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Protein

Genome polyprotein

Gene
N/A
Organism
Hepatitis GB virus B (GBV-B) (GB virus B)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Probably also regulates many host cellular functions such as antiviral state inhibition, cell transformation and apoptosis (By similarity).By similarity
Envelope glycoproteins E1 and E2 are involved in virus attachment to the host cell as well as in virus endocytosis and fusion with host membrane.By similarity
P13 may function as a multimeric ion channel protein (viroporin).1 Publication
Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3.By similarity
NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (By similarity). NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction and likely RNA stable secondary structure in the template strand. Cleaves and inhibits the human antiviral protein MAVS.By similarity1 Publication
NS5A is a component of the replication complex involved in RNA-binding.By similarity
NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication.By similarity

Catalytic activityi

Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per NS3 protease domain.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per NS5A N-terminal domain.By similarity
  • Mg2+, Mn2+Note: Magnesium or manganese ions for NS3 helicase activity.

Kineticsi

  1. KM=0.64 mM for ATP for NS3 NTPase
  2. KM=1.41 mM for CTP for NS3 NTPase
  3. KM=1.12 mM for UTP for NS3 NTPase
  4. KM=1.87 mM for dATP for NS3 NTPase
  5. KM=1.22 mM for dCTP for NS3 NTPase
  6. KM=0.65 mM for dTTP for NS3 NTPase

    pH dependencei

    Stable from 6 to 8.5.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei997 – 9971Charge relay system; for serine protease NS3 activityBy similarity
    Active sitei1021 – 10211Charge relay system; for serine protease NS3 activityBy similarity
    Metal bindingi1037 – 10371ZincBy similarity
    Metal bindingi1039 – 10391ZincBy similarity
    Active sitei1079 – 10791Charge relay system; for serine protease NS3 activityBy similarity
    Metal bindingi1085 – 10851ZincBy similarity
    Metal bindingi1089 – 10891ZincBy similarity
    Metal bindingi1905 – 19051ZincBy similarity
    Metal bindingi1923 – 19231ZincBy similarity
    Metal bindingi1925 – 19251ZincBy similarity
    Metal bindingi1947 – 19471ZincBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1144 – 11518ATPCurated

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, Ribonucleoprotein, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel

    Keywords - Biological processi

    Activation of host autophagy by virus, Apoptosis, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Interferon antiviral system evasion, Ion transport, Transcription, Transcription regulation, Transport, Viral attachment to host cell, Viral penetration into host cytoplasm, Viral RNA replication, Virus entry into host cell

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding, Viral nucleoprotein, Zinc

    Protein family/group databases

    MEROPSiC18.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 12 chains:
    OrganismiHepatitis GB virus B (GBV-B) (GB virus B)
    Taxonomic identifieri39113 [NCBI]
    Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridae
    Virus hostiCallithrix jacchus (White-tufted-ear marmoset) [TaxID: 9483]
    Saguinus [TaxID: 9486]

    Subcellular locationi

    Envelope glycoprotein E1 :
    • Virion membrane Curated; Single-pass type I membrane protein Curated
    • Host endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity

    • Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein (By similarity).By similarity
    Envelope glycoprotein E2 :
    • Virion membrane Curated; Single-pass type I membrane protein Curated
    • Host endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity

    • Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein (By similarity).By similarity
    Serine protease NS3 :
    Non-structural protein 5A :
    RNA-directed RNA polymerase :

