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Protein

Genome polyprotein

Gene
N/A
Organism
Coxsackievirus B3 (strain Nancy)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host CD55 and CXADR to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).By similarity
Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).By similarity
Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).By similarity
Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 (By similarity).By similarity
Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity (By similarity).By similarity
Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).By similarity
Viral protein genome-linked: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA (PubMed:18632861). VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (PubMed:18632861). VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).By similarity1 Publication
Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).By similarity
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).By similarity
RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated (By similarity).PROSITE-ProRule annotation

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
NTP + H2O = NDP + phosphate.

Cofactori (for Chain RNA-directed RNA polymerase)

Mg2+2 PublicationsNote: Requires the presence of 3CDpro or 3CPro.1 Publication

Enzyme regulationi

RNA-directed RNA polymerase: replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei872For Protease 2A activityBy similarity1
Active sitei890For Protease 2A activityBy similarity1
Active sitei961For Protease 2A activityBy similarity1
Active sitei1580For Protease 3C activitySequence analysis1
Active sitei1611For Protease 3C activitySequence analysis1
Active sitei1687For Protease 3C activityBy similarity1
Metal bindingi1956Magnesium1 Publication1
Active sitei2052For RdRp activityBy similarity1
Metal bindingi2053Magnesium1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
Biological processActivation of host autophagy by virus, DNA replication, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, 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, Magnesium, Metal-binding, Nucleotide-binding

Protein family/group databases

MEROPSiC03.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 17 chains:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
Protease 2A (EC:3.4.22.29)
Short name:
P2A
Alternative name(s):
Picornain 2A
Protein 2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Alternative name(s):
Protein 3B
Short name:
P3B
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
OrganismiCoxsackievirus B3 (strain Nancy)
Taxonomic identifieri103903 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007760 Componenti: Genome
  • UP000181225 Componenti: Genome

Subcellular locationi

Capsid protein VP0 :
Capsid protein VP4 :
Capsid protein VP2 :
Capsid protein VP3 :
Capsid protein VP1 :
Protein 2B :
Protein 2C :
Protein 3A :
Protein 3AB :
Protease 3C :
Protein 3CD :
RNA-directed RNA polymerase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 1495CytoplasmicSequence analysisAdd BLAST1494
Intramembranei1496 – 1511Sequence analysisAdd BLAST16
Topological domaini1512 – 2185CytoplasmicSequence analysisAdd BLAST674

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, Virion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2396505.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00004262662 – 2185Genome polyproteinBy similarityAdd BLAST2184
ChainiPRO_00004262672 – 848P1By similarityAdd BLAST847
ChainiPRO_00004262682 – 332Capsid protein VP0Sequence analysisAdd BLAST331
ChainiPRO_00004262692 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042627070 – 332Capsid protein VP2Sequence analysisAdd BLAST263
ChainiPRO_0000426271333 – 568Capsid protein VP3Sequence analysisAdd BLAST236
ChainiPRO_0000426272568 – 851Capsid protein VP1Sequence analysisAdd BLAST284
ChainiPRO_0000426273852 – 1429P2By similarityAdd BLAST578
ChainiPRO_0000426274852 – 1001Protease 2ASequence analysisAdd BLAST150
ChainiPRO_00000395871002 – 1100Protein 2BSequence analysisAdd BLAST99
ChainiPRO_00000395881101 – 1429Protein 2CSequence analysisAdd BLAST329
ChainiPRO_00004262751430 – 2185P3By similarityAdd BLAST756
ChainiPRO_00004262761430 – 1540Protein 3ABSequence analysisAdd BLAST111
ChainiPRO_00000395891430 – 1518Protein 3ASequence analysisAdd BLAST89
ChainiPRO_00004262771519 – 1540Viral protein genome-linkedSequence analysisAdd BLAST22
ChainiPRO_00004262781541 – 2185Protein 3CDSequence analysisAdd BLAST645
ChainiPRO_00004262791541 – 1722Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00004262801723 – 2185RNA-directed RNA polymeraseBy similarityAdd BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei1521O-(5'-phospho-RNA)-tyrosineBy similarity1

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity).By similarity
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion (By similarity).By similarity
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.By similarity
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion (By similarity).By similarity
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei69 – 70Cleavage; by autolysisSequence analysis2
Sitei332 – 333Cleavage; by Protease 3CSequence analysis2
Sitei851 – 852Cleavage; by Protease 2ASequence analysis2
Sitei1001 – 1002Cleavage; by Protease 3CSequence analysis2
Sitei1429 – 1430Cleavage; by Protease 3CSequence analysis2
Sitei1518 – 1519Cleavage; by Protease 3CSequence analysis2
Sitei1540 – 1541Cleavage; by Protease 3CSequence analysis2
Sitei1723 – 1724Cleavage; by Protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Expressioni

Inductioni

Translated cap independently from an internal ribosome entry site (IRES).1 Publication

Interactioni

Subunit structurei

Capsid protein VP1: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Interacts with host CD55 and CXADR. Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid (By similarity). Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 (By similarity). Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity). Protein 3AB: interacts with protein 3CD (By similarity). Viral protein genome-linked: interacts with RNA-directed RNA polymerase (By similarity). Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked (PubMed:18632861). RNA-directed RNA polymerase: interacts with protein 3CD (By similarity).By similarity1 Publication

Chemistry databases

BindingDBiP03313.

