Skip Header

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

P12915

- POLG_BOVEV

UniProt

P12915 - POLG_BOVEV

(max 400 entries)x

Your basket is currently empty.

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
Bovine enterovirus (strain VG-5-27) (BEV)
Status
Reviewed - 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 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 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. 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei317 – 3182Cleavage; by Protease 3CSequence Analysis
Sitei840 – 8412Cleavage; by Protease 2ASequence Analysis
Active sitei861 – 8611For Protease 2A activityBy similarity
Active sitei879 – 8791For Protease 2A activityBy similarity
Active sitei950 – 9501For Protease 2A activityBy similarity
Sitei990 – 9912Cleavage; by Protease 3CSequence Analysis
Sitei1419 – 14202Cleavage; by Protease 3CSequence Analysis
Sitei1508 – 15092Cleavage; by Protease 3CSequence Analysis
Sitei1531 – 15322Cleavage; by Protease 3CSequence Analysis
Active sitei1571 – 15711For Protease 3C activitySequence Analysis
Active sitei1602 – 16021For Protease 3C activitySequence Analysis
Active sitei1678 – 16781For Protease 3C activitySequence Analysis
Sitei1714 – 17152Cleavage; by Protease 3CSequence Analysis
Active sitei2042 – 20421For RdRp activityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. ion channel activity Source: UniProtKB-KW
  4. RNA binding Source: UniProtKB-KW
  5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  6. RNA helicase activity Source: InterPro
  7. structural molecule activity Source: InterPro

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
  2. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
  3. induction by virus of host autophagy Source: UniProtKB
  4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  5. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
  6. protein oligomerization Source: UniProtKB-KW
  7. RNA-protein covalent cross-linking Source: UniProtKB-KW
  8. suppression by virus of host gene expression Source: UniProtKB-KW
  9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
  10. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  11. suppression by virus of host translation initiation factor activity Source: UniProtKB
  12. transcription, DNA-templated Source: InterPro
  13. viral RNA genome replication Source: InterPro
  14. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Activation 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

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.020.

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
OrganismiBovine enterovirus (strain VG-5-27) (BEV)
Taxonomic identifieri12065 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
ProteomesiUP000006566: Genome

Subcellular locationi

Chain Capsid protein VP0 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP2 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP3 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP1 : Virion By similarity. Host cytoplasm By similarity
Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 3AB : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain Protein 3CD : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
Chain RNA-directed RNA polymerase : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

GO - Cellular componenti

  1. host cell cytoplasmic vesicle Source: UniProtKB-KW
  2. integral to membrane of host cell Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 21752174Genome polyproteinBy similarityPRO_0000426107Add
BLAST
Chaini2 – 840839P1By similarityPRO_0000426108Add
BLAST
Chaini2 – 317316Capsid protein VP0Sequence AnalysisPRO_0000426109Add
BLAST
Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426110Add
BLAST
Chaini70 – 317248Capsid protein VP2Sequence AnalysisPRO_0000426111Add
BLAST
Chaini318 – 557240Capsid protein VP3Sequence AnalysisPRO_0000426112Add
BLAST
Chaini557 – 840284Capsid protein VP1Sequence AnalysisPRO_0000426113Add
BLAST
Chaini841 – 1419579P2By similarityPRO_0000426114Add
BLAST
Chaini841 – 990150Protease 2ASequence AnalysisPRO_0000039463Add
BLAST
Chaini991 – 108999Protein 2BSequence AnalysisPRO_0000039464Add
BLAST
Chaini1090 – 1419330Protein 2CSequence AnalysisPRO_0000039465Add
BLAST
Chaini1420 – 2175756P3By similarityPRO_0000426115Add
BLAST
Chaini1420 – 1531112Protein 3ABSequence AnalysisPRO_0000426116Add
BLAST
Chaini1420 – 150889Protein 3ASequence AnalysisPRO_0000039466Add
BLAST
Chaini1509 – 153123Viral protein genome-linkedSequence AnalysisPRO_0000426117Add
BLAST
Chaini1532 – 2175644Protein 3CDSequence AnalysisPRO_0000426118Add
BLAST
Chaini1532 – 1713182Protease 3CSequence AnalysisPRO_0000426119Add
BLAST
Chaini1714 – 2175462RNA-directed RNA polymeraseBy similarityPRO_0000426120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Modified residuei1511 – 15111O-(5'-phospho-RNA)-tyrosineBy similarity

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 uridylated 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

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRIDEiP12915.