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei133 – 15321HelicalSequence analysisAdd
    BLAST
    Transmembranei324 – 34421HelicalSequence analysisAdd
    BLAST
    Transmembranei582 – 60221HelicalSequence analysisAdd
    BLAST
    Transmembranei628 – 64821HelicalSequence analysisAdd
    BLAST
    Transmembranei660 – 68021HelicalSequence analysisAdd
    BLAST
    Transmembranei706 – 72621HelicalSequence analysisAdd
    BLAST
    Transmembranei737 – 75721HelicalSequence analysisAdd
    BLAST
    Transmembranei790 – 81021HelicalSequence analysisAdd
    BLAST
    Transmembranei847 – 86721HelicalSequence analysisAdd
    BLAST
    Transmembranei1565 – 158521HelicalSequence analysisAdd
    BLAST
    Transmembranei1653 – 167321HelicalSequence analysisAdd
    BLAST
    Transmembranei1678 – 169821HelicalSequence analysisAdd
    BLAST
    Transmembranei1722 – 174221HelicalSequence analysisAdd
    BLAST
    Transmembranei1783 – 180321HelicalSequence analysisAdd
    BLAST
    Transmembranei1864 – 188421HelicalSequence analysisAdd
    BLAST
    Transmembranei2844 – 286421HelicalSequence analysisAdd
    BLAST

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi613 – 6131G → A: Reduces cleavage between E2 and p13. 1 Publication
    Mutagenesisi669 – 6691G → N: Reduces cleavage between E2 and p13. 1 Publication
    Mutagenesisi730 – 7323ASA → NSN: Reduces cleavage between p13 and NS2-3. 1 Publication
    Mutagenesisi1150 – 11501K → A: Complete loss of ATPase and dsRNA unwinding activities. 1 Publication

    Keywords - Diseasei

    Oncogene

    Chemistry

    ChEMBLiCHEMBL5981.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 156156Core proteinSequence analysisPRO_0000037678Add
    BLAST
    Chaini157 – 349193Envelope glycoprotein E1PRO_0000037679Add
    BLAST
    Chaini350 – 613264Envelope glycoprotein E2PRO_0000037680Add
    BLAST
    Chaini614 – 732119p13CuratedPRO_0000037681Add
    BLAST
    Chaini614 – 66956p6Sequence analysisPRO_0000284104Add
    BLAST
    Chaini670 – 73263p7Sequence analysisPRO_0000284105Add
    BLAST
    Chaini733 – 940208Protease NS2-3PROSITE-ProRule annotationPRO_0000037682Add
    BLAST
    Chaini941 – 1564624Serine protease NS3Sequence analysisPRO_0000037683Add
    BLAST
    Chaini1565 – 161551Non-structural protein 4ASequence analysisPRO_0000037684Add
    BLAST
    Chaini1616 – 1863248Non-structural protein 4BSequence analysisPRO_0000037685Add
    BLAST
    Chaini1864 – 2274411Non-structural protein 5ASequence analysisPRO_0000037686Add
    BLAST
    Chaini2275 – 2864590RNA-directed RNA polymeraseSequence analysisPRO_0000037687Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi165 – 1651N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi212 – 2121N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi264 – 2641N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi380 – 3801N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi400 – 4001N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi422 – 4221N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi446 – 4461N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi467 – 4671N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi512 – 5121N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi782 – 7821N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi1057 – 10571N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi1273 – 12731N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi1559 – 15591N-linked (GlcNAc...); by hostSequence analysis
    Lipidationi1863 – 18631S-palmitoyl cysteine; by hostBy similarity
    Glycosylationi2640 – 26401N-linked (GlcNAc...); by hostSequence analysis
    Glycosylationi2722 – 27221N-linked (GlcNAc...); by hostSequence analysis

