Skip Header

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

Genome polyprotein

Gene
N/A
Organism
Coxsackievirus A9 (strain Griggs)
Status
Reviewed-Annotation score: 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 integrin ITGAV/ITGB6 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 sitei888For Protease 2A activityBy similarity1
Active sitei906For Protease 2A activityBy similarity1
Active sitei977For Protease 2A activityBy similarity1
Active sitei1596For Protease 3C activitySequence analysis1
Active sitei1627For Protease 3C activitySequence analysis1
Active sitei1703For Protease 3C activityBy similarity1
Metal bindingi1972MagnesiumBy similarity1
Active sitei2068For RdRp activityBy similarity1
Metal bindingi2069MagnesiumBy similarity1

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 A9 (strain Griggs)
Taxonomic identifieri12068 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000000288 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 – 1511CytoplasmicSequence analysisAdd BLAST1510
Intramembranei1512 – 1527Sequence analysisAdd BLAST16
Topological domaini1528 – 2201CytoplasmicSequence analysisAdd BLAST674

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_00004261642 – 2201Genome polyproteinBy similarityAdd BLAST2200
ChainiPRO_00004261652 – 849P1By similarityAdd BLAST848
ChainiPRO_00004261662 – 330Capsid protein VP0Sequence analysisAdd BLAST329
ChainiPRO_00004261672 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042616870 – 330Capsid protein VP2Sequence analysisAdd BLAST261
ChainiPRO_0000426169331 – 566Capsid protein VP3Sequence analysisAdd BLAST236
ChainiPRO_0000426170566 – 867Capsid protein VP1Sequence analysisAdd BLAST302
ChainiPRO_0000426171868 – 1445P2By similarityAdd BLAST578
ChainiPRO_0000426172868 – 1017Protease 2ASequence analysisAdd BLAST150
ChainiPRO_00000395081018 – 1116Protein 2BSequence analysisAdd BLAST99
ChainiPRO_00000395091117 – 1445Protein 2CSequence analysisAdd BLAST329
ChainiPRO_00004261731446 – 2201P3By similarityAdd BLAST756
ChainiPRO_00004261741446 – 1556Protein 3ABSequence analysisAdd BLAST111
ChainiPRO_00000395101446 – 1534Protein 3ASequence analysisAdd BLAST89
ChainiPRO_00004261751535 – 1556Viral protein genome-linkedSequence analysisAdd BLAST22
ChainiPRO_00004261761557 – 2201Protein 3CDSequence analysisAdd BLAST645
ChainiPRO_00004261771557 – 1738Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00004261781739 – 2201RNA-directed RNA polymeraseBy similarityAdd BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei1537O-(5'-phospho-RNA)-tyrosineBy similarity1

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity).By similarity
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion (By similarity).By similarity
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.By similarity
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion (By similarity).By similarity
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei69 – 70Cleavage; by autolysisSequence analysis2
Sitei330 – 331Cleavage; by Protease 3CSequence analysis2
Sitei867 – 868Cleavage; by Protease 2ASequence analysis2
Sitei1017 – 1018Cleavage; by Protease 3CSequence analysis2
Sitei1445 – 1446Cleavage; by Protease 3CSequence analysis2
Sitei1534 – 1535Cleavage; by Protease 3CSequence analysis2
Sitei1556 – 1557Cleavage; by Protease 3CSequence analysis2
Sitei1739 – 1740Cleavage; 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). Interacts with host integrin ITGAV/ITGB6 heterodimer. 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

