UniProtKB - Q82122 (POLG_HRV16)
Genome polyprotein
Functioni
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity).
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 VP1 mainly forms the vertices of the capsid (By similarity).
Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells (By similarity).
This attachment induces virion internalization (By similarity).
Tyrosine kinases are probably involved in the entry process (By similarity).
After binding to its receptor, the capsid undergoes conformational changes (By similarity).
Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity).
Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity).
By similarityForms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity).
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 similarityForms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity).
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 similarityLies on the inner surface of the capsid shell (By similarity).
After binding to the host receptor, the capsid undergoes conformational changes (By similarity).
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 (By similarity).
By similarityComponent of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity).
Allows the capsid to remain inactive before the maturation step (By similarity).
By similarityCysteine protease that cleaves viral polyprotein and specific host proteins (By similarity).
It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (By similarity).
Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (By similarity).
Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).
Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity).
By similarityPlays 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 cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.
By similarityInduces 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 similarityLocalizes the viral replication complex to the surface of membranous vesicles (By similarity).
It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity).
This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).
Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity).
By similarityActs 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 (By similarity).
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 (By similarity).
Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity).
During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity).
By similarityInvolved 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. Protein 3CD binds to the 5'UTR of the viral genome.
By similarityMajor viral protease that mediates proteolytic processing of the polyprotein (By similarity).
Cleaves host EIF5B, contributing to host translation shutoff (By similarity).
Cleaves also host PABPC1, contributing to host translation shutoff (By similarity).
Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (PubMed:33093214).
By similarity1 PublicationReplicates 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 similarityCatalytic activityi
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H+ + phosphateBy similarityEC:3.6.1.15By similarity
- EC:2.7.7.48PROSITE-ProRule annotation
- Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.By similarity EC:3.4.22.29
- 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.PROSITE-ProRule annotation EC:3.4.22.28
Cofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 871 | For protease 2A activityBy similarity | 1 | |
Active sitei | 888 | For protease 2A activityBy similarity | 1 | |
Metal bindingi | 905 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 907 | Zinc; structuralBy similarity | 1 | |
Active sitei | 959 | For protease 2A activityBy similarity | 1 | |
Metal bindingi | 965 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 967 | Zinc; via pros nitrogen; structuralBy similarity | 1 | |
Sitei | 1115 | Involved in the interaction with host RTN3By similarity | 1 | |
Metal bindingi | 1353 | ZincBy similarity | 1 | |
Metal bindingi | 1364 | ZincBy similarity | 1 | |
Metal bindingi | 1369 | ZincBy similarity | 1 | |
Active sitei | 1550 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1581 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1657 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 1927 | Magnesium 1; catalytic; for RdRp activityBy similarity | 1 | |
Metal bindingi | 1927 | Magnesium 2; catalytic; for RdRp activityBy similarity | 1 | |
Metal bindingi | 2020 | Magnesium 1; catalytic; for RdRp activityBy similarity | 1 | |
Metal bindingi | 2020 | Magnesium 2; catalytic; for RdRp activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1353 – 1369 | C4-type; degenerateBy similarityAdd BLAST | 17 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cysteine-type endopeptidase activity Source: UniProtKB-EC
- ion channel activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- nucleoside-triphosphatase activity Source: InterPro
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: InterPro
- structural molecule activity Source: InterPro
GO - Biological processi
- DNA replication Source: UniProtKB-KW
- endocytosis involved in viral entry into host cell Source: UniProtKB-KW
- induction by virus of host autophagy Source: UniProtKB
- pore formation by virus in membrane of host cell Source: UniProtKB-KW
- pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
- positive stranded viral RNA replication Source: UniProtKB
- protein complex oligomerization Source: UniProtKB-KW
- RNA-protein covalent cross-linking Source: UniProtKB-KW
- suppression by virus of host gene expression Source: UniProtKB-KW
- suppression by virus of host mRNA export from nucleus Source: UniProtKB
- suppression by virus of host translation initiation factor activity Source: UniProtKB
- suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity Source: UniProtKB
- transcription, DNA-templated Source: InterPro
- viral RNA genome replication Source: InterPro
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Enzyme and pathway databases
BRENDAi | 2.7.7.48, 2703 3.4.22.28, 2703 |
Protein family/group databases
MEROPSi | N08.001 |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved 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 Alternative name(s): Picornain 2A Protein 2A Alternative name(s): Protein 3B Short name: P3B Protein 3CD (EC:3.4.22.28) Alternative name(s): Picornain 3CPROSITE-ProRule annotation Short name: P3CPROSITE-ProRule annotation RNA-directed RNA polymerasePROSITE-ProRule annotation (EC:2.7.7.48PROSITE-ProRule annotation) Short name: RdRp Alternative name(s): 3D polymerase Short name: 3Dpol Protein 3D Short name: 3D |
Organismi | Human rhinovirus 16 (HRV-16) |
Taxonomic identifieri | 31708 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Enterovirus › Rhinovirus A |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
- Virion By similarity
- Host cytoplasm Curated
- Virion By similarity
- Host cytoplasm Curated
- Virion By similarity
- Host cytoplasm Curated
- 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.
