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P36290

- POLG_CXA24

UniProt

P36290 - POLG_CXA24

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Protein
Genome polyprotein
Gene
N/A
Organism
Coxsackievirus A24 (strain EH24/70)
Status
Reviewed - Annotation score: 5 out of 5 - 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.
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.

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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
Sitei69 – 702Cleavage; by autolysis Reviewed prediction
Sitei340 – 3412Cleavage; by Protease 3C Reviewed prediction
Active sitei906 – 9061For Protease 2A activity By similarity
Active sitei924 – 9241For Protease 2A activity By similarity
Active sitei995 – 9951For Protease 2A activity By similarity
Sitei1035 – 10362Cleavage; by Protease 3C Reviewed prediction
Sitei1132 – 11332Cleavage; by Protease 3C Reviewed prediction
Sitei1461 – 14622Cleavage; by Protease 3C Reviewed prediction
Sitei1548 – 15492Cleavage; by Protease 3C Reviewed prediction
Sitei1570 – 15712Cleavage; by Protease 3C Reviewed prediction
Active sitei1610 – 16101For Protease 3C activity Reviewed prediction
Active sitei1641 – 16411For Protease 3C activity Reviewed prediction
Active sitei1717 – 17171For Protease 3C activity By similarity
Sitei1753 – 17542Cleavage; by Protease 3C Reviewed prediction
Active sitei2081 – 20811For RdRp activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1261 – 12688ATP Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
  2. RNA-protein covalent cross-linking Source: UniProtKB-KW
  3. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
  4. induction by virus of host autophagy Source: UniProtKB
  5. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  6. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
  7. protein oligomerization Source: UniProtKB-KW
  8. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
  10. suppression by virus of host translation Source: UniProtKB-KW
  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

MEROPSiC03.001.

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 A24 (strain EH24/70)
Taxonomic identifieri36404 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007759: 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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 15251524Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1526 – 154116 Reviewed prediction
Add
BLAST
Topological domaini1542 – 2214673Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW
  2. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  3. integral to membrane of host cell Source: UniProtKB-KW
  4. membrane 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 host By similarity
Chaini2 – 22142213Genome polyprotein By similarity
PRO_0000426221Add
BLAST
Chaini2 – 885884P1 By similarity
PRO_0000426222Add
BLAST
Chaini2 – 340339Capsid protein VP0 Reviewed prediction
PRO_0000426223Add
BLAST
Chaini2 – 6968Capsid protein VP4 Reviewed prediction
PRO_0000426224Add
BLAST
Chaini70 – 340271Capsid protein VP2 Reviewed prediction
PRO_0000426225Add
BLAST
Chaini341 – 580240Capsid protein VP3 Reviewed prediction
PRO_0000426226Add
BLAST
Chaini581 – 885305Capsid protein VP1 Reviewed prediction
PRO_0000426227Add
BLAST
Chaini886 – 1461576P2 By similarity
PRO_0000426228Add
BLAST
Chaini886 – 1035150Protease 2A Reviewed prediction
PRO_0000426229Add
BLAST
Chaini1036 – 113297Protein 2B Reviewed prediction
PRO_0000039554Add
BLAST
Chaini1133 – 1461329Protein 2C Reviewed prediction
PRO_0000039555Add
BLAST
Chaini1462 – 2214753P3 By similarity
PRO_0000426230Add
BLAST
Chaini1462 – 1570109Protein 3AB Reviewed prediction
PRO_0000426231Add
BLAST
Chaini1462 – 154887Protein 3A Reviewed prediction
PRO_0000039556Add
BLAST
Chaini1549 – 157022Viral protein genome-linked Reviewed prediction
PRO_0000426232Add
BLAST
Chaini1571 – 2214644Protein 3CD Reviewed prediction
PRO_0000426233Add
BLAST
Chaini1571 – 1752182Protease 3C Reviewed prediction
PRO_0000426234Add
BLAST
Chaini1753 – 2214462RNA-directed RNA polymerase By similarity
PRO_0000426235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By similarity
Modified residuei1551 – 15511O-(5'-phospho-RNA)-tyrosine By 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.
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.
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.
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.
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.

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

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.

Structurei

3D structure databases

ProteinModelPortaliP36290.
SMRiP36290. Positions 2-578, 886-1035, 1462-1520, 1571-2214.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1237 – 1393157SF3 helicase
Add
BLAST
Domaini1571 – 1736166Peptidase C3
Add
BLAST
Domaini1980 – 2095116RdRp catalytic
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni581 – 60121Amphipatic alpha-helix Reviewed prediction
Add
BLAST
Regioni1462 – 148423Disordered By similarity
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProiIPR000605. 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]
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.