    Post-translational modificationi

    Specific enzymatic cleavages in vivo yield mature proteins. P13 may be further cleaved into p6 and p7 if the internal cleavage site is used.2 Publications
    Envelope E1 and E2 glycoproteins are highly N-glycosylated.
    NS5A is phosphorylated in a basal form termed p56. p58 is a hyperphosphorylated form of p56. p56 and p58 coexist in the cell in roughly equivalent amounts. Hyperphosphorylation is dependent on the presence of NS4A. Human AKT1, RPS6KB1/p70S6K, MAP2K1/MEK1, MAP2K6/MKK6 and CSNK1A1/CKI-alpha kinases may be responsible for NS5A phosphorylation (By similarity).By similarity
    NS4B is palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions (By similarity).By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei156 – 1572Cleavage; by host signal peptidaseSequence analysis
    Sitei349 – 3502Cleavage; by host signal peptidaseCurated
    Sitei613 – 6142Cleavage; by host signal peptidaseCurated
    Sitei669 – 6702Cleavage; by host signal peptidaseSequence analysis
    Sitei732 – 7332Cleavage; by host signal peptidaseCurated
    Sitei940 – 9412Cleavage; by protease NS2-3PROSITE-ProRule annotation
    Sitei?1564 – ?15652Cleavage; by serine protease NS3Sequence analysis
    Sitei1615 – 16162Cleavage; by serine protease NS3Sequence analysis
    Sitei1863 – 18642Cleavage; by serine protease NS3Sequence analysis
    Sitei2274 – 22752Cleavage; by serine protease NS3Sequence analysis

    Keywords - PTMi

    Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Interactioni

    Subunit structurei

    NS4A interacts with NS3 serine protease and stabilizes its folding. NS3-NS4A complex is essential for the activation of the latter and allows membrane anchorage of NS3. NS3 interacts with human MAVS (Probable).1 Publication

    Structurei

    Secondary structure

    1
    2864
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi745 – 76117Combined sources
    Turni766 – 7683Combined sources
    Helixi769 – 78517Combined sources
    Helixi849 – 86517Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LZPNMR-A734-764[»]
    2LZQNMR-A764-789[»]
    2MKBNMR-A845-869[»]
    DisProtiDP00674.
    ProteinModelPortaliQ69422.
    SMRiQ69422. Positions 1265-1366.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini819 – 940122Peptidase C18PROSITE-ProRule annotationAdd
    BLAST
    Domaini1131 – 1281151Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1284 – 1449166Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini2485 – 2603119RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1228 – 12314DECH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi172 – 19928Cys-richAdd
    BLAST
    Compositional biasi677 – 6815Poly-Ala
    Compositional biasi2145 – 218642Pro-richAdd
    BLAST
    Compositional biasi2232 – 22354Poly-Thr

    Domaini

    The N-terminal one-third of serine protease NS3 contains the protease activity. This region contains a zinc atom that does not belong to the active site, but may play a structural rather than a catalytic role. This region is essential for the activity of protease NS2-3, maybe by contributing to the folding of the latter. The helicase activity is located in the C-terminus of NS3 (By similarity).By similarity

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 peptidase C18 domain.PROSITE-ProRule annotation
    Contains 1 peptidase S29 domain.Curated
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding, Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011492. DEAD_Flavivir.
    IPR002521. HCV_core_C.
    IPR002519. HCV_env.
    IPR002518. HCV_NS2.
    IPR000745. HCV_NS4a.
    IPR001490. HCV_NS4b.
    IPR002868. HCV_NS5a.
    IPR013193. HCV_NS5a_1B_dom.
    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.
    PF01542. HCV_core. 1 hit.
    PF01539. HCV_env. 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.
    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.