12201
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Beta strandi26 – 29Combined sources4
Beta strandi33 – 35Combined sources3
Helixi36 – 38Combined sources3
Helixi51 – 54Combined sources4
Beta strandi57 – 59Combined sources3
Beta strandi63 – 65Combined sources3
Beta strandi83 – 87Combined sources5
Beta strandi90 – 96Combined sources7
Turni113 – 115Combined sources3
Helixi126 – 128Combined sources3
Beta strandi138 – 140Combined sources3
Beta strandi147 – 151Combined sources5
Helixi153 – 155Combined sources3
Helixi159 – 167Combined sources9
Beta strandi168 – 180Combined sources13
Beta strandi188 – 197Combined sources10
Beta strandi203 – 205Combined sources3
Helixi212 – 214Combined sources3
Beta strandi225 – 227Combined sources3
Helixi239 – 241Combined sources3
Turni242 – 245Combined sources4
Helixi248 – 253Combined sources6
Beta strandi254 – 260Combined sources7
Turni261 – 263Combined sources3
Beta strandi265 – 271Combined sources7
Beta strandi276 – 280Combined sources5
Turni282 – 284Combined sources3
Beta strandi288 – 299Combined sources12
Beta strandi308 – 324Combined sources17
Turni338 – 341Combined sources4
Beta strandi353 – 355Combined sources3
Helixi374 – 377Combined sources4
Helixi394 – 398Combined sources5
Beta strandi400 – 404Combined sources5
Beta strandi411 – 416Combined sources6
Turni419 – 421Combined sources3
Turni423 – 427Combined sources5
Helixi429 – 434Combined sources6
Beta strandi437 – 442Combined sources6
Beta strandi444 – 450Combined sources7
Beta strandi459 – 465Combined sources7
Helixi475 – 478Combined sources4
Beta strandi481 – 487Combined sources7
Beta strandi493 – 498Combined sources6
Beta strandi503 – 505Combined sources3
Beta strandi507 – 510Combined sources4
Beta strandi519 – 526Combined sources8
Beta strandi536 – 546Combined sources11
Beta strandi551 – 555Combined sources5
Helixi602 – 604Combined sources3
Helixi612 – 615Combined sources4
Helixi628 – 630Combined sources3
Helixi632 – 636Combined sources5
Beta strandi640 – 650Combined sources11
Helixi654 – 657Combined sources4
Beta strandi658 – 662Combined sources5
Beta strandi665 – 668Combined sources4
Helixi669 – 675Combined sources7
Beta strandi678 – 695Combined sources18
Beta strandi709 – 715Combined sources7
Helixi728 – 731Combined sources4
Beta strandi733 – 735Combined sources3
Beta strandi737 – 741Combined sources5
Beta strandi748 – 751Combined sources4
Beta strandi756 – 762Combined sources7
Beta strandi766 – 769Combined sources4
Turni770 – 772Combined sources3
Beta strandi773 – 777Combined sources5
Helixi778 – 781Combined sources4
Beta strandi786 – 793Combined sources8
Beta strandi800 – 818Combined sources19
Beta strandi843 – 845Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D4MX-ray2.901569-867[»]
270-330[»]
3331-568[»]
42-69[»]
3J2Jelectron microscopy9.54A631-852[»]
B331-568[»]
C79-330[»]
ProteinModelPortaliP21404.
SMRiP21404.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21404.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1221 – 1377SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1557 – 1722Peptidase C3Add BLAST166
Domaini1966 – 2082RdRp catalyticPROSITE-ProRule annotationAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni566 – 582Amphipatic alpha-helixSequence analysisAdd BLAST17
Regioni1446 – 1469DisorderedBy similarityAdd BLAST24

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi858 – 860Cell attachment site3

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 1 peptidase C3 domain.Curated
Contains 2 peptidase C3 domains.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.
InterProiIPR003593. AAA+_ATPase.
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.
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]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
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.

