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P12916

- POLG_HRV1B

UniProt

P12916 - POLG_HRV1B

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Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 1B (HRV-1B)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks By similarity.
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 mmbers 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
Sitei332 – 3332Cleavage; by Protease 3C Reviewed prediction
Active sitei875 – 8751For Protease 2A activity By similarity
Active sitei892 – 8921For Protease 2A activity By similarity
Active sitei963 – 9631For Protease 2A activity By similarity
Sitei999 – 10002Cleavage; by Protease 3C Reviewed prediction
Sitei1416 – 14172Cleavage; by Protease 3C Reviewed prediction
Sitei1493 – 14942Cleavage; by Protease 3C Reviewed prediction
Sitei1514 – 15152Cleavage; by Protease 3C Reviewed prediction
Active sitei1554 – 15541For Protease 3C activity Reviewed prediction
Active sitei1585 – 15851For Protease 3C activity Reviewed prediction
Active sitei1661 – 16611For Protease 3C activity By similarity
Sitei1697 – 16982Cleavage; by Protease 3C Reviewed prediction
Active sitei2024 – 20241For RdRp activity By similarity

GO - Molecular functioni

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

GO - Biological processi

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

MEROPSiC03.007.

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
OrganismiHuman rhinovirus 1B (HRV-1B)
Taxonomic identifieri12129 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusRhinovirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007681: 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 – 14701469Cytoplasmic Reviewed predictionAdd
BLAST
Intramembranei1471 – 148616 Reviewed predictionAdd
BLAST
Topological domaini1487 – 2157671Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host By similarity
Chaini2 – 21572156Genome polyprotein By similarityPRO_0000426491Add
BLAST
Chaini2 – 847846P1 By similarityPRO_0000426492Add
BLAST
Chaini2 – 332331Capsid protein VP0 Reviewed predictionPRO_0000426493Add
BLAST
Chaini2 – 6968Capsid protein VP4 Reviewed predictionPRO_0000426494Add
BLAST
Chaini70 – 332263Capsid protein VP2 Reviewed predictionPRO_0000426495Add
BLAST
Chaini333 – 567235Capsid protein VP3 Reviewed predictionPRO_0000426496Add
BLAST
Chaini567 – 847281Capsid protein VP1 Reviewed predictionPRO_0000426497Add
BLAST
Chaini847 – 1416570P2 By similarityPRO_0000426498Add
BLAST
Chaini847 – 999153Protease 2A Reviewed predictionPRO_0000426499Add
BLAST
Chaini1000 – 109495Protein 2B Reviewed predictionPRO_0000040004Add
BLAST
Chaini1095 – 1416322Protein 2C Reviewed predictionPRO_0000040005Add
BLAST
Chaini1417 – 2157741P3 By similarityPRO_0000426500Add
BLAST
Chaini1417 – 151498Protein 3AB Reviewed predictionPRO_0000426501Add
BLAST
Chaini1417 – 149377Protein 3A Reviewed predictionPRO_0000040006Add
BLAST
Chaini1494 – 151421Viral protein genome-linked Reviewed predictionPRO_0000426502Add
BLAST
Chaini1515 – 2157643Protein 3CD Reviewed predictionPRO_0000426503Add
BLAST
Chaini1515 – 1696182Protease 3C Reviewed predictionPRO_0000426504Add
BLAST
Chaini1697 – 2157461RNA-directed RNA polymerase By similarityPRO_0000426505Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By similarity
Modified residuei1496 – 14961O-(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

Secondary structure

1
2157
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1699 – 17057
Helixi1706 – 17094
Turni1726 – 17305
Helixi1751 – 17566
Helixi1769 – 178315
Helixi1794 – 17996
Beta strandi1802 – 18043
Beta strandi1809 – 18113
Helixi1817 – 18204
Helixi1824 – 18274
Turni1830 – 18334
Helixi1836 – 184510
Beta strandi1851 – 18555
Helixi1862 – 18665
Beta strandi1872 – 18754
Helixi1878 – 189720
Turni1901 – 19044
Helixi1911 – 192111
Beta strandi1924 – 19296
Beta strandi1931 – 19344
Helixi1936 – 19383
Helixi1941 – 195313
Helixi1959 – 19613
Helixi1962 – 19654
Beta strandi1966 – 19716
Beta strandi1974 – 19818
Helixi1989 – 200820
Helixi2014 – 20163
Beta strandi2018 – 20225
Beta strandi2025 – 20328
Helixi2036 – 20416
Helixi2042 – 20465
Turni2064 – 20663
Beta strandi2072 – 20765
Beta strandi2078 – 20803
Beta strandi2083 – 20875
Helixi2090 – 20978
Beta strandi2099 – 21013
Helixi2103 – 21053
Helixi2106 – 211712
Helixi2118 – 21203
Helixi2122 – 213211
Helixi2136 – 21405
Helixi2146 – 21549

