Genome polyprotein
Details
- Name
- Genome polyprotein
- Synonyms
- 3.4.22.29
- P2A
- Gene Name
- Not Available
- Organism
- BEV
- Amino acid sequence
>lcl|BSEQ0019540|Genome polyprotein MGAQLSRNTAGSHTTGTYATGGSTINYNNINYYSHAASAAQNKQDFTQDPSKFTQPIADV IKETAVPLKSPSAEACGYSDRVAQLTLGNSTITTQEAANICVAYGCWPAKLSDTDATSVD KPTEPGVSADAFYTLRSKPWQADSKGWYWKLPDALNNTGMFGQNAQFHYIYRGGWAVHVQ CNATKFHQGTLLVLAIPEHQIATQEQPAFDRTMPGSEGGTFQEPFWLEDGTSLGNSLIYP HQWINLRTNNSATLILPYVNAIPMDSAIRHSNWTLAIIPVAPLKYAAETTPLVPITVTIA PMETEYNGLRRAIASNQGLPTKPGPGSYQFMTTDEDCSPCILPDFQPTLEIFIPGKVNNL LEIAQVESILEANNREGVEGVERYVIPVSVQDALDAQIYALRLELGGSGPLSSSLLGTLA KHYTQWSGSVEITCMFTGTFMTTGKVLLAYTPPGGDMPRNREEAMLGTHVVWDFGLQSSI TLVIPWISASHFRGVSNDDVLNYQYYAAGHVTIWYQTNMVIPPGFPNTAGIIMMIAAQPN FSFRIQKDREDMTQTAILQNDPGKMLKDAIDKQVAGALVAGTTTSTHSVATDSTPALQAA ETGATSTARDESMIETRTIVPTHGIHETSVESFFGRSSLVGMPLLATGTSITNWRIDFRE FVQLRAKMSWFTYMRFDVEFTIIATSSTGQNVTTEQHTTYQVMYVPPGAPVPSNQDSFQW QSGCNPSVFADTDGPPAQFSVPFMSSANAYSTVYDGYARFMDTDPDRYGILPSNFLGFMY FRTLEDAAHQVRFRICAKIKHTSCWIPRAPRQAPYKKRYNLVFSGDSDRICSNRASLTSY GPFGQQQGAAYVGSYKILNRHLATYADWENEVWQSYQRDLLVTRVDAHGCDTIARCNCRS GIYYCKSTAKHYPIVVTPPSIYKIEANDYYPERMQTHILLGIGFAEPGDCGGLLRCEHGV MGILTVGGGDHVGFADVRDLLWIEDDAMEQGITDYVQQLGNAFGAGFTAEIANYTNQLRD MLMGSDSVVEKIIRSLVRLVSALVIVVRNHQDLITVGATLALLGCEGSPWKWLKRKVCQI LGINMAERQSDNWMKKFTEMCNAFRGLDWIAAKISKFIDWLKQKILPELKERAEFVKKLK QLPLLEAQVNTLEHSSASQERQEQLFGNVQYLAHHCRKNAPLYAAEAKRVYHLEKRVLGA MQFKTKNRIEPVCALIHGSPGTGQSLATMIVGRKLAEYEGSDVYSLPPDPDHFDGYQQQA VVVMDDLLQNPDGKDMTLFCQMVSTAPFTVPMAALEDKGKLFTSKFVLASTNAGQVTPPT VADYKALQRRFFFDCDIEVQKEYKRDGVTLDVAKATETCEDCSPANFKKCMPLICGKALQ LKSRKGDGMRYSLDTLISELRRESNRRYNIGNVLEALFQGPVCYKPLRIEVHEEEPAPSA ISDLLQAVDSEEVREYCRSKGWIVEERVTELKLERNVNRALAVIQSVSLIAAVAGTIYIV YRLFSGMQGPYSGIGTNYATKKPVVRQVQTQGPLFDFGVSLLKKNIRTVKTGAGEFTALG VYDTVVVLPRHAMPGKTIEMNGKDIEVLDAYDLNDKTDTSLELTIVKLKMNEKFRDIRAM VPDQITDYNEAVVVVNTSYYPQLFTCVGRVKDYGFLNLAGRPTHRVLMYEFPTKAGQCGG VVISMGKIVGVHVGGNGAQGFAASLLRRYFTAEQGQIEYIEKSKDAGYPVINAPTQTKLE PSVFFDVFPGVKEPAVLHKKDKRLETNFEEALFSKYIGNVQRDMPEELLIAIDHYSEQLK MLNIDPRPISMEDAIYGTEGLEALDLGTSASYPYVAMGIKKRDILNKETRDVTKMQECID KYGLNLPMVTYVKDELRAPDKIRKGKSRLIEASSLNDSVAMRCYFGNLYKVFHTNPGTIS GCAVGCDPETFWSKIPVMMDGELFGFDYTAYDASLSPMWFHALAEVLRRIGFVECKHFID QLCCSHHLYMDKHYYVVGGMPSGCSGTSIFNSMINNLIIRTLVLTVYKNIDLDDLKIIAY GDDVLASYPYEIDASLLAEAGKSFGLIMTPPDKSAEFVKLTWDNVTFLKRKFVRDARYPF LVHPVMDMSNIHESIRWTKDPRHTEDHVRSLCLLAWHCGEEEYNEFVTKIRSVPVGRALH LPSFKALERKWYDSF