Structurei

Secondary structure

12185
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni1528 – 1530Combined sources3
Helixi1542 – 1554Combined sources13
Beta strandi1555 – 1560Combined sources6
Beta strandi1563 – 1572Combined sources10
Beta strandi1574 – 1578Combined sources5
Helixi1579 – 1581Combined sources3
Beta strandi1585 – 1589Combined sources5
Beta strandi1592 – 1603Combined sources12
Beta strandi1609 – 1617Combined sources9
Helixi1627 – 1629Combined sources3
Beta strandi1637 – 1644Combined sources8
Beta strandi1646 – 1649Combined sources4
Beta strandi1652 – 1667Combined sources16
Beta strandi1670 – 1680Combined sources11
Beta strandi1690 – 1693Combined sources4
Beta strandi1696 – 1705Combined sources10
Beta strandi1708 – 1713Combined sources6
Helixi1716 – 1719Combined sources4
Beta strandi1725 – 1731Combined sources7
Helixi1732 – 1735Combined sources4
Turni1752 – 1756Combined sources5
Beta strandi1761 – 1763Combined sources3
Helixi1777 – 1782Combined sources6
Helixi1795 – 1809Combined sources15
Turni1810 – 1812Combined sources3
Helixi1820 – 1825Combined sources6
Beta strandi1835 – 1837Combined sources3
Helixi1843 – 1845Combined sources3
Helixi1850 – 1853Combined sources4
Turni1856 – 1859Combined sources4
Helixi1862 – 1871Combined sources10
Beta strandi1877 – 1881Combined sources5
Beta strandi1885 – 1887Combined sources3
Helixi1888 – 1892Combined sources5
Beta strandi1898 – 1901Combined sources4
Helixi1904 – 1923Combined sources20
Turni1927 – 1930Combined sources4
Helixi1937 – 1947Combined sources11
Beta strandi1950 – 1953Combined sources4
Beta strandi1955 – 1959Combined sources5
Helixi1960 – 1963Combined sources4
Helixi1966 – 1978Combined sources13
Turni1983 – 1986Combined sources4
Helixi1987 – 1993Combined sources7
Beta strandi1994 – 1999Combined sources6
Beta strandi2002 – 2008Combined sources7
Helixi2017 – 2036Combined sources20
Helixi2042 – 2044Combined sources3
Beta strandi2046 – 2050Combined sources5
Beta strandi2053 – 2060Combined sources8
Helixi2064 – 2073Combined sources10
Beta strandi2078 – 2080Combined sources3
Beta strandi2083 – 2085Combined sources3
Turni2092 – 2094Combined sources3
Beta strandi2100 – 2104Combined sources5
Beta strandi2106 – 2108Combined sources3
Beta strandi2111 – 2115Combined sources5
Helixi2118 – 2125Combined sources8
Beta strandi2127 – 2129Combined sources3
Helixi2131 – 2133Combined sources3
Helixi2134 – 2145Combined sources12
Helixi2146 – 2148Combined sources3
Helixi2150 – 2160Combined sources11
Helixi2164 – 2168Combined sources5
Helixi2174 – 2184Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VB0X-ray2.40A1541-1723[»]
2ZTXX-ray1.72A1541-1723[»]
2ZTYX-ray1.72A1541-1723[»]
2ZTZX-ray2.00A/B1541-1723[»]
2ZU1X-ray1.38A/B1541-1723[»]
2ZU3X-ray1.75A1541-1723[»]
3CDUX-ray2.10A1724-2185[»]
3CDWX-ray2.50A1724-2185[»]
H1519-1540[»]
4WFXX-ray1.81A1724-2185[»]
4WFYX-ray2.06A1724-2185[»]
4WFZX-ray1.80A1724-2185[»]
4Y2AX-ray2.90A1724-2185[»]
ProteinModelPortaliP03313.
SMRiP03313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03313.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1205 – 1361SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1541 – 1706Peptidase C3Add BLAST166
Domaini1950 – 2066RdRp catalyticPROSITE-ProRule annotationAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni568 – 584Amphipatic alpha-helixSequence analysisAdd BLAST17
Regioni1430 – 1453DisorderedBy similarityAdd BLAST24

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

OrthoDBiVOG0900001E.