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

    Q69422-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPVISTQTSP VPAPRTRKNK QTQASYPVSI KTSVERGQRA KRKVQRDARP
    60 70 80 90 100
    RNYKIAGIHD GLQTLAQAAL PAHGWGRQDP RHKSRNLGIL LDYPLGWIGD
    110 120 130 140 150
    VTTHTPLVGP LVAGAVVRPV CQIVRLLEDG VNWATGWFGV HLFVVCLLSL
    160 170 180 190 200
    ACPCSGARVT DPDTNTTILT NCCQRNQVIY CSPSTCLHEP GCVICADECW
    210 220 230 240 250
    VPANPYISHP SNWTGTDSFL ADHIDFVMGA LVTCDALDIG ELCGACVLVG
    260 270 280 290 300
    DWLVRHWLIH IDLNETGTCY LEVPTGIDPG FLGFIGWMAG KVEAVIFLTK
    310 320 330 340 350
    LASQVPYAIA TMFSSVHYLA VGALIYYASR GKWYQLLLAL MLYIEATSGN
    360 370 380 390 400
    PIRVPTGCSI AEFCSPLMIP CPCHSYLSEN VSEVICYSPK WTRPVTLEYN
    410 420 430 440 450
    NSISWYPYTI PGARGCMVKF KNNTWGCCRI RNVPSYCTMG TDAVWNDTRN
    460 470 480 490 500
    TYEACGVTPW LTTAWHNGSA LKLAILQYPG SKEMFKPHNW MSGHLYFEGS
    510 520 530 540 550
    DTPIVYFYDP VNSTLLPPER WARLPGTPPV VRGSWLQVPQ GFYSDVKDLA
    560 570 580 590 600
    TGLITKDKAW KNYQVLYSAT GALSLTGVTT KAVVLILLGL CGSKYLILAY
    610 620 630 640 650
    LCYLSLCFGR ASGYPLRPVL PSQSYLQAGW DVLSKAQVAP FALIFFICCY
    660 670 680 690 700
    LRCRLRYAAL LGFVPMAAGL PLTFFVAAAA AQPDYDWWVR LLVAGLVLWA
    710 720 730 740 750
    GRDRGPRIAL LVGPWPLVAL LTLLHLATPA SAFDTEIIGG LTIPPVVALV
    760 770 780 790 800
    VMSRFGFFAH LLPRCALVNS YLWQRWENWF WNVTLRPERF LLVLVCFPGA
    810 820 830 840 850
    TYDTLVTFCV CHVALLCLTS SAASFFGTDS RVRAHRMLVR LGKCHAWYSH
    860 870 880 890 900
    YVLKFFLLVF GENGVFFYKH LHGDVLPNDF ASKLPLQEPF FPFEGKARVY
    910 920 930 940 950
    RNEGRRLACG DTVDGLPVVA RLGDLVFAGL AMPPDGWAIT APFTLQCLSE
    960 970 980 990 1000
    RGTLSAMAVV MTGIDPRTWT GTIFRLGSLA TSYMGFVCDN VLYTAHHGSK
    1010 1020 1030 1040 1050
    GRRLAHPTGS IHPITVDAAN DQDIYQPPCG AGSLTRCSCG ETKGYLVTRL
    1060 1070 1080 1090 1100
    GSLVEVNKSD DPYWCVCGAL PMAVAKGSSG APILCSSGHV IGMFTAARNS
    1110 1120 1130 1140 1150
    GGSVSQIRVR PLVCAGYHPQ YTAHATLDTK PTVPNEYSVQ ILIAPTGSGK
    1160 1170 1180 1190 1200
    STKLPLSYMQ EKYEVLVLNP SVATTASMPK YMHATYGVNP NCYFNGKCTN
    1210 1220 1230 1240 1250
    TGASLTYSTY GMYLTGACSR NYDVIICDEC HATDATTVLG IGKVLTEAPS
    1260 1270 1280 1290 1300
    KNVRLVVLAT ATPPGVIPTP HANITEIQLT DEGTIPFHGK KIKEENLKKG
    1310 1320 1330 1340 1350