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

Secondary structure

1
2175
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 353
Helixi36 – 383
Helixi51 – 544
Beta strandi57 – 593
Beta strandi78 – 814
Beta strandi83 – 875
Beta strandi90 – 967
Helixi103 – 1053
Turni113 – 1153
Helixi126 – 1283
Beta strandi147 – 1515
Helixi153 – 1553
Helixi159 – 1679
Beta strandi168 – 18013
Beta strandi187 – 19711
Beta strandi203 – 2053
Helixi209 – 2124
Helixi215 – 2173
Helixi224 – 2263
Turni227 – 2304
Helixi234 – 2385
Beta strandi239 – 2457
Turni246 – 2483
Beta strandi250 – 2567
Beta strandi261 – 2633
Turni267 – 2693
Beta strandi273 – 28917
Beta strandi294 – 30916
Turni325 – 3284
Beta strandi340 – 3423
Beta strandi356 – 3594
Helixi361 – 3644
Helixi382 – 3843
Beta strandi386 – 3894
Beta strandi397 – 4026
Helixi410 – 4134
Helixi415 – 4206
Beta strandi423 – 4286
Beta strandi430 – 4367
Beta strandi445 – 4517
Beta strandi453 – 4553
Helixi461 – 4644
Beta strandi467 – 4737
Beta strandi475 – 4773
Beta strandi479 – 4846
Beta strandi489 – 4913
Beta strandi493 – 4953
Turni499 – 5024
Helixi503 – 5064
Beta strandi510 – 5178
Beta strandi527 – 53711
Beta strandi542 – 5465
Helixi600 – 6023
Helixi610 – 6134
Helixi626 – 6283
Helixi630 – 6345
Beta strandi638 – 6414
Turni647 – 6493
Beta strandi651 – 6555
Helixi662 – 6687
Beta strandi671 – 68515
Beta strandi699 – 7057
Beta strandi714 – 7163
Helixi718 – 7214
Beta strandi723 – 7253
Beta strandi727 – 7315
Beta strandi737 – 7415
Beta strandi746 – 7527
Beta strandi756 – 7594
Helixi765 – 7673
Helixi772 – 7743
Beta strandi778 – 7858
Beta strandi792 – 80716
Beta strandi818 – 8203

