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Protein

Genome polyprotein

Gene
N/A
Organism
Coxsackievirus A24 (strain EH24/70)
Status
Reviewed-Annotation score: 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).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.

Cofactori (for Chain RNA-directed RNA polymerase)

Mg2+By similarityNote: Requires the presence of 3CDpro or 3CPro.By similarity

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 sitei906For Protease 2A activityBy similarity1
Active sitei924For Protease 2A activityBy similarity1
Active sitei995For Protease 2A activityBy similarity1
Active sitei1610For Protease 3C activitySequence analysis1
Active sitei1641For Protease 3C activitySequence analysis1
Active sitei1717For Protease 3C activityBy similarity1
Metal bindingi1986MagnesiumBy similarity1
Active sitei2081For RdRp activityBy similarity1
Metal bindingi2082MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1261 – 1268ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

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, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiN08.001.

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 virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007759 Componenti: Genome

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 1525CytoplasmicSequence analysisAdd BLAST1524
Intramembranei1526 – 1541Sequence analysisAdd BLAST16
Topological domaini1542 – 2214CytoplasmicSequence analysisAdd BLAST673

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00004262212 – 2214Genome polyproteinBy similarityAdd BLAST2213
ChainiPRO_00004262222 – 885P1By similarityAdd BLAST884
ChainiPRO_00004262232 – 340Capsid protein VP0Sequence analysisAdd BLAST339
ChainiPRO_00004262242 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042622570 – 340Capsid protein VP2Sequence analysisAdd BLAST271
ChainiPRO_0000426226341 – 580Capsid protein VP3Sequence analysisAdd BLAST240
ChainiPRO_0000426227581 – 885Capsid protein VP1Sequence analysisAdd BLAST305
ChainiPRO_0000426228886 – 1461P2By similarityAdd BLAST576
ChainiPRO_0000426229886 – 1035Protease 2ASequence analysisAdd BLAST150
ChainiPRO_00000395541036 – 1132Protein 2BSequence analysisAdd BLAST97
ChainiPRO_00000395551133 – 1461Protein 2CSequence analysisAdd BLAST329
ChainiPRO_00004262301462 – 2214P3By similarityAdd BLAST753
ChainiPRO_00004262311462 – 1570Protein 3ABSequence analysisAdd BLAST109
ChainiPRO_00000395561462 – 1548Protein 3ASequence analysisAdd BLAST87
ChainiPRO_00004262321549 – 1570Viral protein genome-linkedSequence analysisAdd BLAST22
ChainiPRO_00004262331571 – 2214Protein 3CDSequence analysisAdd BLAST644
ChainiPRO_00004262341571 – 1752Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00004262351753 – 2214RNA-directed RNA polymeraseBy similarityAdd BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei1551O-(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
Sitei340 – 341Cleavage; by Protease 3CSequence analysis2
Sitei885 – 886Cleavage; by Protease 2ASequence analysis2
Sitei1035 – 1036Cleavage; by Protease 3CSequence analysis2
Sitei1132 – 1133Cleavage; by Protease 3CSequence analysis2
Sitei1461 – 1462Cleavage; by Protease 3CSequence analysis2
Sitei1548 – 1549Cleavage; by Protease 3CSequence analysis2
Sitei1570 – 1571Cleavage; by Protease 3CSequence analysis2
Sitei1753 – 1754Cleavage; by Protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Expressioni

Inductioni

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

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

ProteinModelPortaliP36290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1237 – 1393SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1571 – 1736Peptidase C3Add BLAST166
Domaini1980 – 2095RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni581 – 601Amphipatic alpha-helixSequence analysisAdd BLAST21
Regioni1462 – 1484DisorderedBy similarityAdd BLAST23

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

CDDicd00205. rhv_like. 3 hits.
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.
IPR009003. Peptidase_S1_PA.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[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