    RHLIFEATKK HCDELANELA RKGITAVSYY RGCDISKIPE GDCVVVATDA
    1360 1370 1380 1390 1400
    LCTGYTGDFD SVYDCSLMVE GTCHVDLDPT FTMGVRVCGV SAIVKGQRRG
    1410 1420 1430 1440 1450
    RTGRGRAGIY YYVDGSCTPS GMVPECNIVE AFDAAKAWYG LSSTEAQTIL
    1460 1470 1480 1490 1500
    DTYRTQPGLP AIGANLDEWA DLFSMVNPEP SFVNTAKRTA DNYVLLTAAQ
    1510 1520 1530 1540 1550
    LQLCHQYGYA APNDAPRWQG ARLGKKPCGV LWRLDGADAC PGPEPSEVTR
    1560 1570 1580 1590 1600
    YQMCFTEVNT SGTAALAVGV GVAMAYLAID TFGATCVRRC WSITSVPTGA
    1610 1620 1630 1640 1650
    TVAPVVDEEE IVEECASFIP LEAMVAAIDK LKSTITTTSP FTLETALEKL
    1660 1670 1680 1690 1700
    NTFLGPHAAT ILAIIEYCCG LVTLPDNPFA SCVFAFIAGI TTPLPHKIKM
    1710 1720 1730 1740 1750
    FLSLFGGAIA SKLTDARGAL AFMMAGAAGT ALGTWTSVGF VFDMLGGYAA
    1760 1770 1780 1790 1800
    ASSTACLTFK CLMGEWPTMD QLAGLVYSAF NPAAGVVGVL SACAMFALTT
    1810 1820 1830 1840 1850
    AGPDHWPNRL LTMLARSNTV CNEYFIATRD IRRKILGILE ASTPWSVISA
    1860 1870 1880 1890 1900
    CIRWLHTPTE DDCGLIAWGL EIWQYVCNFF VICFNVLKAG VQSMVNIPGC
    1910 1920 1930 1940 1950
    PFYSCQKGYK GPWIGSGMLQ ARCPCGAELI FSVENGFAKL YKGPRTCSNY
    1960 1970 1980 1990 2000
    WRGAVPVNAR LCGSARPDPT DWTSLVVNYG VRDYCKYEKL GDHIFVTAVS
    2010 2020 2030 2040 2050
    SPNVCFTQVP PTLRAAVAVD GVQVQCYLGE PKTPWTTSAC CYGPDGKGKT
    2060 2070 2080 2090 2100
    VKLPFRVDGH TPGVRMQLNL RDALETNDCN SINNTPSDEA AVSALVFKQE
    2110 2120 2130 2140 2150
    LRRTNQLLEA ISAGVDTTKL PAPSIEEVVV RKRQFRARTG SLTLPPPPRS
    2160 2170 2180 2190 2200
    VPGVSCPESL QRSDPLEGPS NLPSSPPVLQ LAMPMPLLGA GECNPFTAIG
    2210 2220 2230 2240 2250
    CAMTETGGGP DDLPSYPPKK EVSEWSDGSW STTTTASSYV TGPPYPKIRG
    2260 2270 2280 2290 2300
    KDSTQSAPAK RPTKKKLGKS EFSCSMSYTW TDVISFKTAS KVLSATRAIT
    2310 2320 2330 2340 2350
    SGFLKQRSLV YVTEPRDAEL RKQKVTINRQ PLFPPSYHKQ VRLAKEKASK
    2360 2370 2380 2390 2400
    VVGVMWDYDE VAAHTPSKSA KSHITGLRGT DVRSGAARKA VLDLQKCVEA
    2410 2420 2430 2440 2450
    GEIPSHYRQT VIVPKEEVFV KTPQKPTKKP PRLISYPHLE MRCVEKMYYG
    2460 2470 2480 2490 2500
    QVAPDVVKAV MGDAYGFVDP RTRVKRLLSM WSPDAVGATC DTVCFDSTIT
    2510 2520 2530 2540 2550
    PEDIMVETDI YSAAKLSDQH RAGIHTIARQ LYAGGPMIAY DGREIGYRRC
    2560 2570 2580 2590 2600
    RSSGVYTTSS SNSLTCWLKV NAAAEQAGMK NPRFLICGDD CTVIWKSAGA
    2610 2620 2630 2640 2650