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
4.10.80.10. 1 hit.
InterProiView protein in InterPro
IPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
PfamiView protein in Pfam
PF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
SMARTiView protein in SMART
SM00382. AAA. 1 hit.
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiView protein in PROSITE
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P03313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAQVSTQKT GAHETRLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP
60 70 80 90 100
GKFTEPVKDI MIKSLPALNS PTVEECGYSD RARSITLGNS TITTQECANV
110 120 130 140 150
VVGYGVWPDY LKDSEATAED QPTQPDVATC RFYTLDSVQW QKTSPGWWWK
160 170 180 190 200
LPDALSNLGL FGQNMQYHYL GRTGYTVHVQ CNASKFHQGC LLVVCVPEAE
210 220 230 240 250
MGCATLDNTP SSAELLGGDT AKEFADKPVA SGSNKLVQRV VYNAGMGVGV
260 270 280 290 300
GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL
310 320 330 340 350
DYCPGSTTYV PITVTIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD
360 370 380 390 400
FQSPSAMPQY DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY
410 420 430 440 450
QIPVRSNEGS GTQVFGFPLQ PGYSSVFSRT LLGEILNYYT HWSGSIKLTF
460 470 480 490 500
MFCGSAMATG KFLLAYSPPG AGAPTKRVDA MLGTHVIWDV GLQSSCVLCI
510 520 530 540 550
PWISQTHYRF VASDEYTAGG FITCWYQTNI VVPADAQSSC YIMCFVSACN
560 570 580 590 600
DFSVRLLKDT PFISQQNFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA
610 620 630 640 650
LTAAETGHTS QVVPGDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYK
660 670 680 690 700
NSGAKRYAEW VLTPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ
710 720 730 740 750
NQDAQILTHQ IMYVPPGGPV PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSI
760 770 780 790 800
PFLSIGNAYS NFYDGWSEFS RNGVYGINTL NNMGTLYARH VNAGSTGPIK
810 820 830 840 850
STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFQPSGVTT TRQSITTMTN
860 870 880 890 900
TGAFGQQSGA VYVGNYRVVN RHLATSADWQ NCVWESYNRD LLVSTTTAHG
910 920 930 940 950
CDIIARCQCT TGVYFCASKN KHYPISFEGP GLVEVQESEY YPRRYQSHVL
960 970 980 990 1000
LAAGFSEPGD CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME
1010 1020 1030 1040 1050
QGVKDYVEQL GNAFGSGFTN QICEQVNLLK ESLVGQDSIL EKSLKALVKI
1060 1070 1080 1090 1100
ISALVIVVRN HDDLITVTAT LALIGCTSSP WRWLKQKVSQ YYGIPMAERQ
1110 1120 1130 1140 1150
NNSWLKKFTE MTNACKGMEW IAVKIQKFIE WLKVKILPEV REKHEFLNRL
1160 1170 1180 1190 1200
KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR
1210 1220 1230 1240 1250
VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL
1260 1270 1280 1290 1300
NSSVYSLPPD PDHFDGYKQQ AVVIMDDLCQ NPDGKDVSLF CQMVSSVDFV
1310 1320 1330 1340 1350
PPMAALEEKG ILFTSPFVLA STNAGSINAP TVSDSRALAR RFHFDMNIEV
1360 1370 1380 1390 1400
ISMYSQNGKI NMPMSVKTCD DECCPVNFKK CCPLVCGKAI QFIDRRTQVR
1410 1420 1430 1440 1450
YSLDMLVTEM FREYNHRHSV GTTLEALFQG PPVYREIKIS VAPETPPPPA
1460 1470 1480 1490 1500
IADLLKSVDS EAVREYCKEK GWLVPEINST LQIEKHVSRA FICLQALTTF
1510 1520 1530 1540 1550
VSVAGIIYII YKLFAGFQGA YTGVPNQKPR VPTLRQAKVQ GPAFEFAVAM
1560 1570 1580 1590 1600
MKRNSSTVKT EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK
1610 1620 1630 1640 1650
ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AKEEVEVNEA VLAINTSKFP
1660 1670 1680 1690 1700
NMYIPVGQVT EYGFLNLGGT PTKRMLMYNF PTRAGQCGGV LMSTGKVLGI
1710 1720 1730 1740 1750
HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPVI NTPSKTKLEP
1760 1770 1780 1790 1800
SVFHQVFEGN KEPAVLRSGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA
1810 1820 1830 1840 1850
VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK
1860 1870 1880 1890 1900
RDILSKKTKD LTKLKECMDK YGLNLPMVTY VKDELRSIEK VAKGKSRLIE
1910 1920 1930 1940 1950
ASSLNDSVAM RQTFGNLYKT FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG
1960 1970 1980 1990 2000
HLIAFDYSGY DASLSPVWFA CLKMLLEKLG YTHKETNYID YLCNSHHLYR
2010 2020 2030 2040 2050
DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY
2060 2070 2080 2090 2100
GDDVIASYPW PIDASLLAEA GKGYGLIMTP ADKGECFNEV TWTNATFLKR
2110 2120 2130 2140 2150
YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE
2160 2170 2180
HEYEEFIRKI RSVPVGRCLT LPAFSTLRRK WLDSF
Length:2,185
Mass (Da):243,453
Last modified:January 23, 2007 - v4
