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Protein

Genome polyprotein

Gene
N/A
Organism
Hepatitis C virus subtype 1b
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + H2O = ADP + phosphate.SAAS annotation
NTP + H2O = NDP + phosphate.SAAS annotation
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).SAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1123 – 11231ZincCombined sources
Metal bindingi1125 – 11251ZincCombined sources
Metal bindingi1171 – 11711ZincCombined sources
Metal bindingi1175 – 11751Zinc; via pros nitrogenCombined sources
Binding sitei1267 – 12671ADPCombined sources
Binding sitei1493 – 14931ADPCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1233 – 12386ADPCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

HelicaseSAAS annotation, Hydrolase, Nucleotidyltransferase, RNA-directed RNA polymeraseSAAS annotation, Transferase

Keywords - Biological processi

Activation of host autophagy by virusSAAS annotation, Host-virus interaction, Viral attachment to host cellSAAS annotation, Viral RNA replicationSAAS annotation, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Metal-bindingCombined sources, Nucleotide-binding, ZincCombined sources

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyproteinSAAS annotation
OrganismiHepatitis C virus subtype 1bImported
Taxonomic identifieri31647 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeHepacivirus

Subcellular locationi

  • Virion SAAS annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei718 – 74023HelicalSequence analysisAdd
BLAST
Transmembranei752 – 77827HelicalSequence analysisAdd
BLAST
Transmembranei784 – 80320HelicalSequence analysisAdd
BLAST
Transmembranei815 – 83521HelicalSequence analysisAdd
BLAST
Transmembranei1660 – 168829HelicalSequence analysisAdd
BLAST
Transmembranei1825 – 184521HelicalSequence analysisAdd
BLAST
Transmembranei1851 – 187020HelicalSequence analysisAdd
BLAST
Transmembranei1882 – 190221HelicalSequence analysisAdd
BLAST
Transmembranei2990 – 300718HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid proteinSAAS annotation, Host membraneSAAS annotation, Membrane, Virion

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi1123 ↔ 1171Combined sources
Modified residuei2642 – 26421Cysteine sulfinic acid (-SO2H)Combined sources
Disulfide bondi2722 ↔ 2730Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D3UX-ray2.00A/B2420-2989[»]
2D3ZX-ray1.80A/B2420-2989[»]
2D41X-ray2.10A/B2420-2989[»]
2FVCX-ray2.00A/B2420-2982[»]
2GC8X-ray2.20A/B2420-2989[»]
2HAIX-ray1.58A2420-2989[»]
2IJNX-ray2.20A/B2422-2989[»]
2QE2X-ray2.90A/B2420-2989[»]
2QE5X-ray2.60A/B/C/D2420-2989[»]
3HHKX-ray1.70A/B2420-2982[»]
3O8BX-ray1.95A/B1029-1657[»]
3O8CX-ray2.00A/B1029-1657[»]
3O8DX-ray2.05A/B1029-1657[»]
3O8RX-ray2.30A/B1029-1657[»]
ProteinModelPortaliQ99AU2.
SMRiQ99AU2. Positions 2-45, 902-1026, 1029-1657, 1973-2003, 2008-2170, 2420-2982.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99AU2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini903 – 1026124Peptidase C18InterPro annotationAdd
BLAST
Domaini1217 – 1369153Helicase ATP-bindingInterPro annotationAdd
BLAST
Domaini1361 – 1538178Helicase C-terminalInterPro annotationAdd
BLAST
Domaini2633 – 2751119RdRp catalyticInterPro annotationAdd
BLAST

Sequence similaritiesi

Contains RdRp catalytic domain.SAAS annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysisSAAS annotation