- 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.
- 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.
- 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.
- Virion By similarity
- Host cytoplasm By similarity
- Host nucleus By similarity
- Host cytoplasm By similarity
- 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.
- 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.
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 2 – 1466 | CytoplasmicSequence analysisAdd BLAST | 1465 | |
Intramembranei | 1467 – 1482 | Sequence analysisAdd BLAST | 16 | |
Topological domaini | 1483 – 2153 | CytoplasmicSequence analysisAdd BLAST | 671 |
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, T=pseudo3 icosahedral capsid protein, VirionPathology & Biotechi
Chemistry databases
ChEMBLi | CHEMBL5296 |
DrugBanki | DB08715, 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2-METHYL-4-ISOXAZOLYL]-PHENOL DB08713, 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2N-METHYL-2H-TETRAZOL-5-YL]-PHENOL DB08714, 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL DB03017, Lauric acid DB08231, Myristic acid |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostBy similarity | |||
ChainiPRO_0000426551 | 2 – 2153 | Genome polyproteinAdd BLAST | 2152 | |
ChainiPRO_0000426552 | 2 – 853 | P1Add BLAST | 852 | |
ChainiPRO_0000426553 | 2 – 330 | Capsid protein VP0Add BLAST | 329 | |
ChainiPRO_0000426554 | 2 – 69 | Capsid protein VP4Add BLAST | 68 | |
ChainiPRO_0000426555 | 70 – 330 | Capsid protein VP2Add BLAST | 261 | |
ChainiPRO_0000426556 | 331 – 562 | Capsid protein VP3Add BLAST | 232 | |
ChainiPRO_0000426557 | 563 – 853 | Capsid protein VP1Add BLAST | 291 | |
ChainiPRO_0000426558 | 854 – 1412 | P2Add BLAST | 559 | |
ChainiPRO_0000426559 | 854 – 995 | Protease 2AAdd BLAST | 142 | |
ChainiPRO_0000040041 | 996 – 1090 | Protein 2BAdd BLAST | 95 | |
ChainiPRO_0000040042 | 1091 – 1412 | Protein 2CAdd BLAST | 322 | |
ChainiPRO_0000426560 | 1413 – 2153 | P3Add BLAST | 741 | |
ChainiPRO_0000426561 | 1413 – 1510 | Protein 3ABAdd BLAST | 98 | |
ChainiPRO_0000040043 | 1413 – 1489 | Protein 3AAdd BLAST | 77 | |
ChainiPRO_0000426562 | 1490 – 1510 | Viral protein genome-linkedAdd BLAST | 21 | |
ChainiPRO_0000426563 | 1511 – 2153 | Protein 3CDAdd BLAST | 643 | |
ChainiPRO_0000426564 | 1511 – 1693 | Protease 3CAdd BLAST | 183 | |
ChainiPRO_0000426565 | 1694 – 2153 | RNA-directed RNA polymeraseAdd BLAST | 460 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine; by hostBy similarity | 1 | |
Modified residuei | 1492 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 69 – 70 | Cleavage; by autolysisBy similarity | 2 | |
Sitei | 330 – 331 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 853 – 854 | Cleavage; by autolysisBy similarity | 2 | |
Sitei | 995 – 996 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1090 – 1091 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1412 – 1413 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1489 – 1490 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1510 – 1511 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1693 – 1694 | Cleavage; by protease 3CBy similarity | 2 |
Keywords - PTMi
Autocatalytic cleavage, Covalent protein-RNA linkage, Lipoprotein, Myristate, PhosphoproteinProteomic databases
PRIDEi | Q82122 |
Interactioni
Subunit structurei
Interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers.