Checksum:i1B5ECE3DA47338FF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16R → G in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti177V → D in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti469P → L in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti487I → V in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti510F → Y in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti516Y → C in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti566Q → E in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti593T → N in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti650K → E in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti854 – 865FGQQS…VYVGN → IWTTIRGSVCGD in AAA74400 (PubMed:3027968).CuratedAdd BLAST12
Sequence conflicti873L → S in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1097A → P in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1280Q → H in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1437I → F in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1503V → M in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1616K → E in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1624R → G in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1627R → G in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1630L → V in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1718Y → N in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1734D → V in AAA74400 (PubMed:3027968).Curated1
Sequence conflicti1758E → V (PubMed:3027968).Curated1
Sequence conflicti1758E → V (PubMed:6088796).Curated1
Sequence conflicti1824V → R (PubMed:3027968).Curated1
Sequence conflicti1824V → R (PubMed:6088796).Curated1
Sequence conflicti1867C → R (PubMed:3027968).Curated1
Sequence conflicti1867C → R (PubMed:6088796).Curated1
Sequence conflicti1880Y → H (PubMed:3027968).Curated1
Sequence conflicti1880Y → H (PubMed:6088796).Curated1
Sequence conflicti2001D → N (PubMed:3027968).Curated1
Sequence conflicti2001D → N (PubMed:6088796).Curated1
Sequence conflicti2095A → V (PubMed:3027968).Curated1
Sequence conflicti2095A → V (PubMed:6088796).Curated1
Sequence conflicti2115V → A (PubMed:3027968).Curated1
Sequence conflicti2115V → A (PubMed:6088796).Curated1
Sequence conflicti2175S → T (PubMed:3027968).Curated1
Sequence conflicti2175S → T (PubMed:6088796).Curated1
Sequence conflicti2178R → G (PubMed:3027968).Curated1
Sequence conflicti2178R → G (PubMed:6088796).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33854 Genomic RNA. Translation: AAA42931.1.
K02709 Genomic RNA. Translation: AAA42932.1.
M16572 Genomic RNA. Translation: AAA74400.1.
PIRiA26354. GNNYB3.
A34664. GNNYBT.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33854 Genomic RNA. Translation: AAA42931.1.
K02709 Genomic RNA. Translation: AAA42932.1.
M16572 Genomic RNA. Translation: AAA74400.1.
PIRiA26354. GNNYB3.
A34664. GNNYBT.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VB0X-ray2.40A1541-1723[»]
2ZTXX-ray1.72A1541-1723[»]
2ZTYX-ray1.72A1541-1723[»]
2ZTZX-ray2.00A/B1541-1723[»]
2ZU1X-ray1.38A/B1541-1723[»]
2ZU3X-ray1.75A1541-1723[»]
3CDUX-ray2.10A1724-2185[»]
3CDWX-ray2.50A1724-2185[»]
H1519-1540[»]
4WFXX-ray1.81A1724-2185[»]
4WFYX-ray2.06A1724-2185[»]
4WFZX-ray1.80A1724-2185[»]
4Y2AX-ray2.90A1724-2185[»]
ProteinModelPortaliP03313.
SMRiP03313.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP03313.
ChEMBLiCHEMBL2396505.

Protein family/group databases

MEROPSiC03.011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG0900001E.

Miscellaneous databases

EvolutionaryTraceiP03313.

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
4.10.80.10. 1 hit.
InterProiView protein in InterPro
IPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
PfamiView protein in Pfam
PF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
SMARTiView protein in SMART
SM00382. AAA. 1 hit.
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiView protein in PROSITE
PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_CXB3N
AccessioniPrimary (citable) accession number: P03313
Secondary accession number(s): Q66322
, Q66323, Q66324, Q66325, Q66326, Q66327, Q66328, Q83744
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 12, 2017
This is version 177 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.