« Hide

        10         20         30         40         50
MGAQVSSQKV GAHENTNVAT GGSTVNYTTI NYYKDSASNA ASKLDFSQDP
60 70 80 90 100
SKFTEPVKDI MLKSAPALNS PNVEACGYSD RVRQITLGNS TITTQEAANA
110 120 130 140 150
VVAYGEWPSY LDDREANPID APTEPDVSSN RFYTLDSVQW TSTSRGWWWK
160 170 180 190 200
LPDALKDMGM FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAIPEYV
210 220 230 240 250
MACNTEAKTS YVSYINANPG EKGGVFSSTY NPSEEASEGR KFAALDYLLG
260 270 280 290 300
CGVLAGNAFV YPHQIINLRT NNSATLVLPY VNSLAIDCMA KHNNWGLVIL
310 320 330 340 350
PLCKLDYAPN SSTEIPITVT IAPMFTEFNG LRNITVPATQ GLPTMLTPGS
360 370 380 390 400
SQFLTSDDFQ SPCALPNFDV TPPIHIPGEV FNMMELAEID SMIPMNSVTG
410 420 430 440 450
KANTMEMYPI PLDDKGGKTP IFSISLSPAS DKRLQYTMLG EILNYYTHWT
460 470 480 490 500
GSLRFTFLFC GSMMATGKIL LSYSPPGAKP PTTRKDAMLG THIIWDLGLQ
510 520 530 540 550
SSCTMLAPWI SNTVYRRCIK DDFTEGGYIT CFYQTRIVVP SGTPTSMFML
560 570 580 590 600
AFVSACPDFS VRLLRDTNHI SQRTLFARAQ GIEETIDTVI SNALQLSQPK
610 620 630 640 650
PQKQLTAQST PSTSGVNSQE VPALTAVETG VSGQAIPSDV IETRHVVNYK
660 670 680 690 700
TRSESTLESF FGRSACVTML EVENFNATTE ADKKKQFTTW AITYTDTVQL
710 720 730 740 750
RRKLEFFTYS RFDLEMTFVI TERYYTSNTG YARNQVYQLM YIPPGAPRPT
760 770 780 790 800
AWDDYTWQSS SNPSVFYTYG SAPPRISIPY VGIANAYSHF YDGFARVPLK
810 820 830 840 850
DETVDSGDTY YGLVTINDFG TLAVRVVNEF NPARIISKIR VYMKPKHVRC
860 870 880 890 900
WCPRPPRAVP YRGEGVDFKQ DSITPLIAVE NINTFGGFGH QNMAVYVAGY
910 920 930 940 950
KICNYHLATP EDHDNAVRVL WNRDLMIVSS RAQGSDTIAR CNCRTGVYYC
960 970 980 990 1000
KSMKKYYPVT VTEPTFQYME ANDYYPARYQ THMLLGMGFA EPGDCGGILR
1010 1020 1030 1040 1050
CNHGVMGIVT AGGNGIVAFA DIRDLWVYEE EAMEQGITSY IESLGAAFGS
1060 1070 1080 1090 1100
GFTNQIGEKV SELTSMVTSS ITEKLLKTLI KIISTLVIIS RNYEDTTTVL
1110 1120 1130 1140 1150
ATLALLGCDY SPWQWIKKKA CDVLELPYVM RQGDSWLKKF TEACNAAKGL
1160 1170 1180 1190 1200
EWISNKISKF IDWLKERIIP EAKDKVEFIT KLKQLGILEN QINTIHQSCP
1210 1220 1230 1240 1250
SQEQQEILFN NVRWLAIQSR RFAPLYAVEA KRISKLENTI NNYIQFKSKH
1260 1270 1280 1290 1300
RIEPVCMLIH GSPGTGKSIA TSLIGRAIAE KENTSTYSLP PDPTHFDGYK
1310 1320 1330 1340 1350
QQGVVIMDDL NQNPDGNDMK LFCQMVSTVE FIPPMASLEE KGILFTSDYV
1360 1370 1380 1390 1400
LASTNSHTIT PPTVSHSDAL NRRFAFDMEV YTMSEHSIKG KLNMATATQL
1410 1420 1430 1440 1450
CKDCPQPANF KKCCPLVCGK ALQLMDKNTR QRFTLDEITT LVINERNRRA
1460 1470 1480 1490 1500
NIGNCMEALF QGPIQYRDVM IDIKETPAPD YINDLLQSVD SQELRDYCEK
1510 1520 1530 1540 1550
KGWIARLNND LVMERNLNRA MTILQAVTTF AAVAAVVYVM YKLFAGHQGA
1560 1570 1580 1590 1600
YTGLPNKKPS VPTVRTAKVQ GPGFDYAVAM AKRNILTATT SKGEFTMLGV
1610 1620 1630 1640 1650
HDNVAILPTH AAPGDSIVID GKEVEVLDAE ALEDQSGTNL EITIVKLKRN
1660 1670 1680 1690 1700
EKFRDIRPHI PTQITETNDG VLIVNTSKYP NMYVPVGAVT EQGYLNLGGR
1710 1720 1730 1740 1750
QTARTLMYNF PTRAGQCGGV ITCTGKVIGM HVGGNGSHGF AAALKRSYFT
1760 1770 1780 1790 1800
QSQGEIQWMR PSKEVGYPVI NAPSKTKLEP SVFHHVFEGA KEPAVLTKND
1810 1820 1830 1840 1850
PRLKTDFEEA IFSKYVGNKI TEVDEYMKEA VDHYAGQLMS LDINTEQMCL
1860 1870 1880 1890 1900
EDAMYGTDGL EALDLSTSAG YPYVAMGKKK RDILNKQTRD TKEMQRLLDT
1910 1920 1930 1940 1950
YGINLPLVTY VKDELRSKTK VEQGKSRLIE ASSLNDSVAM RMAFGNLYAA
1960 1970 1980 1990 2000
FHKNPGVVTG SAVGCDPDLF WSKIPVLMEE KLFAFDYTGY DASLSPAWFE
2010 2020 2030 2040 2050
ALKMVLEKIG FGDRVDYIDY LNHSHHLYKN KTYCVKGGMP SGCSGTSIFN
2060 2070 2080 2090 2100
SMINNLIIRT LLLKTYKGID LDHLKMIAYG DDVIASYPHE VDASLLAQSG
2110 2120 2130 2140 2150
KDYGLTMTPA DKSATFETVT WENVTFLKRF FRADEKYPFL VHPVMPMKEI
2160 2170 2180 2190 2200
HESIRWTKDP RNTQDHVRSL CLLAWHNGEE EYNKFLAKVR SVPIGRALLL
2210
PEYSTLYRRW LDSF
Length:2,214
Mass (Da):247,214
Last modified:January 23, 2007 - v3
Checksum:iE0DD74569E1B22B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90457 Genomic RNA. No translation available.
PIRiA48548.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90457 Genomic RNA. No translation available.
PIRiA48548.

3D structure databases

ProteinModelPortaliP36290.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiN08.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
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.
IPR009003. Peptidase_S1_PA.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.