- Number of residues
- 2175
- Molecular Weight
- 242501.72
- Theoretical pI
- 6.49
- GO Classification
- FunctionsATP binding / cysteine-type endopeptidase activity / ion channel activity / RNA binding / RNA helicase activity / RNA-directed RNA polymerase activity / structural molecule activityProcessesDNA replication / endocytosis involved in viral entry into host cell / induction by virus of host autophagy / pore formation by virus in membrane of host cell / pore-mediated entry of viral genome into host cell / positive stranded viral RNA replication / protein oligomerization / RNA-protein covalent cross-linking / suppression by virus of host gene expression / suppression by virus of host mRNA export from nucleus / suppression by virus of host RIG-I activity by RIG-I proteolysis / suppression by virus of host translation initiation factor activity / transcription, DNA-templated / viral RNA genome replication / virion attachment to host cellComponentshost cell cytoplasmic vesicle membrane / integral to membrane of host cell / membrane / T=pseudo3 icosahedral viral capsid
- General Function
- Structural molecule activity
- Specific Function
- 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).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).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).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).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).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).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).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).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).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).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).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).Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (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).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Virion
- Gene sequence
>lcl|BSEQ0019541|Genome polyprotein ATGGGAGCCCAGTTGAGCAGAAATACTGCCGGGAGCCACACTACTGGAACCTACGCTACC GGAGGCTCAACCATTAATTATAACAACATTAACTACTACAGCCACGCCGCTTCTGCAGCG CAGAACAAACAAGACTTCACCCAGGACCCATCCAAGTTCACTCAGCCAATTGCGGATGTG ATAAAGGAGACAGCGGTTCCACTTAAGTCACCAAGCGCAGAAGCGTGCGGTTACAGTGAT CGCGTAGCCCAGTTGACACTTGGCAACAGCACTATCACTACCCAAGAGGCAGCAAATATA TGCGTTGCTTATGGCTGCTGGCCTGCAAAGCTTAGCGACACTGATGCCACATCAGTGGAC AAGCCCACTGAACCAGGTGTATCAGCGGAGCGCTTTTATACCCTCCGTTCCAAGCCGTGG CAGGCAGATAGCAAGGGGTGGTATTGGAAGCTACCCGATGCACTCAACAATACAGGAATG TTTGGACAGAACGCCCAGTTCCACTACATCTATAGAGGTGGGTGGGCAGTGCACGTCCAA TGCAATGCAACCAAATTCCACCAGGGCACGCTCCTTGTGCTTGCAATCCCAGAACACCAA ATCGCCACACAAGAGCAGCCCGCTTTTGACAGAACCATGCCAGGCAGCGAAGGCGGCACT TTCCAAGAGCCCTTCTGGCTCGAGGATGGAACGTCTTTAGGAAACTCCCTGATCTATCCG CACCAGTGGATCAACCTTAGGACAAACAATTCAGCAACCCTGATATTACCATACGTGAAT GCCATTCCGATGGACTCGGCCATTAGGCATTCAAATTGGACACTAGCTATCATTCCAGTT GCACCCTTGAAATATGCAGCCGAGACCACGCCGCTTGTCCCCATTACTGTGACTATCGCA CCGATGGAGACGGAGTACAACGGGCTTAGACGCGCTATAGCTAGCAATCAAGGCCTTCCA ACTAAGCCAGGGCCAGGTTCCTACCAGTTCATGACTACTGATGAGGATTGTTCCCCGTGC ATTTTGCCTGATTTCCAGCCGACCCCTGAAATTTTCATCCCTGGTAAGGTCAATAACCTT TTGGAAATTGCGCAAGTTGAGTCTATCCTTGAGGCCAACAACAGGGAAGGGGTAGAGGGT GTTGAGCGGTATGTCATCCCAGTAAGTGTTCAGGACGCATTGGATGCCCAGATTTATGCC CTAAGACTTGAGCTTGGCGGAAGTGGCCCTCTCTCCTCCAGCCTTCTAGGTACCTTAGCA AAGCATTATACCCAATGGAGTGGGTCAGTGGAGATCACCTGCATGTTCACTGGCACCTTC ATGACAACAGGAAAGGTCCTCTTGGCATACACACCTCCAGGTGGAGATATGCCTAGGAAT AGAGAAGAAGCCATGCTTGGAACGCATGTTGTCTGGGACTTTGGTCTACAATCATCAATA ACCTTGGTCATACCTTGGATCTCTGCATCACATTTTAGAGGAGTCAGTAATGACGATGTG CTGAATTACCAATATTATGCAGCAGGTCATGTCACCATCTGGTACCAAACAAACATGGTA ATCCCTCCGGGATTCCCTAACACGGCAGGCATAATCATGATGATTGCCGCACAGCCAAAC TTCTCCTTCCGCATTCAAAAGGATAGGGAAGACATGACCCAAACTGCAATTCTGCAGAAT GACCCAGGCAAGATGCTAAAGGATGCGATTGACAAACAAGTTGCAGGAGCCCTAGTTGCT GGTACCACGACATCCACCCACTCAGTAGCCACGGACAGCACACCAGCCCTGCAGGCCGCT GAGACTGGTGCCACGTCAACTGCCAGGGATGAGAGCATGATTGAGACCCGCACTATTGTG CCGACTCACGGTATCCACGAGACAAGTGTGGAGAGTTTCTTTGGACGCTCCTCACTCGTG GGTATGCCGCTGCTGGCCACTGGCACCAGTATCACCAACTGGCGCATTGACTTCAGGGAG TTCGTCCAGTTGAGAGCCAAGATGTCCTGGTTTACTTACATGCGCTTTGACGTGGAGTTC ACCATAATTGCAACAAGTTCTACTGGGCAGAATGTTACCACCGAGCAGCACACCACTTAC CAGGTGATGTACGTCCCCCCTGGGGCACCCGTTCCCTCCAATCAAGACTCATTTCAGTGG CAATCTGGGTGCAACCCCTCGGTATTCGCGGACACGGACGGACCACCTGCCCAATTCTCA GTACCCTTCATGAGCTCAGCCAATGCGTATTCCACGGTTTATGATGGGTACGCACGATTC ATGGACACTGACCCAGATAGATATGGCATCCTCCCGAGCAATTTCCTGGGATTCATGTAC TTCAGGACACTCGAAGACGCAGCACACCAAGTAAGGTTCCGCATCTGTGCCAAAATAAAA CACACCAGCTGCTGGATCCCACGTGCACCCAGACAAGCACCATACAAGAAGAGGTACAAC