Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q66474 (POLG_EC06C)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Genome polyprotein

Gene
N/A
Organism
Echovirus 6 (strain Charles)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 cell receptor 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 cytoplasmic 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. 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. 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 similarity
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.

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 sitei878For Protease 2A activityBy similarity1
Active sitei896For Protease 2A activityBy similarity1
Active sitei967For Protease 2A activityBy similarity1
Active sitei1586For Protease 3C activitySequence analysis1
Active sitei1617For Protease 3C activitySequence analysis1
Active sitei1693For Protease 3C activityBy similarity1
Active sitei2058For RdRp activityBy similarity1

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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, Nucleotide-binding

Protein family/group databases

MEROPSiC03.011

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 17 chains:
P3
Protein 3AB
P2
P1
Capsid protein VP0
Alternative name(s):
VP4-VP2
Capsid protein VP4
Alternative name(s):
P1A
Virion protein 4
Capsid protein VP2
Alternative name(s):
P1B
Virion protein 2
Capsid protein VP3
Alternative name(s):
P1C
Virion protein 3
Capsid protein VP1
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
Viral protein genome-linked
Short name:
VPg
Alternative name(s):
Protein 3B
Short name:
P3B
Protein 3CD (EC:3.4.22.28)
Protease 3C (EC:3.4.22.28)
Short name:
P3C
RNA-directed RNA polymerase (EC:2.7.7.48)
Short name:
RdRp
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
OrganismiEchovirus 6 (strain Charles)
Taxonomic identifieri103913 [NCBI]
Taxonomic lineageiViruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus › Enterovirus B ›
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000002693 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 :
Viral protein genome-linked :
Protease 3C :
Protein 3CD :
RNA-directed RNA polymerase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 1501CytoplasmicSequence analysisAdd BLAST1500
Intramembranei1502 – 1517Sequence analysisAdd BLAST16
Topological domaini1518 – 2191CytoplasmicSequence analysisAdd BLAST674

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00004263862 – 2191Genome polyproteinBy similarityAdd BLAST2190
ChainiPRO_00004263872 – 849P1By similarityAdd BLAST848
ChainiPRO_00004263882 – 330Capsid protein VP0Sequence analysisAdd BLAST329
ChainiPRO_00004263892 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042639070 – 330Capsid protein VP2Sequence analysisAdd BLAST261
ChainiPRO_0000426391331 – 566Capsid protein VP3Sequence analysisAdd BLAST236
ChainiPRO_0000426392566 – 857Capsid protein VP1Sequence analysisAdd BLAST292
ChainiPRO_0000426393858 – 1435P2By similarityAdd BLAST578
ChainiPRO_0000426394858 – 1007Protease 2ASequence analysisAdd BLAST150
ChainiPRO_00000396751008 – 1106Protein 2BSequence analysisAdd BLAST99
ChainiPRO_00000396761107 – 1435Protein 2CSequence analysisAdd BLAST329
ChainiPRO_00004263951436 – 2191P3By similarityAdd BLAST756
ChainiPRO_00004263961436 – 1546Protein 3ABSequence analysisAdd BLAST111
ChainiPRO_00000396771436 – 1524Protein 3ASequence analysisAdd BLAST89
ChainiPRO_00004263971525 – 1546Viral protein genome-linkedSequence analysisAdd BLAST22
ChainiPRO_00004263981547 – 2191Protein 3CDSequence analysisAdd BLAST645
ChainiPRO_00004263991547 – 1728Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00004264001729 – 2191RNA-directed RNA polymeraseBy similarityAdd BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei1527O-(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
Sitei330 – 331Cleavage; by Protease 3CSequence analysis2
Sitei857 – 858Cleavage; by Protease 2ASequence analysis2
Sitei1007 – 1008Cleavage; by Protease 3CSequence analysis2
Sitei1435 – 1436Cleavage; by Protease 3CSequence analysis2
Sitei1524 – 1525Cleavage; by Protease 3CSequence analysis2
Sitei1546 – 1547Cleavage; by Protease 3CSequence analysis2
Sitei1729 – 1730Cleavage; by Protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRIDEiQ66474