By similarityInteracts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity).
Interacts with capsid protein VP2, capsid protein VP3 and capsid protein VP4 following cleavage of capsid protein VP0 (By similarity).
By similarityInteracts with capsid protein VP1 and capsid protein VP3 in the mature capsid.
By similarityInteracts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity).
Interacts with capsid protein VP4 in the mature capsid (By similarity).
Interacts with protein 2C; this interaction may be important for virion morphogenesis (By similarity).
By similarityHomohexamer; forms a hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases (By similarity).
Interacts (via N-terminus) with host RTN3 (via reticulon domain); this interaction is important for viral replication (By similarity).
Interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity).
By similarityHomodimer (By similarity).
Interacts with host GBF1 (By similarity).
Interacts (via GOLD domain) with host ACBD3 (via GOLD domain); this interaction allows the formation of a viral protein 3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate the recruitment of host PI4KB in order to synthesize PI4P at the viral RNA replication sites (By similarity).
By similarityInteracts with Viral protein genome-linked and with protein 3CD.
By similarityChemistry databases
BindingDBi | Q82122 |
Structurei
Secondary structure
3D structure databases
SMRi | Q82122 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q82122 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1186 – 1346 | SF3 helicasePROSITE-ProRule annotationAdd BLAST | 161 | |
Domaini | 1511 – 1689 | Peptidase C3PROSITE-ProRule annotationAdd BLAST | 179 | |
Domaini | 1921 – 2034 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 114 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 565 – 582 | Amphipathic alpha-helixSequence analysisAdd BLAST | 18 | |
Regioni | 1091 – 1224 | OligomerizationBy similarityAdd BLAST | 134 | |
Regioni | 1091 – 1160 | Membrane-bindingBy similarityAdd BLAST | 70 | |
Regioni | 1112 – 1116 | RNA-bindingBy similarity | 5 | |
Regioni | 1396 – 1403 | RNA-bindingBy similarity | 8 | |
Regioni | 1407 – 1412 | OligomerizationBy similarity | 6 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1353 – 1369 | C4-type; degenerateBy similarityAdd BLAST | 17 |
Keywords - Domaini
Repeat, Zinc-fingerFamily and domain databases
CDDi | cd00205, rhv_like, 3 hits |
Gene3Di | 2.40.10.10, 4 hits 2.60.120.20, 3 hits 3.30.70.270, 1 hit 3.40.50.300, 1 hit 6.10.20.20, 1 hit |
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR000605, Helicase_SF3_ssDNA/RNA_vir IPR014759, Helicase_SF3_ssRNA_vir IPR027417, P-loop_NTPase IPR014838, P3A IPR036203, P3A_soluble_dom IPR044067, PCV_3C_PRO IPR000081, Peptidase_C3 IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR003138, Pico_P1A IPR002527, Pico_P2B IPR001676, Picornavirus_capsid IPR043128, Rev_trsase/Diguanyl_cyclase IPR033703, Rhv-like IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR029053, Viral_coat |