CTGGTATTCAGTGGGGATTCCGACAGGATTTGTTCTAACAGAGCCAGCTTGACTAGCTAT GGACCCTTTGGGCAGCAGCAGGGTGCTGCGTATGTGGGCTCCTACAAAATTTTAAACAGA CACCTTGCCACATACGCTGATTGGGAAAATGAAGTCTGGCAATCTTACCAGCGTGATCTA CTTGTTACTAGAGTTGATGCTCACGGGTGTGACACCATCGCTCGATGCAATTGCAGATCT GGTATCTATTACTGCAAATCCACAGCCAAGCACTATCCTATTGTAGTCACGCCCCCATCT ATCTACAAGATTGAGGCCAACGATTATTACCCAGAAAGAATGCAAACTCACATCCTTCTT GGGATTGGCTTCGCTGAGCCCGGTGATTGCGGTGGTCTTCTTCGTTGTGAGCATGGTGTT ATGGGCATTCTTACGGTTGGCGGTGGAGACCATGTCGGGTTTGCAGATGTTCGTGACCTC CTTTGGATAGAGGATGACGCCATGGAACAGGGAATCACTGACTACGTCCAACAGTTAGGC AATGCCTTTGGAGCTGGATTCACTGCTGAGATTGCAAATTACACCAACCAACTCAGGGAC ATGTTAATGGGCTCAGATTCAGTAGTAGAGAAGATCATTAGGTCTCTTGTCCGACTGGTT TCTGCGCTGGTTATAGTGGTGAGAAACCACCAGGATTTGATTACCGTGGGAGCAACCCTC GCCCTTCTAGGTTGTGAAGGCTCTCCATGGAAATGGCTGAAGAGAAAGGTTTGCCAAATT CTTGGAATCAACATGGCAGAAAGGCAGTCAGACAACTGGATGAAAAAGTTCACTGAGATG TGCAACGCCTTCAGAGGCCTAGACTGGATCGCAGCAAAAATCTCCAAGTTTATTGATTGG CTTAAACAAAAGATCCTACCAGAACTCAAAGAGAGAGCAGAGTTCGTCAAGAAGTTAAAA CAGCTCCCACTCTTAGAGGCTCAGGTGAACACTCTGGAACACTCTTCCGCTAGTCAGGAG AGGCAAGAACAATTGTTTGGGAATGTTCAGTACCTTGCCCATCATTGTAGAAAGAACGCC CCGCTTTATGCCGCAGAAGCTAAGCGCGTCTACCATCTAGAGAAGCGCGTCCTCCGTGCC ATGCAGTTCAAGACCAAGAACCGCATTGAACCTGTATGTGCACTGATTCATGGCTCACCT GGTACCGGTCAGTCGTTGGCTACTATGATAGTAGGAAGAAAACTGGCTGAGTACGAAGGT TCCGACGTCTACTCCCTACCGCCTGACCCGGATCATTTTGATGGCTACCAACAACAAGCC GTCGTAGTGATGGATGATTTACTTCAAAACCCCGATGGGAAGGACATGACCTTGTTTTGC CAAATGGTTTCGACGGCTCCTTTTACTGTGCCCATGGCTGCTTTGGAGGATAAGGGGAAG CTCTTCACTTCCAAATTTGTGCTAGCTTCTACTAATGCAGGCCAAGTTACTCCGCCAACC GTGGCTGATTATAAGGCGCTGCAGAGAAGGTTTTTCTTTGATTGTGACATTGAGGTCCAG AAGGAATACAAAAGAGATGGGGTCACTCTGGATGTGGCCAAGGCTACTGAGACCTGTGAA GACTGCTCCCCAGCCAATTTCAAGAAGTGCATGCCGTTGATTTGCGGAAAGGCCCTCCAG CTAAAATCGCGCAAGGGCGATGGGATGAGATACAGCCTGGACACCCTGATTAGTGAGCTT CGGCGTGAGAGCAACCGCCGTTACAATATTGGCAACGTCCTTGAGGCCCTGTTCCAAGGG CCAGTGTGTTATAAGCCTCTTAGAATTGAAGTTCATGAGGAAGAACCAGCACCTTCCGCC ATTAGCGATTTGCTGCAGGCAGTCGATAGTGAGGAGGTGAGGGAATATTGCAGGTCCAAG GGTTGGATTGTTGAAGAGAGGGTCACTGAACTTAAGCTTGAGCGCAACGTGAACCGTGCG CTGGCAGTCATTCAGAGTGTGTCTCTCATTGCTGCAGTGGCTGGGACCATTTACATAGTT TATCGCCTCTTTTCTGGTATGCAGGGCCCTTACTCAGGTATCGGCACAAACTACGCCACA AAGAAACCAGTGGTAAGACAGGTACAAACCCAAGGTCCTCTTTTTGATTTCGGCGTCTCC CTACTTAAGAAGAACATTAGGACAGTCAAAACAGGTGCAGGCGAGTTTACCGCCCTGGGG GTTTATGATACTGTGGTGGTCCTGCCCCGCCATGCCATGCCTGGCAAGACCATTGAAATG