    DADKQAMRVF ASWMKVMGAP QDCVPQPKYS LEELTSCSSN VTSGITKSGK
    2660 2670 2680 2690 2700
    PYYFLTRDPR IPLGRCSAEG LGYNPSAAWI GYLIHHYPCL WVSRVLAVHF
    2710 2720 2730 2740 2750
    MEQMLFEDKL PETVTFDWYG KNYTVPVEDL PSIIAGVHGI EAFSVVRYTN
    2760 2770 2780 2790 2800
    AEILRVSQSL TDMTMPPLRA WRKKARAVLA SAKRRGGAHA KLARFLLWHA
    2810 2820 2830 2840 2850
    TSRPLPDLDK TSVARYTTFN YCDVYSPEGD VFVTPQRRLQ KFLVKYLAVI
    2860
    VFALGLIAVG LAIS
    Length:2,864
    Mass (Da):312,705
    Last modified:November 1, 1996 - v1
    Checksum:i5F5A7D8FAF0CDE81
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti395 – 3951V → I.
    Natural varianti703 – 7031D → N.
    Natural varianti706 – 7061P → H.
    Natural varianti727 – 7271A → V.
    Natural varianti791 – 7911L → F.
    Natural varianti804 – 8041T → A.
    Natural varianti940 – 9401T → M.
    Natural varianti1879 – 18791F → L.
    Natural varianti1895 – 18951V → A.
    Natural varianti1919 – 19191L → P.
    Natural varianti1945 – 19451R → K.
    Natural varianti1966 – 19661R → G.
    Natural varianti1973 – 19731T → P.
    Natural varianti1979 – 19791Y → C.
    Natural varianti1990 – 19901L → M.
    Natural varianti2052 – 20521K → Q.
    Natural varianti2082 – 20821I → T.
    Natural varianti2095 – 20951L → P.
    Natural varianti2097 – 20971F → I.
    Natural varianti2174 – 21741S → P.
    Natural varianti2196 – 21961F → L.
    Natural varianti2201 – 22011C → R.
    Natural varianti2203 – 22031M → V.
    Natural varianti2221 – 22211E → G.
    Natural varianti2228 – 22281G → E.
    Natural varianti2233 – 22331T → A.
    Natural varianti2244 – 22441P → L.
    Natural varianti2268 – 22681G → E.
    Natural varianti2271 – 22711E → K.
    Natural varianti2833 – 28331V → I.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U22304 Genomic RNA. Translation: AAC54059.1.
    AF179612 Genomic RNA. Translation: AAF01368.1.
    AJ277947 Genomic RNA. Translation: CAC33083.1.
    AJ428955 Genomic RNA. Translation: CAD21957.1.
    AY534873 Genomic RNA. Translation: AAS45125.1.
    AY534874 Genomic RNA. Translation: AAS45126.1.
    AY534875 Genomic RNA. Translation: AAS45127.1.
    AY534876 Genomic RNA. Translation: AAS45128.1.
    AY534877 Genomic RNA. Translation: AAS45129.1.
    AY534878 Genomic RNA. Translation: AAS45130.1.
    RefSeqiNP_056931.1. NC_001655.1.