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR002521. HCV_core_C.
IPR002522. HCV_core_N.
IPR002519. HCV_env.
IPR002531. HCV_NS1.
IPR002518. HCV_NS2.
IPR000745. HCV_NS4a.
IPR001490. HCV_NS4b.
IPR002868. HCV_NS5a.
IPR013193. HCV_NS5a_1B_dom.
IPR024350. HCV_NS5a_C.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR013192. NS5A_1a.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR004109. Peptidase_S29.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
[Graphical view]
PfamiPF07652. Flavi_DEAD. 1 hit.
PF01543. HCV_capsid. 1 hit.
PF01542. HCV_core. 1 hit.
PF01539. HCV_env. 1 hit.
PF01560. HCV_NS1. 1 hit.
PF01538. HCV_NS2. 1 hit.
PF01006. HCV_NS4a. 1 hit.
PF01001. HCV_NS4b. 1 hit.
PF01506. HCV_NS5a. 1 hit.
PF08300. HCV_NS5a_1a. 1 hit.
PF08301. HCV_NS5a_1b. 1 hit.
PF12941. HCV_NS5a_C. 1 hit.
PF02907. Peptidase_S29. 1 hit.
PF00998. RdRP_3. 1 hit.
[Graphical view]
ProDomiPD001388. HCV_env. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51693. HCV_NS2_PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99AU2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR
60 70 80 90 100
KTSERSQPRG RRQPIPKARR PEGRTWAQPG YPWPLYGNEG MGWAGWLLSP
110 120 130 140 150
RGSRPSWGPT DPRRRSRNLG KVIDTLTCGF ADLMGYIPLV GAPLGGAARA
160 170 180 190 200
LAHGVRVLED GVNYATGNLP GCSFSIFLLA LLSCLTIPAS AYEVRNVSGI
210 220 230 240 250
YHVTNDCSNS SIVYEAADMI MHTPGCVPCV RESNFSRCWV ALTPTLAARN
260 270 280 290 300
SSIPTTTIRR HVDLLVGAAA LCSAMYVGDL CGSVFLVSQL FTFSPRRYET
310 320 330 340 350
VQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQAVVDMVAG
360 370 380 390 400
AHWGVLAGLA YYSMVGNWAK VLIVMLLFAG VDGHTHVTGG RVASSTQSLV
410 420 430 440 450
SWLSQGPSQK IQLVNTNGSW HINRTALNCN DSLQTGFIAA LFYAHRFNAS
460 470 480 490 500
GCPERMASCR PIDKFAQGWG PITHVVPNIS DQRPYCWHYA PQPCGIVPAS
510 520 530 540 550
QVCGPVYCFT PSPVVVGTTD RSGVPTYSWG ENETDVLLLN NTRPPQGNWF
560 570 580 590 600
GCTWMNSTGF TKTCGGPPCN IGGVGNNTLI CPTDCFRKHP EATYTKCGSG
610 620 630 640 650
PWLTPRCLVD YPYRLWHYPC TINFTIFKVR MYVGGVEHRL NAACNWTRGE
660 670 680 690 700
RCDLEDRDRS ELSPLLLSTT EWQVLPCSFT TLPALSTGLI HLHQNIVDVQ
710 720 730 740 750
YLYGVGSVVV SVVIKWEYVL LLFLLLADAR VCACLWMMLL IAQAEATLEN
760 770 780 790 800
LVVLNAASVA GAHGLLSFLV FFCAAWYIKG RLVPGAAYAL YGVWPLLLLL
810 820 830 840 850