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BEVX-ray3.001560-840[»]
270-317[»]
3318-559[»]
42-69[»]
ProteinModelPortaliP12915.
SMRiP12915. Positions 23-62, 74-559, 573-990, 1419-1480, 1532-2175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12915.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 14851484CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1502 – 2175674CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei1486 – 150116Sequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1194 – 1352159SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1532 – 1697166Peptidase C3Add
BLAST
Domaini1941 – 2056116RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni557 – 57418Amphipatic alpha-helixSequence AnalysisAdd
BLAST
Regioni1420 – 144324DisorderedBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 1 peptidase C3 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProiIPR004004. Helic/Pol/Pept_Calicivir-typ.
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.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF08727. 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.
[Graphical view]
PRINTSiPR00918. CALICVIRUSNS.
ProDomiPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12915-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAQLSRNTA GSHTTGTYAT GGSTINYNNI NYYSHAASAA QNKQDFTQDP
60 70 80 90 100
SKFTQPIADV IKETAVPLKS PSAEACGYSD RVAQLTLGNS TITTQEAANI
110 120 130 140 150
CVAYGCWPAK LSDTDATSVD KPTEPGVSAD AFYTLRSKPW QADSKGWYWK
160 170 180 190 200
LPDALNNTGM FGQNAQFHYI YRGGWAVHVQ CNATKFHQGT LLVLAIPEHQ
210 220 230 240 250
IATQEQPAFD RTMPGSEGGT FQEPFWLEDG TSLGNSLIYP HQWINLRTNN
260 270 280 290 300
SATLILPYVN AIPMDSAIRH SNWTLAIIPV APLKYAAETT PLVPITVTIA
310 320 330 340 350
PMETEYNGLR RAIASNQGLP TKPGPGSYQF MTTDEDCSPC ILPDFQPTLE
360 370 380 390 400
IFIPGKVNNL LEIAQVESIL EANNREGVEG VERYVIPVSV QDALDAQIYA
410 420 430 440 450
LRLELGGSGP LSSSLLGTLA KHYTQWSGSV EITCMFTGTF MTTGKVLLAY
460 470 480 490 500
TPPGGDMPRN REEAMLGTHV VWDFGLQSSI TLVIPWISAS HFRGVSNDDV
510 520 530 540 550
LNYQYYAAGH VTIWYQTNMV IPPGFPNTAG IIMMIAAQPN FSFRIQKDRE
560 570 580 590 600
DMTQTAILQN DPGKMLKDAI DKQVAGALVA GTTTSTHSVA TDSTPALQAA
610 620 630 640 650
ETGATSTARD ESMIETRTIV PTHGIHETSV ESFFGRSSLV GMPLLATGTS
660 670 680 690 700
ITNWRIDFRE FVQLRAKMSW FTYMRFDVEF TIIATSSTGQ NVTTEQHTTY
710 720 730 740 750
QVMYVPPGAP VPSNQDSFQW QSGCNPSVFA DTDGPPAQFS VPFMSSANAY
760 770 780 790 800
STVYDGYARF MDTDPDRYGI LPSNFLGFMY FRTLEDAAHQ VRFRICAKIK
810 820 830 840 850
HTSCWIPRAP RQAPYKKRYN LVFSGDSDRI CSNRASLTSY GPFGQQQGAA
860 870 880 890 900
YVGSYKILNR HLATYADWEN EVWQSYQRDL LVTRVDAHGC DTIARCNCRS
910 920 930 940 950
GIYYCKSTAK HYPIVVTPPS IYKIEANDYY PERMQTHILL GIGFAEPGDC
960 970 980 990 1000
GGLLRCEHGV MGILTVGGGD HVGFADVRDL LWIEDDAMEQ GITDYVQQLG
1010 1020 1030 1040 1050
NAFGAGFTAE IANYTNQLRD MLMGSDSVVE KIIRSLVRLV SALVIVVRNH
1060 1070 1080 1090 1100
QDLITVGATL ALLGCEGSPW KWLKRKVCQI LGINMAERQS DNWMKKFTEM
1110 1120 1130 1140 1150
CNAFRGLDWI AAKISKFIDW LKQKILPELK ERAEFVKKLK QLPLLEAQVN
1160 1170 1180 1190 1200
TLEHSSASQE RQEQLFGNVQ YLAHHCRKNA PLYAAEAKRV YHLEKRVLGA
1210 1220 1230 1240 1250
MQFKTKNRIE PVCALIHGSP GTGQSLATMI VGRKLAEYEG SDVYSLPPDP
1260 1270 1280 1290 1300
DHFDGYQQQA VVVMDDLLQN PDGKDMTLFC QMVSTAPFTV PMAALEDKGK
1310 1320 1330 1340 1350
LFTSKFVLAS TNAGQVTPPT VADYKALQRR FFFDCDIEVQ KEYKRDGVTL
1360 1370 1380 1390 1400
DVAKATETCE DCSPANFKKC MPLICGKALQ LKSRKGDGMR YSLDTLISEL
1410 1420 1430 1440 1450
RRESNRRYNI GNVLEALFQG PVCYKPLRIE VHEEEPAPSA ISDLLQAVDS
1460 1470 1480 1490 1500
EEVREYCRSK GWIVEERVTE LKLERNVNRA LAVIQSVSLI AAVAGTIYIV
1510 1520 1530 1540 1550
YRLFSGMQGP YSGIGTNYAT KKPVVRQVQT QGPLFDFGVS LLKKNIRTVK
1560 1570 1580 1590 1600
TGAGEFTALG VYDTVVVLPR HAMPGKTIEM NGKDIEVLDA YDLNDKTDTS
1610 1620 1630 1640 1650
LELTIVKLKM NEKFRDIRAM VPDQITDYNE AVVVVNTSYY PQLFTCVGRV
1660 1670 1680 1690 1700
KDYGFLNLAG RPTHRVLMYE FPTKAGQCGG VVISMGKIVG VHVGGNGAQG
1710 1720 1730 1740 1750
FAASLLRRYF TAEQGQIEYI EKSKDAGYPV INAPTQTKLE PSVFFDVFPG
1760 1770 1780 1790 1800
VKEPAVLHKK DKRLETNFEE ALFSKYIGNV QRDMPEELLI AIDHYSEQLK
1810 1820 1830 1840 1850
MLNIDPRPIS MEDAIYGTEG LEALDLGTSA SYPYVAMGIK KRDILNKETR
1860 1870 1880 1890 1900
DVTKMQECID KYGLNLPMVT YVKDELRAPD KIRKGKSRLI EASSLNDSVA
1910 1920 1930 1940 1950
MRCYFGNLYK VFHTNPGTIS GCAVGCDPET FWSKIPVMMD GELFGFDYTA
1960 1970 1980 1990 2000
YDASLSPMWF HALAEVLRRI GFVECKHFID QLCCSHHLYM DKHYYVVGGM
2010 2020 2030 2040 2050
PSGCSGTSIF NSMINNLIIR TLVLTVYKNI DLDDLKIIAY GDDVLASYPY
2060 2070 2080 2090 2100
EIDASLLAEA GKSFGLIMTP PDKSAEFVKL TWDNVTFLKR KFVRDARYPF
2110 2120 2130 2140 2150
LVHPVMDMSN IHESIRWTKD PRHTEDHVRS LCLLAWHCGE EEYNEFVTKI
2160 2170
RSVPVGRALH LPSFKALERK WYDSF
Length:2,175
Mass (Da):242,504
Last modified:January 23, 2007 - v3
Checksum:i44FCADE8704E48FD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00214 Genomic RNA. Translation: BAA24003.1. Sequence problems.
PIRiA29824. GNNYBE.
RefSeqiNP_045756.1. NC_001859.1.