Pfami | View protein in Pfam 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 |
SUPFAMi | SSF50494, SSF50494, 2 hits SSF52540, SSF52540, 1 hit SSF56672, SSF56672, 1 hit SSF89043, SSF89043, 1 hit |
PROSITEi | View protein in PROSITE PS51874, PCV_3C_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit PS51218, SF3_HELICASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MGAQVSRQNV GTHSTQNMVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP
60 70 80 90 100
SKFTDPVKDV LEKGIPTLQS PSVEACGYSD RIIQITRGDS TITSQDVANA
110 120 130 140 150
VVGYGVWPHY LTPQDATAID KPTQPDTSSN RFYTLDSKMW NSTSKGWWWK
160 170 180 190 200
LPDALKDMGI FGENMFYHFL GRSGYTVHVQ CNASKFHQGT LLVVMIPEHQ
210 220 230 240 250
LATVNKGNVN AGYKYTHPGE AGREVGTQVE NEKQPSDDNW LNFDGTLLGN
260 270 280 290 300
LLIFPHQFIN LRSNNSATLI VPYVNAVPMD SMVRHNNWSL VIIPVCQLQS
310 320 330 340 350
NNISNIVPIT VSISPMCAEF SGARAKTVVQ GLPVYVTPGS GQFMTTDDMQ
360 370 380 390 400
SPCALPWYHP TKEIFIPGEV KNLIEMCQVD TLIPINSTQS NIGNVSMYTV
410 420 430 440 450
TLSPQTKLAE EIFAIKVDIA SHPLATTLIG EIASYFTHWT GSLRFSFMFC
460 470 480 490 500
GTANTTLKVL LAYTPPGIGK PRSRKEAMLG THVVWDVGLQ STVSLVVPWI
510 520 530 540 550
SASQYRFTTP DTYSSAGYIT CWYQTNFVVP PNTPNTAEML CFVSGCKDFC
560 570 580 590 600
LRMARDTDLH KQTGPITQNP VERYVDEVLN EVLVVPNINQ SHPTTSNAAP
610 620 630 640 650
VLDAAETGHT NKIQPEDTIE TRYVQSSQTL DEMSVESFLG RSGCIHESVL
660 670 680 690 700
DIVDNYNDQS FTKWNINLQE MAQIRRKFEM FTYARFDSEI TMVPSVAAKD
710 720 730 740 750
GHIGHIVMQY MYVPPGAPIP TTRDDYAWQS GTNASVFWQH GQPFPRFSLP
760 770 780 790 800
FLSIASAYYM FYDGYDGDTY KSRYGTVVTN DMGTLCSRIV TSEQLHKVKV
810 820 830 840 850
VTRIYHKAKH TKAWCPRPPR AVQYSHTHTT NYKLSSEVHN DVAIRPRTNL
860 870 880 890 900
TTVGPSDMYV HVGNLIYRNL HLFNSDIHDS ILVSYSSDLI IYRTSTQGDG
910 920 930 940 950
YIPTCNCTEA TYYCKHKNRY YPINVTPHDW YEIQESEYYP KHIQYNLLIG
960 970 980 990 1000
EGPCEPGDCG GKLLCKHGVI GIITAGGEGH VAFIDLRHFH CAEEQGITDY
1010 1020 1030 1040 1050
IHMLGEAFGS GFVDSVKDQI NSINPINNIS SKMVKWMLRI ISAMVIIIRN
1060 1070 1080 1090 1100
SSDPQTIIAT LTLIGCNGSP WRFLKEKFCK WTQLTYIHKE SDSWLKKFTE
1110 1120 1130 1140 1150
MCNAARGLEW IGNKISKFID WMKSMLPQAQ LKVKYLSELK KLNFLEKQVE
1160 1170 1180 1190 1200
NLRAADTNTQ EKIKCEIDTL HDLSCKFLPL YASEAKRIKV LYHKCTNIIK
1210 1220 1230 1240 1250
QKKRSEPVAV MIHGPPGTGK SITTSFLARM ITNESDIYSL PPDPKYFDGY
1260 1270 1280 1290 1300
DNQSVVIMDD IMQNPGGEDM TLFCQMVSSV TFIPPMADLP DKGKPFDSRF
1310 1320 1330 1340 1350
VLCSTNHSLL APPTISSLPA MNRRFYLDLD ILVHDNYKDN QGKLDVSRAF
1360 1370 1380 1390 1400
RLCDVDSKIG NAKCCPFVCG KAVTFKDRNT CRTYSLSQIY NQILEEDKRR
1410 1420 1430 1440 1450
RQVVDVMSAI FQGPISMDKP PPPAITDLLR SVRTPEVIKY CQDNKWIVPA