LALPPRAYAM DREMAASCGG AVFVGLVLLT LSPYYKVFLA RLIWWLQYFI
860 870 880 890 900
TRAEAHLQVW VPPLNVRGGR DAIILLTCAV HPELIFDITK LLLAILGPLM
910 920 930 940 950
VLQAGITRVP YFVRAQGLIH ACMLVRKVAG GHYVQMAFMK LGALTGTYIY
960 970 980 990 1000
NHLTPLRDWA HAGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIILGL
1010 1020 1030 1040 1050
PVSARRGKEI LLGPADSLEG RGWRLLAPIT AYSQQTRGLL GCIITSLTGR
1060 1070 1080 1090 1100
DKNQVEGEVQ VVSTATQSFL ATCVNGVCWT VYHGAGSKTL AGPKGPITQM
1110 1120 1130 1140 1150
YTNVDQDLVG WQAPPGARSL TPCTCGSSDL YLVTRHADVI PVRRRGDSRG
1160 1170 1180 1190 1200
SLLSPRPVSY LKGSSGGPLL CPSGHAVGIF RAAVCTRGVA KAVDFVPVES
1210 1220 1230 1240 1250
METTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAQGYK
1260 1270 1280 1290 1300
VLVLNPSVAA TLGFGAYMSK AHGIDPNIRT GVRTITTGAP VTYSTYGKFL
1310 1320 1330 1340 1350
ADGGCSGGAY DIIICDECHS TDSTTILGIG TVLDQAETAG ARLVVLATAT
1360 1370 1380 1390 1400
PPGSVTVPHP NIEEVALSNT GEIPFYGKAI PIEAIRGGRH LIFCHSKKKC
1410 1420 1430 1440 1450
DELAAKLSGL GINAVAYYRG LDVSVIPTIG DVVVVATDAL MTGYTGDFDS
1460 1470 1480 1490 1500
VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRRGIYR
1510 1520 1530 1540 1550
FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV
1560 1570 1580 1590 1600
CQDHLEFWES VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP
1610 1620 1630 1640 1650
PPSWDQMWKC LIRLKPTLHG PTPLLYRLGA VQNEVTLTHP ITKYIMACMS
1660 1670 1680 1690 1700
ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV VIVGRIILSG RPAIVPDREL
1710 1720 1730 1740 1750
LYQEFDEMEE CATHLPYIEQ GMQLAEQFKQ KALGLLQTAT KQAEAAAPVV
1760 1770 1780 1790 1800
ESKWRALETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP
1810 1820 1830 1840 1850
LTTQSTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD
1860 1870 1880 1890 1900
ILAGYGAGVA GALVAFKVMS GEMPSTEDLV NLLPAILSPG ALVVGVVCAA
1910 1920 1930 1940 1950
ILRRHVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA AARVTQILSS
1960 1970 1980 1990 2000
LTITQLLKRL HQWINEDCST PCSGSWLRDV WDWICTVLTD FKTWLQSKLL
2010 2020 2030 2040 2050
PQLPGVPFFS CQRGYKGVWR GDGIMQTTCP CGAQITGHVK NGSMRIVGPK
2060 2070 2080 2090 2100
TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGDFH
2110 2120 2130 2140 2150
YVTGMTTDNV KCPCQVPAPE FFSEVDGVRL HRYAPACRPL LREEVTFQVG
2160 2170 2180 2190 2200
LNQYLVGSQL PCEPEPDVAV LTSMLTDPSH ITAETAKRRL ARGSPPSLAS
