 hits.
3.30.387.10. 1 hit.
3.40.50.150. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR026470. Flavi_E_Stem/Anchor_dom.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR001850. Flavivirus_NS3_S7.
IPR027287. Flavovir_Ig-like.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
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.
[Graphical view]
PfamiPF01003. 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.
[Graphical view]
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. 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.
PROSITEiPS51527. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular analysis of dengue virus attenuation after serial passage in primary dog kidney cells."
    Puri B., Nelson W.M., Henchal E.A., Hoke C.H., Eckels K.H., Dubois D.R., Porter K.R., Hayes C.G.
    J. Gen. Virol. 78:2287-2291(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate 45AZ5 and Isolate WestPac.
  2. "Sequence of the dengue-1 virus genome in the region encoding the three structural proteins and the major nonstructural protein NS1."
    Mason P.W., McAda P.C., Mason T.L., Fournier M.J.
    Virology 161:262-267(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1226.
  3. "Genetic relatedness among structural protein genes of dengue 1 virus strains."
    Chu M.C., O'Rourke E.J., Trent D.W.
    J. Gen. Virol. 70:1701-1712(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-792.
    Strain: Isolate Philippines/836-1/1984.
  4. "Structure and function of flavivirus NS5 methyltransferase."
    Zhou Y., Ray D., Zhao Y., Dong H., Ren S., Li Z., Guo Y., Bernard K.A., Shi P.-Y., Li H.
    J. Virol. 81:3891-3903(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF METHYLTRANSFERASE ACTIVITY.
  5. "NS5 of dengue virus mediates STAT2 binding and degradation."
    Ashour J., Laurent-Rolle M., Shi P.Y., Garcia-Sastre A.
    J. Virol. 83:5408-5418(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5, INTERACTION WITH HUMAN STAT2.
  6. "Serotype-specific structural differences in the protease-cofactor complexes of the dengue virus family."
    Chandramouli S., Joseph J.S., Daudenarde S., Gatchalian J., Cornillez-Ty C., Kuhn P.
    J. Virol. 84:3059-3067(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1394-1661.

Entry informationi

Entry nameiPOLG_DEN1W
AccessioniPrimary (citable) accession number: P17763
Secondary accession number(s): P27910, P89313, P89314
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 12, 2006
Last modified: June 8, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.