P21404-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAQVSTQKT GAHETSLSAA GNSIIHYTNI NYYKDAASNS ANRQDFTQDP
60 70 80 90 100
SKFTEPVKDV MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV
110 120 130 140 150
VVGYGRWPTY LRDDEATAED QPTQPDVATC RFYTLDSIKW EKGSVGWWWK
160 170 180 190 200
FPEALSDMGL FGQNMQYHYL GRAGYTIHLQ CNASKFHQGC LLVVCVPEAE
210 220 230 240 250
MGGAVVGQAF SATAMANGDK AYEFTSATQS DQTKVQTAIH NAGMGVGVGN
260 270 280 290 300
LTIYPHQWIN LRTNNSATIV MPYINSVPMD NMFRHYNFTL MVIPFVKLDY
310 320 330 340 350
ADTASTYVPI TVTVAPMCAE YNGLRLAQAQ GLPTMNTPGS TQFLTSDDFQ
360 370 380 390 400
SPCALPQFDV TPSMNIPGEV KNLMEIAEVD SVVPVNNVQD TTDQMEMFRI
410 420 430 440 450
PVTINAPLQQ QVFGLRLQPG LDSVFKHTLL GEILNYYAHW SGSMKLTFVF
460 470 480 490 500
CGSAMATGKF LIAYSPPGAN PPKTRKDAML GTHIIWDIGL QSSCVLCVPW
510 520 530 540 550
ISQTHYRLVQ QDEYTSAGYV TCWYQTGMIV PPGTPNSSSI MCFASACNDF
560 570 580 590 600
SVRMLRDTPF ISQDNKLQGD VEEAIERARC TVADTMRTGP SNSASVPALT
610 620 630 640 650
AVETGHTSQV TPSDTMQTRH VKNYHSRSES TVENFLGRSA CVYMEEYKTT
660 670 680 690 700
DKHVNKKFVA WPINTKQMVQ MRRKLEMFTY LRFDMEVTFV ITSRQDPGTT
710 720 730 740 750
LAQDMPVLTR QIMYVPPGGP IPAKVDDYAW QTSTNPSIFW TEGNAPARMS
760 770 780 790 800
IPFISIGNAY SNFYDGWSNF DQRGSYGYNT LNNLGHIYVR HVSGSSPHPI
810 820 830 840 850
TSTIRVYFKP KHTRAWVPRP PRLCQYKKAF SVDFTPTPIT DTRKDINTVT
860 870 880 890 900
TVAQSRRRGD MSTLNTHGAF GQQSGAVYVG NYRVINRHLA THTDWQNCVW
910 920 930 940 950
EDYNRDLLVS TTTAHGCDVI ARCQCTTGVY FCASKNKHYP VSFEGPGLVE
960 970 980 990 1000
VQESEYYPKR YQSHVLLAAG FSEPGDCGGI LRCEHGVIGI VTMGGEGVVG
1010 1020 1030 1040 1050
FADVRDLLWL EDDAMEQGVK DYVEQLGNAF GSGFTNQICE QVNLLKESLV
1060 1070 1080 1090 1100
GQDSILEKSL KALVKIISAL VIVVRNHDDL ITVTAILALI GCTSSPWRWL
1110 1120 1130 1140 1150
KQKVSQYYGI PMAERQNDSW LKKFTEMTNA CKRMEWIAIK IQKFIEWLKV
1160 1170 1180 1190 1200
KILPEVREKH EFLNRLKQLP LLESQIATIE QSAPSQSDQE QLFSNVQYFA
1210 1220 1230 1240 1250
HYCRKYAPLY AAEAKRVFSL EKKMSNYIQF KSKCRIEPVC LLLHGSPGAG
1260 1270 1280 1290 1300
KSVATNLIGR SLAEKLNSSV YSLPPDPDHF DGYKQQAVVI MDDLCQNPDG
1310 1320 1330 1340 1350
KDVSLFCQMV SSVDFVPPMA ALEEKGILFT SPFVLASTNA GSINAPTVSD
1360 1370 1380 1390 1400
SRALARRFHF DMNIEVISMY SQNGKINMPM SVKTCDEECC PVNFKKCCPL
1410 1420 1430 1440 1450
VCGKAIQFID RRTQVRYSLD MLVTEMFREY NHRHSVGATL EALFQGPPIY
1460 1470 1480 1490 1500
REIKISVAPE TPPPPVIADL LKSVDSEDVR EYCKEKGWLI PEVNSTLQIE
1510 1520 1530 1540 1550
KYVSRAFICL QAITTFVSVA GIIYIIYKLF AGFQGAYTGI PNQKPKVPTL
1560 1570 1580 1590 1600
RQAKVQGPAF EFAVAMMKRN SSTVKTEYGE FTMLGIYDRW AVLPRHAKPG
1610 1620 1630 1640 1650
PTILMNDQEV GVMDAKELVD KDGTNLELTL LKLNRNEKFR DIRGFLAKEE
1660 1670 1680 1690 1700
MEVNEAVLAI NTSKFPNMYI PVGQVTDYGF LNLGGTPTKR MLMYNFPTRA
1710 1720 1730 1740 1750
GQCGGVLMST GKVLGIHVGG NGHQGFSAAL LKHYFNDEQG EIEFIESSKD
1760 1770 1780 1790 1800
AGFPIINTPS KTKLEPSVFH QVFEGVKEPA VLRNGDPRLK ANFEEAIFSK
1810 1820 1830 1840 1850
YIGNVNTHVD EYMLEAVDHY AGQLATLDIS TEPMKLEDAV YGTEGLEALD
1860 1870 1880 1890 1900
LTTSAGYPYV ALGIKKRDIL SKKTRDLTKL KECMDKYGLN LPMITYVKDQ
1910 1920 1930 1940 1950
LRSAEKVAKG KSRLIEASSL NDSVAMRQTF GNLYKTFHLN PGIVTGSAVG
1960 1970 1980 1990 2000
CDPDLFWSKI PVMLNGHLIA FDYSGYDASL SPVWFACLKL LLEKLGYSHK
2010 2020 2030 2040 2050
ETNYIDYLCN SHHLYRDKHY FVRGGMPSGC SGTSIFNSMI NNIIIRTLML
2060 2070 2080 2090 2100
KVYKGIDLDQ FRMIAYGDDV IASYPWPIDA SLLAEAGKDY GLIMTPADKG
2110 2120 2130 2140 2150
ECFNEVTWTN VTFLKRYFRA DEQYPFLVHP VMPMKDIHES IRWTKDPKNT
2160 2170 2180 2190 2200
QDHVRSLCLL AWHNGEHEYE EFIRKIRSVP VGRCLTLPAF STLRRKWLDS

F
Length:2,201
Mass (Da):246,535
Last modified:January 23, 2007 - v4
Checksum:iCCEA86F9E80F385F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00627 Genomic RNA. Translation: BAA00518.1.
PIRiJQ0523. GNNYA9.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00627 Genomic RNA. Translation: BAA00518.1.
PIRiJQ0523. GNNYA9.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D4MX-ray2.901569-867[»]
270-330[»]
3331-568[»]
42-69[»]
3J2Jelectron microscopy9.54A631-852[»]
B331-568[»]
C79-330[»]
ProteinModelPortaliP21404.
SMRiP21404.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiN08.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP21404.

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProiIPR003593. AAA+_ATPase.
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.
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]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
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_CXA9
AccessioniPrimary (citable) accession number: P21404
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 157 of the entry and version 4 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

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.