2210 2220 2230 2240 2250
SSASQLSAPS LKATCTTHHV SPDADLIEAN LLWRQEMGGN ITRVESENKV
2260 2270 2280 2290 2300
VVLDSFDPLR AEEDEREVSV PAEILRKSKK FPAAMPIWAR PDYNPPLLES
2310 2320 2330 2340 2350
WKDPDYVPPV VHGCPLPPIK APPIPPPRRK RTVVLTESSV SSALAELATK
2360 2370 2380 2390 2400
TFGSSESSAV DSGTATALPD QASDDGDKGS DVESYSSMPP LEGEPGDPDL
2410 2420 2430 2440 2450
SDGSWSTVSE EASEDVVCCS MSYTWTGALI TPCAAEESKL PINALSNSLL
2460 2470 2480 2490 2500
RHHNMVYATT SRSAGLRQKK VTFDRLQVLD DHYRDVLKEM KAKASTVKAK
2510 2520 2530 2540 2550
LLSVEEACKL TPPHSAKSKF GYGAKDVRNL SSKAVNHIHS VWKDLLEDTV
2560 2570 2580 2590 2600
TPIDTTIMAK NEVFCVQPEK GGRKPARLIV FPDLGVRVCE KMALYDVVST
2610 2620 2630 2640 2650
LPQVVMGSSY GFQYSPGQRV EFLVNTWKSK KNPMGFSYDT RCFDSTVTEN
2660 2670 2680 2690 2700
DIRVEESIYQ CCDLAPEARQ AIKSLTERLY IGGPLTNSKG QNCGYRRCRA
2710 2720 2730 2740 2750
SGVLTTSCGN TLTCYLKASA ACRAAKLQDC TMLVNGDDLV VICESAGTQE
2760 2770 2780 2790 2800
DAASLRVFTE AMTRYSAPPG DPPQPEYDLE LITSCSSNVS VAHDASGKRV
2810 2820 2830 2840 2850
YYLTRDPTTP LARAAWETAR HTPVNSWLGN IIMYAPTLWA RMILMTHFFS
2860 2870 2880 2890 2900
ILLAQEQLEK ALDCQIYGAC YSIEPLDLPQ IIERLHGLSA FSLHSYSPGE
2910 2920 2930 2940 2950
INRVASCLRK LGVPPLRVWR HRARSVRARL LSQGGRAATC GKYLFNWAVK
2960 2970 2980 2990 3000
TKLKLTPIPA ASQLDLSGWF VAGYSGGDIY HSLSRARPRW FMLCLLLLSV
3010
GVGIYLLPNR
Length:3,010
Mass (Da):327,011
Last modified:June 1, 2001 - v1
Checksum:i053B9A653B0AB335
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF333324 mRNA. Translation: AAK08509.1.
PIRiA61196.
PQ0246.
PQ0804.
PS0329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF333324 mRNA. Translation: AAK08509.1.
PIRiA61196.
PQ0246.
PQ0804.
PS0329.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D3UX-ray2.00A/B2420-2989[»]
2D3ZX-ray1.80A/B2420-2989[»]
2D41X-ray2.10A/B2420-2989[»]
2FVCX-ray2.00A/B2420-2982[»]
2GC8X-ray2.20A/B2420-2989[»]
2HAIX-ray1.58A2420-2989[»]
2IJNX-ray2.20A/B2422-2989[»]
2QE2X-ray2.90A/B2420-2989[»]
2QE5X-ray2.60A/B/C/D2420-2989[»]
3HHKX-ray1.70A/B2420-2982[»]
3O8BX-ray1.95A/B1029-1657[»]
3O8CX-ray2.00A/B1029-1657[»]
3O8DX-ray2.05A/B1029-1657[»]
3O8RX-ray2.30A/B1029-1657[»]
ProteinModelPortaliQ99AU2.
SMRiQ99AU2. Positions 2-45, 902-1026, 1029-1657, 1973-2003, 2008-2170, 2420-2982.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