AATGGGAAGGACATTGAAGTTTTGGACGCTTATGACCTCAACGACAAGACCGACACTTCT CTAGAATTGACCATAGTGAAATTGAAAATGAATGAGAAGTTCAGGGACATTAGAGCAATG GTTCCGGACCAAATTACAGATTACAATGAGGCAGTGGTGGTTGTGAATACCTCATACTAC CCCCAGCTTTTTACCTGCGTGGGGCGTGTCAAGGACTACGGATTCCTGAACCTTGCTGGC AGGCCAACACATAGAGTTTTGATGTATGAATTCCCCACCAAGGCAGGCCAATGCGGTGGT GTGGTTATTAGCATGGGTAAGATAGTGGGTGTCCACGTAGGAGGTAACGGTGCCCAAGGT TTTGCCGCCTCCCTTCTACGCAGGTACTTTACAGCAGAACAAGGACAAATTGAATATATC GAGAAGAGTAAAGATGCCGGGTACCCCGTGATCAATGCACCCACCCAAACCAAATTAGAG CCCAGTGTTTTCTTTGATGTTTTCCCCGGGGTGAAAGAACCAGCGGTACTCCACAAGAAG GACAAGAGGCTTGAAACCAACTTTGAGGAAGCTCTATTTTCCAAGTACATAGGAAATGTA CAAAGGGACATGCCTGAGGAATTACTCATTGCCATAGATCATTATTCTGAACAACTCAAA ATGTTGAATATTGACCCGAGGCCCATTTCAATGGAGGATGCAATTTACGGTACAGAGGGG CTTGAGGCACTTGATCTTGGAACTAGTGCGAGCTACCCGTACGTTGCAATGGGCATCAAG AAAAGAGATATTTTGAATAAAGAGACCAGGGATGTCACTAAGATGCAAGAGTGCATAGAT AAGTATGGTTTAAATCTACCCATGGTCACCTATGTCAAGGATGAACTCAGGGCGCCAGAT AAGATCAGGAAAGGAAAAAGCCGTTTGATAGAGGCATCTAGCTTGAATGATTCAGTAGCC ATGCGGTGCTACTTTGGGAACCTCTACAAGGTTTTCCACACCAACCCTGGAACCATCTCC GGCTGTGCCGTTGGATGCGACCCTGAAACCTTCTGGAGCAAGATCCCAGTGATGATGGAT GGTGAGCTTTTTGGCTTTGATTATACTGCATATGATGCTAGCCTGTCTCCCATGTGGTTC CATGCCCTGGCAGAAGTCCTTAGACGGATTGGATTTGTTGAGTGCAAGCACTTTATTGAT CAACTTTGCTGCAGCCACCACCTTTATATGGATAAGCACTATTATGTGGTTGGGGGCATG CCTTCTGGCTGCTCTGGCACCTCCATCTTCAATTCTATGATTAACAACCTAATCATCCGC ACTCTTGTGCTCACAGTTTATAAAAATATTGATTTGGATGATCTTAAGATAATAGCCTAC GGGGATGACGTGCTCGCGTCGTACCCGTATGAGATTGATGCCAGCCTCTTGGCAGAAGCT GGTAAAAGCTTTGGTCTAATCATGACTCCACCAGATAAATCTGCGGAGTTTGTCAAATTA ACCTGGGATAACGTGACCTTTTTGAAGAGGAAGTTCGTGCGTGATGCACGGTACCCTTTC CTTGTACATCCGGTCATGGACATGTCGAACATCCATGAGTCCATTCGGTGGACGAAAGAT CCCAGGCATACTGAAGACCATGTCCGCTCACTTTGCCTATTGGCCTGGCATTGTGGCGAG GAAGAATACAACGAATTTGTTACAAAGATCCGTTCCGTTCCTGTCGGGAGAGCCCTCCAT CTACCTTCATTCAAGGCGCTCGAGAGGAAATGGTACGACTCTTTCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P12915 UniProtKB Entry Name POLG_BOVEV GenBank Protein ID 2696867 GenBank Gene ID D00214 - General References
- Earle JA, Skuce RA, Fleming CS, Hoey EM, Martin SJ: The complete nucleotide sequence of a bovine enterovirus. J Gen Virol. 1988 Feb;69 ( Pt 2):253-63. [Article]
- Smyth M, Tate J, Hoey E, Lyons C, Martin S, Stuart D: Implications for viral uncoating from the structure of bovine enterovirus. Nat Struct Biol. 1995 Mar;2(3):224-31. [Article]