1460 1470 1480 1490 1500
DCQIERDLNI ANSIITIIAN IISIAGIIYI IYKLFCSLQG PYSGEPKPKT
1510 1520 1530 1540 1550
KVPERRVVAQ GPEEEFGMSI IKNNTCVVTT TNGKFTGLGI YDRILILPTH
1560 1570 1580 1590 1600
ADPGSEIQVN GIHTKVLDSY DLFNKEGVKL EITVLKLDRN EKFRDIRKYI
1610 1620 1630 1640 1650
PESEDDYPEC NLALVANQTE PTIIKVGDVV SYGNILLSGT QTARMLKYNY
1660 1670 1680 1690 1700
PTKSGYCGGV LYKIGQILGI HVGGNGRDGF SSMLLRSYFT EQQGQIQISK
1710 1720 1730 1740 1750
HVKDVGLPSI HTPTKTKLQP SVFYDIFPGS KEPAVLTEKD PRLKVDFDSA
1760 1770 1780 1790 1800
LFSKYKGNTE CSLNEHIQVA VAHYSAQLAT LDIDPQPIAM EDSVFGMDGL
1810 1820 1830 1840 1850
EALDLNTSAG YPYVTLGIKK KDLINNKTKD ISKLKLALDK YDVDLPMITF
1860 1870 1880 1890 1900
LKDELRKKDK IAAGKTRVIE ASSINDTILF RTVYGNLFSK FHLNPGVVTG
1910 1920 1930 1940 1950
CAVGCDPETF WSKIPLMLDG DCIMAFDYTN YDGSIHPIWF KALGMVLDNL
1960 1970 1980 1990 2000
SFNPTLINRL CNSKHIFKST YYEVEGGVPS GCSGTSIFNS MINNIIIRTL
2010 2020 2030 2040 2050
VLDAYKHIDL DKLKIIAYGD DVIFSYKYKL DMEAIAKEGQ KYGLTITPAD
2060 2070 2080 2090 2100
KSSEFKELDY GNVTFLKRGF RQDDKYKFLI HPTFPVEEIY ESIRWTKKPS
2110 2120 2130 2140 2150
QMQEHVLSLC HLMWHNGPEI YKDFETKIRS VSAGRALYIP PYELLRHEWY
EKF
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 547 – 548 | KD → NH in AAA69862 (PubMed:7732663).Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L24917 Genomic RNA Translation: AAA69862.1 |
Similar proteinsi
Cross-referencesi
Web resourcesi
Virus Particle ExploreR db Icosahedral capsid structure at high resolution |
Virus Particle ExploreR db Icosahedral capsid structure |
Virus Particle ExploreR db Icosahedral capsid structure in complex with antiviral drug VP63843 (pleconaril) |
Virus Particle ExploreR db Icosahedral capsid structure in complex with a two-domain fragment of its cellular receptor ICAM1 |
Virus Particle ExploreR db Icosahedral capsid structure in complex with antiviral compound pleconaril |
Virus Particle ExploreR db Icosahedral capsid structure |
Virus Particle ExploreR db Icosahedral capsid structure in complex with antiviral compound pleconaril |
Virus Particle ExploreR db Icosahedral capsid structure in complex with antiviral compound VP61209 |
Virus Particle ExploreR db Icosahedral capsid structure in complex with antiviral compound WIN68934 |
Virus Particle ExploreR db Icosahedral capsid structure in complex with antiviral compound VP65099 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L24917 Genomic RNA Translation: AAA69862.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AYM | X-ray | 2.15 | 1 | 569-853 | [»] | |
2 | 70-330 | [»] | ||||
3 | 331-568 | [»] | ||||
1AYN | X-ray | 2.90 | 1 | 569-853 | [»] | |
2 | 70-330 | [»] | ||||
3 | 331-568 | [»] | ||||
1C8M | X-ray | 2.80 | 1 | 569-853 | [»] | |
2 | 79-330 | [»] | ||||
3 | 331-568 | [»] | ||||
4 | 2-78 | [»] | ||||
1D3E | electron microscopy | 28.00 | 1 | 570-853 | [»] | |