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XR6X-ray2.50A1698-2157[»]
ProteinModelPortaliP12916.
SMRiP12916. Positions 2-69, 80-570, 575-856, 858-996, 1515-1694, 1698-2157.

Miscellaneous databases

EvolutionaryTraceiP12916.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1188 – 1350163SF3 helicaseAdd
BLAST
Domaini1515 – 1680166Peptidase C3Add
BLAST
Domaini1925 – 2038114RdRp catalyticAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni567 – 58418Amphipatic alpha-helix Reviewed predictionAdd
BLAST
Regioni1417 – 143115Disordered By similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
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.
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]
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.

P12916-1 [UniParc]FASTAAdd to Basket

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MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP     50
SKFTDPVKDV LEKGIPTLQS PSVEACGYSD RIIQITRGDS TITSQDVANA 100
VVGYGVWPHY LTPQDATAID KPTQPDTSSN RFYTLESKHW NGDSKGWWWK 150
LPDALKEMGI FGENMYYHFL GRSGYTVHVQ CNASKFHQGT LLVAMIPEHQ 200
LASAKNGSVT AGYNLTHPGE AGRVVGQQRD ANLRQPSDDS WLNFDGTLLG 250
NLLIFPHQFI NLRSNNSATL IVPYVNAVPM DSMLRHNNWS LVIIPISPLR 300
SETTSSNIRP ITVSISPMCA EFSGARAKNV RQGLPVYITP GSGQFMTTDD 350
MQSPCALPWY HPTKEISIPG EVKNLIEMCQ VDTLIPVNNV GTNVGNISMY 400
TVQLGNQMDM AQEVFAIKVD ITSQPLATTL IGEIASYYTH WTGSLRFSFM 450
FCGTANTTLK LLLAYTPPGI DKPATRKDAM LGTHVVWDVG LQSTISLVVP 500
WVSASHFRLT ANDKYSMAGY ITCWYQTNLV VPPNTPQTAD MLCFVSACKD 550
FCLRMARDTD LHIQSGPIEQ NPVENYIDEV LNEVLVVPNI KESHHTTSNS 600
APLLDAAETG HTSNVQPEDA IETRYVMTSQ TRDEMSIESF LGRSGCVHIS 650
RIKVDYNDYN GVNKNFTTWK ITLQEMAQIR RKFELFTYVR FDSEVTLVPC 700
IAGRGDDIGH VVMQYMYVPP GAPIPKTRND FSWQSGTNMS IFWQHGQPFP 750
RFSLPFLSIA SAYYMFYDGY DGDNSSSKYG SIVTNDMGTI CSRIVTEKQE 800
HPVVITTHIY HKAKHTKAWC PRPPRAVPYT HSRVTNYVPK TGDVTTAIVP 850
RASMKTVGPS DLYVHVGNLI YRNLHLFNSE MHDSILVSYS SDLIIYRTNT 900
TGDDYIPSCN CTEATYYCKH KNRYYPIKVT PHDWYEIQES EYYPKHIQYN 950
LLIGEGPCEP GDCGGKLLCR HGVIGIITAG GEGHVAFTDL RQFQCAEEQG 1000
ITDYIHMLGE AFGNGFVDSV KEQINAINPI NSISKKVIKW LLRIISAMVI 1050
IIRNSSDPQT IIATLTLIGC NGSPWRFLKE KFCKWTQLTY IHKESDSWLK 1100
KFTEMCNAAR GLEWIGNKIS KFIDWMKSML PQAQLKVKYL NEIKKLSLLE 1150
KQIENLRAAD NATQEKIKCE IDTLHDLSCK FLPLYAHEAK RIKVLYNKCS 1200
NIIKQRKRSE PVAVMIHGPP GTGKSITTNF LARMITNESD VYSLPPDPKY 1250
FDGYDNQSVV IMDDIMQNPD GEDMTLFCQM VSSVTFIPPM ADLPDKGKPF 1300
DSRFVLCSTN HSLLAPPTIS SLPAMNRRFF FDLDIVVHDN YKDAQGKLNV 1350
SKAFQPCNVN TKIGNAKCCP FVCGKAVSFK DRSTCSTYTL AQVYNHILEE 1400
DKRRRQVVDV MSAIFQGPIS LDAPPPPAIA DLLQSVRTPE VIKYCQDNKW 1450
IVPAECQIER DLSIANSIIT IIANIISIAG IIFVIYKLFC TLQGPYSGEP 1500