    Genome annotation databases

    GeneIDi1403460.
    KEGGivg:1403460.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U22304 Genomic RNA. Translation: AAC54059.1.
    AF179612 Genomic RNA. Translation: AAF01368.1.
    AJ277947 Genomic RNA. Translation: CAC33083.1.
    AJ428955 Genomic RNA. Translation: CAD21957.1.
    AY534873 Genomic RNA. Translation: AAS45125.1.
    AY534874 Genomic RNA. Translation: AAS45126.1.
    AY534875 Genomic RNA. Translation: AAS45127.1.
    AY534876 Genomic RNA. Translation: AAS45128.1.
    AY534877 Genomic RNA. Translation: AAS45129.1.
    AY534878 Genomic RNA. Translation: AAS45130.1.
    RefSeqiNP_056931.1. NC_001655.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LZPNMR-A734-764[»]
    2LZQNMR-A764-789[»]
    2MKBNMR-A845-869[»]
    DisProtiDP00674.
    ProteinModelPortaliQ69422.
    SMRiQ69422. Positions 1265-1366.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry

    ChEMBLiCHEMBL5981.

    Protein family/group databases

    MEROPSiC18.002.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi1403460.
    KEGGivg:1403460.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011492. DEAD_Flavivir.
    IPR002521. HCV_core_C.
    IPR002519. HCV_env.
    IPR002518. HCV_NS2.
    IPR000745. HCV_NS4a.
    IPR001490. HCV_NS4b.
    IPR002868. HCV_NS5a.
    IPR013193. HCV_NS5a_1B_dom.
    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.
    PF01542. HCV_core. 1 hit.
    PF01539. HCV_env. 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.
    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Toward a surrogate model for hepatitis C virus: an infectious molecular clone of the GB virus-B hepatitis agent."
      Bukh J., Apgar C.L., Yanagi M.
      Virology 262:470-478(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Generation of infectious and transmissible virions from a GB virus B full-length consensus clone in tamarins."
      Sbardellati A., Scarselli E., Verschoor E., De Tomassi A., Lazzaro D., Traboni C.
      J. Gen. Virol. 82:2437-2448(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    4. "Cell clones selected from the Huh7 human hepatoma cell line support efficient replication of a subgenomic GB virus B replicon."
      De Tomassi A., Pizzuti M., Graziani R., Sbardellati A., Altamura S., Paonessa G., Traboni C.
      J. Virol. 76:7736-7746(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 940-2864.
    5. Viazov S., Kioureguian K.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1864-2274.
    6. "Nucleoside triphosphatase and RNA helicase activities associated with GB virus B nonstructural protein 3."
      Zhong W., Ingravallo P., Wright-Minogue J., Skelton A., Uss A.S., Chase R., Yao N., Lau J.Y.N., Hong Z.
      Virology 261:216-226(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF SERINE PROTEASE NS3, MUTAGENESIS OF LYS-1150.
    7. "Characterization of GB virus B polyprotein processing reveals the existence of a novel 13-kDa protein with partial homology to hepatitis C virus p7 protein."
      Ghibaudo D., Cohen L., Penin F., Martin A.
      J. Biol. Chem. 279:24965-24975(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    8. "Functional analyses of GB virus B p13 protein: development of a recombinant GB virus B hepatitis virus with a p7 protein."
      Takikawa S., Engle R.E., Emerson S.U., Purcell R.H., St Claire M., Bukh J.
      Proc. Natl. Acad. Sci. U.S.A. 103:3345-3350(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF P13, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF GLY-613; 730-ALA--ALA-732 AND GLY-669.
    9. "GB virus B disrupts RIG-I signaling by NS3/4A-mediated cleavage of the adaptor protein MAVS."
      Chen Z., Benureau Y., Rijnbrand R., Yi J., Wang T., Warter L., Lanford R.E., Weinman S.A., Lemon S.M., Martin A., Li K.
      J. Virol. 81:964-976(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION OF NS3 PROTEASE WITH HUMAN MAVS.

    Entry informationi

    Entry nameiPOLG_GBVB
    AccessioniPrimary (citable) accession number: Q69422
    Secondary accession number(s): Q6QLR5
    , Q6QLR6, Q6QLR7, Q6QLR8, Q6QLR9, Q6QLS0, Q8JKE4, Q999T0, Q9QEW5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: November 1, 1996
    Last modified: May 11, 2016
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Of all animal viruses, GBV-B is the most closely related to HCV.

    Caution

    The core gene probably also codes for alternative reading frame proteins (ARFPs). Many functions depicted for the core protein might belong to the ARFPs.Curated

    Keywords - Technical termi

    3D-structure, Multifunctional enzyme

    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.