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). 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 and with protein 3CD (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ66474
SMRiQ66474
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1211 – 1367SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1547 – 1712Peptidase C3Add BLAST166
Domaini1956 – 2072RdRp catalyticPROSITE-ProRule annotationAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni566 – 582Amphipatic alpha-helixSequence analysisAdd BLAST17
Regioni1436 – 1459DisorderedBy similarityAdd BLAST24

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

OrthoDBiVOG0900006M

Family and domain databases

CDDicd00205 rhv_like, 3 hits
Gene3Di1.10.10.870, 1 hit
2.60.120.20, 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
IPR036203 P3A_soluble_dom
IPR000081 Peptidase_C3
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR003138 Pico_P1A
IPR036988 Pico_P1A_sf
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.

Q66474-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAQVSTQKT GAHETGLSAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP 
        60         70         80         90        100
GKFTEPVKDI MAKTLPALNS PSAEECGYSD RVRSITLGNS TITTQESANV 
       110        120        130        140        150
VVGYGVWPDY LKDDEATAED QPTNPDVATC RFYTLDSVSW MKESQGWWWK 
       160        170        180        190        200
FPDALRDMGL FGQNMQYHYL GRSGYTIHVQ CNASKFHQGC LLVVCVPEAE 
       210        220        230        240        250
MGAATVNEKI NREHLSNGEV ANTFTGTKSS NTNGVQQAVF NAGMGVRVGN 
       260        270        280        290        300
LTVFPHQWIN LRTNNCATIV MPYINSVPMD NMFRHYNFTL MIIPFAKLDY 
       310        320        330        340        350
AAGSSTYIPI TVTVAPMCAE YNGLRLAGHQ GLPVMSTPGS NQFLTSDDYQ 
       360        370        380        390        400
SPTAMPQFDV TPEMHIPGEV KNLMEIAEVD SVVPVNNVNE NVNSLEAYRI 
       410        420        430        440        450
PVHSVTETGA QVFGFTLQPG ADSVMERTLH GEILNYYANW SGSIKLTFMY 
       460        470        480        490        500
CGSAMATGKF LLAYSPPGAG VPKNRKEAML GTHMIWDIGL QSRCVLCVPW 
       510        520        530        540        550
ISQTHYRFVS KDSYTDAGFI TCWYQTSIVV PAEVQNQSVI LCFVSACNDF 
       560        570        580        590        600
SVRLLRDSPF VTQTAFYQND VQNAVERSIV RVADTLPSGP SNSESIPALT 
       610        620        630        640        650
AAETGHTSQV VPSDTIQTRH VRNFHVRSES SVENFLSRSA CVYIVEYKTQ 
       660        670        680        690        700
DTTPDKMYDS WVINTRQVAQ LRRKLEFFTY VRFDVEVTFV ITSVQDDSTR 
       710        720        730        740        750
QNTDTPVLTH QIMYVPPGGP IPHAVDDYNW QTSTNPSVFW TEGNAPPRMS 
       760        770        780        790        800
IPFMSVGNAY SNFYDGWSHF SQTGVYGFNT LNNMGKLYFR HVNDRTISPI 
       810        820        830        840        850
TSKVRIYFKP KHVKAWVPRP PRLCEYTHKD NVDYEPKGVT TSRTSITITN 
       860        870        880        890        900
SKHMETHGAF GQQSGAAYVG NYRVVNRHLA THTDWQNCVW EDYNRDLLVS 
       910        920        930        940        950
TTTAHGCDTI ARCHCTTGVY FCASRNKHHP VVFEGPGLVE VQESGYYPKR 
       960        970        980        990       1000