KPKTKMPERR VVAQGPEEEF GRSILKNNTC VITTDNGKFT GLGIYDRTLI 1550
IPTHADPGRE VQVNGIHTKV LDSYDLYNRD GVKLEITVIQ LDRNEKFRDI 1600
RKYIPETEDD YPECNLALSA NQVEPTIIKV GDVVSYGNIL LSGNQTARML 1650
KYNYPTKSGY CGGVLYKIGQ ILGIHVGGNG RDGFSAMLLR SYFTDTQGQI 1700
KISKHANECG LPTIHTPSKT KLQPSVFYDV FPGSKEPAVS RDNDPRLKVN 1750
FKEALFSKYK GNTECSLNQH MEIAIAHYSA QLITLDIDSK PIALEDSVFG 1800
IEGLEALDLN TSAGFPYVTM GIKKRDLINN KTKDISRLKE ALDKYGVDLP 1850
MITFLKDELR KKEKISAGKT RVIEASSIND TILFRTTFGN LFSKFHLNPG 1900
VVTGSAVGCD PETFWSKIPV MLDGDCIMAF DYTNYDGSIH PVWFQALKKV 1950
LENLSFQSNL IDRLCYSKHL FKSTYYEVAG GVPSGCSGTS IFNTMINNII 2000
IRTLVLDAYK NIDLDKLKII AYGDDVIFSY KYTLDMEAIA NEGKKYGLTI 2050
TPADKSTEFK KLDYNNVTFL KRGFKQDEKH TFLIHPTFPV EEIYESIRWT 2100
KKPSQMQEHV LSLCHLMWHN GRKVYEDFSS KIRSVSAGRA LYIPPYDLLK 2150
HEWYEKF 2157
Length:2,157
Mass (Da):242,315
Last modified:January 23, 2007 - v3
Checksum:i42DB649063B677B9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00239 Genomic RNA. Translation: BAA00168.1.
PIRiA28699. GNNY1B.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00239 Genomic RNA. Translation: BAA00168.1 .
PIRi A28699. GNNY1B.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XR6 X-ray 2.50 A 1698-2157 [» ]
ProteinModelPortali P12916.
SMRi P12916. Positions 2-69, 80-570, 575-856, 858-996, 1515-1694, 1698-2157.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.007.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P12916.

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
4.10.80.10. 2 hits.
InterProi IPR003593. 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.
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 ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
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 nucleotide sequence of human rhinovirus 1B: molecular relationships within the rhinovirus genus."
    Hughes P.J., North C., Jellis C.H., Minor P.D., Stanway G.
    J. Gen. Virol. 69:49-58(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy."
    Love R.A., Maegley K.A., Yu X., Ferre R.A., Lingardo L.K., Diehl W., Parge H.E., Dragovich P.S., Fuhrman S.A.
    Structure 12:1533-1544(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1698-2157.
  3. "Productive entry pathways of human rhinoviruses."
    Fuchs R., Blaas D.
    Adv. Virol. 2012:826301-826301(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiPOLG_HRV1B
AccessioniPrimary (citable) accession number: P12916
Secondary accession number(s): Q82106
, Q82107, Q82108, Q82109, Q82110, Q82111, Q82112, Q82113, Q82114, Q82115, Q89704
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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