2 | 79-330 | [»] | ||||
3 | 331-568 | [»] | ||||
4 | 2-69 | [»] | ||||
1NCR | X-ray | 2.70 | A | 569-853 | [»] | |
B | 70-330 | [»] | ||||
C | 331-568 | [»] | ||||
D | 2-69 | [»] | ||||
1ND2 | X-ray | 2.50 | A | 569-853 | [»] | |
B | 70-330 | [»] | ||||
C | 331-568 | [»] | ||||
D | 2-69 | [»] | ||||
1ND3 | X-ray | 2.80 | A | 569-853 | [»] | |
B | 70-330 | [»] | ||||
C | 331-568 | [»] | ||||
D | 2-69 | [»] | ||||
1QJU | X-ray | 2.80 | 1 | 569-853 | [»] | |
2 | 70-330 | [»] | ||||
3 | 331-568 | [»] | ||||
4 | 2-69 | [»] | ||||
1QJX | X-ray | 2.80 | 1 | 569-853 | [»] | |
2 | 70-330 | [»] | ||||
3 | 331-568 | [»] | ||||
4 | 2-69 | [»] | ||||
1QJY | X-ray | 2.80 | 1 | 569-853 | [»] | |
2 | 70-330 | [»] | ||||
3 | 331-568 | [»] | ||||
4 | 2-69 | [»] | ||||
1TP7 | X-ray | 2.40 | A/B/C/D | 1694-2153 | [»] | |
1XR7 | X-ray | 2.30 | A/B | 1694-2153 | [»] | |
4K50 | X-ray | 2.93 | A/E/I/M | 1694-2153 | [»] | |
SMRi | Q82122 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
BindingDBi | Q82122 |
ChEMBLi | CHEMBL5296 |
DrugBanki | DB08715, 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2-METHYL-4-ISOXAZOLYL]-PHENOL DB08713, 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2N-METHYL-2H-TETRAZOL-5-YL]-PHENOL DB08714, 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL DB03017, Lauric acid DB08231, Myristic acid |
Protein family/group databases
MEROPSi | N08.001 |
Proteomic databases
PRIDEi | Q82122 |
Enzyme and pathway databases
BRENDAi | 2.7.7.48, 2703 3.4.22.28, 2703 |
Miscellaneous databases
EvolutionaryTracei | Q82122 |
Family and domain databases
CDDi | cd00205, rhv_like, 3 hits |
Gene3Di | 2.40.10.10, 4 hits 2.60.120.20, 3 hits 3.30.70.270, 1 hit 3.40.50.300, 1 hit 6.10.20.20, 1 hit |
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR000605, Helicase_SF3_ssDNA/RNA_vir IPR014759, Helicase_SF3_ssRNA_vir IPR027417, P-loop_NTPase IPR014838, P3A IPR036203, P3A_soluble_dom IPR044067, PCV_3C_PRO IPR000081, Peptidase_C3 IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR003138, Pico_P1A IPR002527, Pico_P2B IPR001676, Picornavirus_capsid IPR043128, Rev_trsase/Diguanyl_cyclase IPR033703, Rhv-like IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR029053, Viral_coat |
Pfami | View protein in Pfam 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 |
SUPFAMi | SSF50494, SSF50494, 2 hits SSF52540, SSF52540, 1 hit SSF56672, SSF56672, 1 hit SSF89043, SSF89043, 1 hit |
PROSITEi | View protein in PROSITE PS51874, PCV_3C_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit PS51218, SF3_HELICASE_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_HRV16 | |
Accessioni | Q82122Primary (citable) accession number: Q82122 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 187 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families