YQSHVLLAAG LSEPGDCGGI LRCEHGVIGI VTMGGEGVVG FADVRDLLWL 
      1010       1020       1030       1040       1050
EDDAMEQGVK DYVEQLGNAF GSGFTNQICE QVNLLKESLI GQDSILEKSL 
      1060       1070       1080       1090       1100
KALVKIISAL VIVVRNHDDL ITVTATLALI GCTSSPWRWL KQKVSQYYGI 
      1110       1120       1130       1140       1150
SMAERQNNGW LKKFTEMTNA CKGMEWIAIK IQKFIEWLKV KILPEVREKH 
      1160       1170       1180       1190       1200
EFLNRLKQLP LLESQIATIE QSAPSQSDQE QLFSNVQYFA HYCRKYAPLY 
      1210       1220       1230       1240       1250
AAEAKRVFSL EKKMSNYIQF KSKCRIEPVC LLLHGSPGVG KSVATNLIGR 
      1260       1270       1280       1290       1300
SLAEKLNSSI YSLPPDPDHF DGYKQQAVVI MDDLCQNPDG KDVSLFCQMV 
      1310       1320       1330       1340       1350
SSVDFVPPMA ALEEKGILFT SPFVLASTNA GSINAPTVSD SRALARRFHF 
      1360       1370       1380       1390       1400
DMNIEVISMY NQNGKINMPM SVKTCDEECC PVNFKKCCPL VCGKAIQFID 
      1410       1420       1430       1440       1450
RRTQVRYSLD MLVTEMFREY NHRHSVGATL EALFQGPPVY REIKISVAPE 
      1460       1470       1480       1490       1500
IPPPPAIADL LKSVDSEAVR DYCKEKGWLV PEVNSTLQIE KHVSRAFICL 
      1510       1520       1530       1540       1550
QALTTFVSVA GIIYIIYKLF AGFQGAYTGM PNQKPKVPTL RQAKVQGPAF 
      1560       1570       1580       1590       1600
EFAVAMMKRN SSTVKTEYGE FTMLGIYDRW AVLPRHAKPG PTILMNDQEV 
      1610       1620       1630       1640       1650
GVVDAKELVD KDGTNLELTL LKLNRNEKFR DIRGFLAKEE VEVNEAVLAI 
      1660       1670       1680       1690       1700
NTSKFPNMYI PVGQVTDYGF LNLGGTPTKR MLMYNFPTRA GQCGGVLMST 
      1710       1720       1730       1740       1750
GKVLGIHVGG NGHQGFSAAL LKHYFNDEQG EIEFIESSKD AGYPVINTPS 
      1760       1770       1780       1790       1800
RTKLEPSVFH QVFEGSKEPA VLRNGDPRLK ANFEEAIFSK YIGNVNTHVD 
      1810       1820       1830       1840       1850
EYMLEAIDHY AGQLATLDIS TEPMKLEDAV YGTEGLEALD LTTSAGYPYV 
      1860       1870       1880       1890       1900
ALGIKKRDIL SKKTRDLTKL KECMDKYGLN LPMVTYVKDE LRSAEKVAKG 
      1910       1920       1930       1940       1950
KSRLIEASSL NDSVAMRQTF GNLYKAFHQN PGIVTGSAVG CDPDLFWSKI 
      1960       1970       1980       1990       2000
PVMLDGHLIA FDYSGYDASL SPVWFACLKL LLEKLGYTHK ETNYIDYLCN 
      2010       2020       2030       2040       2050
SHHLYRDKHY FVRGGMPSGC SGTSIFNSMI NNIIIRTLML KVYKGIDLDQ 
      2060       2070       2080       2090       2100
FRMIAYGDDV IASYPWPIDA SLLAEAGKDY GLIMTPADKG ECFNEVTWTN 
      2110       2120       2130       2140       2150
VTFLKRYFRA DEQYPFLVHP VMPMKDIHES IRWTKDPKNT QDHVRSLCLL 
      2160       2170       2180       2190 
AWHNGEQEYE EFIQKIRSVP VGRCLTLPAF STLRRKWLDS F
Length:2,191
Mass (Da):245,277
Last modified:January 23, 2007 - v3
Checksum:i47E70448B05716DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16283 Genomic RNA Translation: AAA65044.1

Similar proteinsi

Entry informationi

Entry nameiPOLG_EC06C
AccessioniPrimary (citable) accession number: Q66474
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 148 of the entry and version 3 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health