Genome annotation databases

GeneIDi1493914.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00214 Genomic RNA. Translation: BAA24003.1 . Sequence problems.
PIRi A29824. GNNYBE.
RefSeqi NP_045756.1. NC_001859.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BEV X-ray 3.00 1 560-840 [» ]
2 70-317 [» ]
3 318-559 [» ]
4 2-69 [» ]
ProteinModelPortali P12915.
SMRi P12915. Positions 23-62, 74-559, 573-990, 1419-1480, 1532-2175.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.020.

Proteomic databases

PRIDEi P12915.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1493914.

Miscellaneous databases

EvolutionaryTracei P12915.

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProi IPR004004. Helic/Pol/Pept_Calicivir-typ.
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.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view ]
Pfami 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.
[Graphical view ]
PRINTSi PR00918. CALICVIRUSNS.
ProDomi PD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The complete nucleotide sequence of a bovine enterovirus."
    Earle J.A.P., Skuce R.A., Fleming C.S., Hoey E.M., Martin S.J.
    J. Gen. Virol. 69:253-263(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Implications for viral uncoating from the structure of bovine enterovirus."
    Smyth M., Tate J., Hoey E.M., Lyons C., Martin S.J., Stuart D.
    Nat. Struct. Biol. 2:224-231(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-840.

Entry informationi

Entry nameiPOLG_BOVEV
AccessioniPrimary (citable) accession number: P12915
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 150 of the entry and version 3 of the sequence. [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. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3