P36290-1 [UniParc]FASTAAdd to Basket

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MGAQVSSQKV GAHENTNVAT GGSTVNYTTI NYYKDSASNA ASKLDFSQDP     50
SKFTEPVKDI MLKSAPALNS PNVEACGYSD RVRQITLGNS TITTQEAANA 100
VVAYGEWPSY LDDREANPID APTEPDVSSN RFYTLDSVQW TSTSRGWWWK 150
LPDALKDMGM FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAIPEYV 200
MACNTEAKTS YVSYINANPG EKGGVFSSTY NPSEEASEGR KFAALDYLLG 250
CGVLAGNAFV YPHQIINLRT NNSATLVLPY VNSLAIDCMA KHNNWGLVIL 300
PLCKLDYAPN SSTEIPITVT IAPMFTEFNG LRNITVPATQ GLPTMLTPGS 350
SQFLTSDDFQ SPCALPNFDV TPPIHIPGEV FNMMELAEID SMIPMNSVTG 400
KANTMEMYPI PLDDKGGKTP IFSISLSPAS DKRLQYTMLG EILNYYTHWT 450
GSLRFTFLFC GSMMATGKIL LSYSPPGAKP PTTRKDAMLG THIIWDLGLQ 500
SSCTMLAPWI SNTVYRRCIK DDFTEGGYIT CFYQTRIVVP SGTPTSMFML 550
AFVSACPDFS VRLLRDTNHI SQRTLFARAQ GIEETIDTVI SNALQLSQPK 600
PQKQLTAQST PSTSGVNSQE VPALTAVETG VSGQAIPSDV IETRHVVNYK 650
TRSESTLESF FGRSACVTML EVENFNATTE ADKKKQFTTW AITYTDTVQL 700
RRKLEFFTYS RFDLEMTFVI TERYYTSNTG YARNQVYQLM YIPPGAPRPT 750
AWDDYTWQSS SNPSVFYTYG SAPPRISIPY VGIANAYSHF YDGFARVPLK 800
DETVDSGDTY YGLVTINDFG TLAVRVVNEF NPARIISKIR VYMKPKHVRC 850
WCPRPPRAVP YRGEGVDFKQ DSITPLIAVE NINTFGGFGH QNMAVYVAGY 900
KICNYHLATP EDHDNAVRVL WNRDLMIVSS RAQGSDTIAR CNCRTGVYYC 950
KSMKKYYPVT VTEPTFQYME ANDYYPARYQ THMLLGMGFA EPGDCGGILR 1000
CNHGVMGIVT AGGNGIVAFA DIRDLWVYEE EAMEQGITSY IESLGAAFGS 1050
GFTNQIGEKV SELTSMVTSS ITEKLLKTLI KIISTLVIIS RNYEDTTTVL 1100
ATLALLGCDY SPWQWIKKKA CDVLELPYVM RQGDSWLKKF TEACNAAKGL 1150
EWISNKISKF IDWLKERIIP EAKDKVEFIT KLKQLGILEN QINTIHQSCP 1200
SQEQQEILFN NVRWLAIQSR RFAPLYAVEA KRISKLENTI NNYIQFKSKH 1250
RIEPVCMLIH GSPGTGKSIA TSLIGRAIAE KENTSTYSLP PDPTHFDGYK 1300
QQGVVIMDDL NQNPDGNDMK LFCQMVSTVE FIPPMASLEE KGILFTSDYV 1350
LASTNSHTIT PPTVSHSDAL NRRFAFDMEV YTMSEHSIKG KLNMATATQL 1400
CKDCPQPANF KKCCPLVCGK ALQLMDKNTR QRFTLDEITT LVINERNRRA 1450
NIGNCMEALF QGPIQYRDVM IDIKETPAPD YINDLLQSVD SQELRDYCEK 1500
KGWIARLNND LVMERNLNRA MTILQAVTTF AAVAAVVYVM YKLFAGHQGA 1550
YTGLPNKKPS VPTVRTAKVQ GPGFDYAVAM AKRNILTATT SKGEFTMLGV 1600
HDNVAILPTH AAPGDSIVID GKEVEVLDAE ALEDQSGTNL EITIVKLKRN 1650
EKFRDIRPHI PTQITETNDG VLIVNTSKYP NMYVPVGAVT EQGYLNLGGR 1700
QTARTLMYNF PTRAGQCGGV ITCTGKVIGM HVGGNGSHGF AAALKRSYFT 1750
QSQGEIQWMR PSKEVGYPVI NAPSKTKLEP SVFHHVFEGA KEPAVLTKND 1800
PRLKTDFEEA IFSKYVGNKI TEVDEYMKEA VDHYAGQLMS LDINTEQMCL 1850
EDAMYGTDGL EALDLSTSAG YPYVAMGKKK RDILNKQTRD TKEMQRLLDT 1900
YGINLPLVTY VKDELRSKTK VEQGKSRLIE ASSLNDSVAM RMAFGNLYAA 1950
FHKNPGVVTG SAVGCDPDLF WSKIPVLMEE KLFAFDYTGY DASLSPAWFE 2000
ALKMVLEKIG FGDRVDYIDY LNHSHHLYKN KTYCVKGGMP SGCSGTSIFN 2050
SMINNLIIRT LLLKTYKGID LDHLKMIAYG DDVIASYPHE VDASLLAQSG 2100
KDYGLTMTPA DKSATFETVT WENVTFLKRF FRADEKYPFL VHPVMPMKEI 2150
HESIRWTKDP RNTQDHVRSL CLLAWHNGEE EYNKFLAKVR SVPIGRALLL 2200
PEYSTLYRRW LDSF 2214
Length:2,214
Mass (Da):247,214
Last modified:January 23, 2007 - v3
Checksum:iE0DD74569E1B22B8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90457 Genomic RNA. No translation available.
PIRiA48548.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90457 Genomic RNA. No translation available.
PIRi A48548.

3D structure databases

ProteinModelPortali P36290.
SMRi P36290. Positions 2-578, 886-1035, 1462-1520, 1571-2214.
ModBasei Search...

Protein family/group databases

MEROPSi C03.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProi 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 ]
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 variant of Coxsackievirus A24, an agent causing acute hemorrhagic conjunctivitis."
    Supanaranond K., Takeda N., Yamazaki S.
    Virus Genes 6:149-158(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOLG_CXA24
AccessioniPrimary (citable) accession number: P36290
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 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

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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