euHCVdbiAF333324.

Miscellaneous databases

EvolutionaryTraceiQ99AU2.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR002521. HCV_core_C.
IPR002522. HCV_core_N.
IPR002519. HCV_env.
IPR002531. HCV_NS1.
IPR002518. HCV_NS2.
IPR000745. HCV_NS4a.
IPR001490. HCV_NS4b.
IPR002868. HCV_NS5a.
IPR013193. HCV_NS5a_1B_dom.
IPR024350. HCV_NS5a_C.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR013192. NS5A_1a.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR004109. Peptidase_S29.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
[Graphical view]
PfamiPF07652. Flavi_DEAD. 1 hit.
PF01543. HCV_capsid. 1 hit.
PF01542. HCV_core. 1 hit.
PF01539. HCV_env. 1 hit.
PF01560. HCV_NS1. 1 hit.
PF01538. HCV_NS2. 1 hit.
PF01006. HCV_NS4a. 1 hit.
PF01001. HCV_NS4b. 1 hit.
PF01506. HCV_NS5a. 1 hit.
PF08300. HCV_NS5a_1a. 1 hit.
PF08301. HCV_NS5a_1b. 1 hit.
PF12941. HCV_NS5a_C. 1 hit.
PF02907. Peptidase_S29. 1 hit.
PF00998. RdRP_3. 1 hit.
[Graphical view]
ProDomiPD001388. HCV_env. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51693. HCV_NS2_PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Emergence of a distinct pattern of viral mutations in chimpanzees infected with a homogeneous inoculum of hepatitis C virus."
    Thomson M., Nascimbeni M., Gonzales S., Murthy K.K., Rehermann B., Liang T.J.
    Gastroenterology 121:1226-1233(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Chimera of HCV-BKImported.
  2. "Identification and structure-based optimization of novel dihydropyrones as potent HCV RNA polymerase inhibitors."
    Li H., Tatlock J., Linton A., Gonzalez J., Borchardt A., Dragovich P., Jewell T., Prins T., Zhou R., Blazel J., Parge H., Love R., Hickey M., Doan C., Shi S., Duggal R., Lewis C., Fuhrman S.
    Bioorg. Med. Chem. Lett. 16:4834-4838(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 2420-2989, SULFINATION AT CYS-2642, DISULFIDE BONDS.
  3. "3-(1,1-dioxo-2H-(1,2,4)-benzothiadiazin-3-yl)-4-hydroxy-2(1H)-quinolinones, potent inhibitors of hepatitis C virus RNA-dependent RNA polymerase."
    Tedesco R., Shaw A.N., Bambal R., Chai D., Concha N.O., Darcy M.G., Dhanak D., Fitch D.M., Gates A., Gerhardt W.G., Halegoua D.L., Han C., Hofmann G.A., Johnston V.K., Kaura A.C., Liu N., Keenan R.M., Lin-Goerke J.
    , Sarisky R.T., Wiggall K.J., Zimmerman M.N., Duffy K.J.
    J. Med. Chem. 49:971-983(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2420-2982.
  4. "Discovery of proline sulfonamides as potent and selective hepatitis C virus NS5b polymerase inhibitors. Evidence for a new NS5b polymerase binding site."
    Gopalsamy A., Chopra R., Lim K., Ciszewski G., Shi M., Curran K.J., Sukits S.F., Svenson K., Bard J., Ellingboe J.W., Agarwal A., Krishnamurthy G., Howe A.Y., Orlowski M., Feld B., O'Connell J., Mansour T.S.
    J. Med. Chem. 49:3052-3055(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2420-2989.
  5. "Non-nucleoside inhibitors binding to hepatitis C virus NS5B polymerase reveal a novel mechanism of inhibition."
    Biswal B.K., Wang M., Cherney M.M., Chan L., Yannopoulos C.G., Bilimoria D., Bedard J., James M.N.
    J. Mol. Biol. 361:33-45(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2420-2989, DISULFIDE BONDS.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2422-2989.
  7. "Identification of anthranilic acid derivatives as a novel class of allosteric inhibitors of hepatitis C NS5B polymerase."
    Nittoli T., Curran K., Insaf S., DiGrandi M., Orlowski M., Chopra R., Agarwal A., Howe A.Y., Prashad A., Floyd M.B., Johnson B., Sutherland A., Wheless K., Feld B., O'Connell J., Mansour T.S., Bloom J.
    J. Med. Chem. 50:2108-2116(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2420-2989, DISULFIDE BONDS.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2420-2982.
  9. "Visualizing ATP-dependent RNA translocation by the NS3 helicase from HCV."
    Appleby T.C., Anderson R., Fedorova O., Pyle A.M., Wang R., Liu X., Brendza K.M., Somoza J.R.
    J. Mol. Biol. 405:1139-1153(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1029-1657 IN COMPLEX WITH ADP AND ZINC, DISULFIDE BONDS.

Entry informationi

Entry nameiQ99AU2_9HEPC
AccessioniPrimary (citable) accession number: Q99AU2
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.