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Protein

Genome polyprotein

Gene

ORF1

Organism
Feline calicivirus (strain Cat/United States/Urbana/1960) (FCV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.
Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation (By similarity).By similarity2 Publications
Protease-polymerase p76 processes the polyprotein: Pro-Pol is first released by autocleavage, then all other proteins are cleaved. Cleaves host translation initiation factor eIF4G1, eIF4G2 and PABP1 thereby inducing a shutdown of host protein synthesis. This shutdown may not prevent viral mRNA from being translated since viral Vpg replaces the cap. May cleave host polyadenylate-binding protein thereby inhibiting cellular translation. It is also an RNA-directed RNA polymerase which replicates genomic and antigenomic viral RNA by recognizing specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA codes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs.

Catalytic activityi

NTP + H2O = NDP + phosphate.
Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1110For protease activityBy similarity1
Active sitei1131For protease activityBy similarity1
Active sitei1193For protease activity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi484 – 491ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase

Keywords - Biological processi

Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Viral RNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.4.22.66. 8732.

Protein family/group databases

MEROPSiC24.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 6 chains:
Alternative name(s):
p39
Alternative name(s):
VPg
p13
Protease-polymerase p76 (EC:2.7.7.48, EC:3.4.22.66)
Short name:
Pro-Pol
Gene namesi
ORF Names:ORF1
OrganismiFeline calicivirus (strain Cat/United States/Urbana/1960) (FCV)
Taxonomic identifieri292349 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageCaliciviridaeVesivirus
Virus hostiFelis catus (Cat) (Felis silvestris catus) [TaxID: 9685]
Proteomesi
  • UP000001098 Componenti: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi46E → A: Complete loss of proteolytic processing between P5.6 and P32; Complete loss of infectious clone recovery. 1 Publication1
Mutagenesisi331E → A: Complete loss of infectious clone recovery. 1 Publication1
Mutagenesisi683E → A: Complete loss of infectious clone recovery. 1 Publication1
Mutagenesisi685E → A: Complete loss of infectious clone recovery. 1 Publication1
Mutagenesisi960E → A: Complete loss of infectious clone recovery. 1 Publication1
Mutagenesisi1071E → A: Complete loss of infectious clone recovery. 1 Publication1
Mutagenesisi1193C → G: Complete loss of proteolytic processing. 1 Publication1
Mutagenesisi1345E → A: No effect on infectious clone recovery. 1 Publication1
Mutagenesisi1419E → A: No effect on infectious clone recovery. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003416361 – 1763Genome polyproteinAdd BLAST1763
ChainiPRO_00000369071 – 46Protein p5.6Add BLAST46
ChainiPRO_000003690847 – 331Protein p32Add BLAST285
ChainiPRO_0000036909332 – 685NTPaseAdd BLAST354
ChainiPRO_0000036910686 – 960Protein p30Add BLAST275
ChainiPRO_0000036911961 – 1071Viral genome-linked proteinAdd BLAST111
ChainiPRO_00000369121072 – 1763Protease-polymerase p76Add BLAST692

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei984O-(5'-phospho-RNA)-tyrosineBy similarity1

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. Pro-Pol is first autocatalytically cleaved, then processes the whole polyprotein.2 Publications
VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei46 – 47Cleavage; by Pro-Pol2
Sitei331 – 332Cleavage; by Pro-Pol2
Sitei685 – 686Cleavage; by Pro-Pol2
Sitei960 – 961Cleavage; by Pro-Pol2
Sitei1071 – 1072Cleavage; by Pro-Pol2

Keywords - PTMi

Covalent protein-RNA linkage, Phosphoprotein

Interactioni

Subunit structurei

Protein p32: homodimer, interacts with NTPase, protein p30 and Pro-Pol. Viral genome-linked protein interacts with capsid protein and Pro-Pol. Protease-polymerase p76: Homooligomers, interacts with Vpg, protein p32 and may interact with capsid protein.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ66914.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini458 – 614SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1095 – 1199Peptidase C24Add BLAST105
Domaini1478 – 1603RdRp catalyticPROSITE-ProRule annotationAdd BLAST126

Domaini

Protease-polymerase is composed of two domains displaying two different catalytic activity. These activities may act independently.

Sequence similaritiesi

Contains 1 peptidase C24 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR003593. AAA+_ATPase.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR000317. Peptidase_C24.
IPR009003. Peptidase_S1_PA.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
[Graphical view]
PfamiPF03510. Peptidase_C24. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
PRINTSiPR00916. 2CENDOPTASE.
PR00918. CALICVIRUSNS.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 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.

Q66914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQTLSFVLK THSVRKDFVH SVKRTLQRRR DLQYLYNKLS RPIRAEACPS
60 70 80 90 100
CASYDVCPNC TSGSIPDDGS SKGQIPSWED VTKTSTYSLL LSEDTSDELH
110 120 130 140 150
PDDLVNVAAH IRKALSTQSH PANVDMCKEQ LTSLLVMAEA MLPQRSRSTL
160 170 180 190 200
PLHQKYVAAR LEWREKFFSK PLDFLLEKIG TSRDILQITA VWKIIIEKAC
210 220 230 240 250
YCKSYGEHWF EAAKQKLREI KSYEHNTLKP LIGAFIDGLR LMTIDNPNPM
260 270 280 290 300
GFLPKLIGLI KPLNLAMIID NHENTLSGWV ITLTAIMELY NITECTIDVI
310 320 330 340 350
TSIITGFYDK IGKATKFYSQ IKALFTGFRS EDVANSFWYM AAAILCYLIT
360 370 380 390 400
GLIPNNGRLS KIKACLAGAT TLVSGIVATQ KLAAMFATWN SESIVNELSA
410 420 430 440 450
RTVAISELNN PTTTSDTDSV ERLLELAKIL HEEIKIHTLN PIMQSYNPIL
460 470 480 490 500
RNLMSTLDGV ITSCNKRKAI AKKRPVPVCY ILTGPPGCGK TTAALALAKK
510 520 530 540 550
LSDQEPSVIN LDVDHHDTYT GNEVCIVDEF DSSDKVDYAN FVIGMVNSAP
560 570 580 590 600
MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSRRAGAF YRRVTIIDVA
610 620 630 640 650
NPLAESHKRA RPGTSVPRSC YKKNFSHLSL AKRGAECWCK EYVLDPKGLQ
660 670 680 690 700
HQSIKAPPPT FLNIDSLAQT MKQDFTLKNM AFEAENGHSE HRYGFVCQQG
710 720 730 740 750
EVETVRRLLN AVRTRLNATF TVCVGSEASS SIGCTAHVLT PDEPFNGKKY
760 770 780 790 800
VVSRCNEASL SALEGNCVQS ALGVCMSTKD LTHLCHFIRG KIVNDSVRLD
810 820 830 840 850
ELPANQHVVT VNSVFDLAWA LRRHLTLAGQ FQAIRAAYDV LTAPDKVPAM
860 870 880 890 900
LRHWMDETSF SDEHVVTQFV TPGGIVILES CGGARIWALG HNVIRAGGVT
910 920 930 940 950
ATPTGGCIRF MGLSAQTMPW SEIFRELFSL LGRIWSSIKV STLVLTALGM
960 970 980 990 1000
YASRFRPKSE AKGKTKSKVG PYRGRGVALT DDEYDEWREH NATRKLDLSV
1010 1020 1030 1040 1050
EDFLMLRHRA ALGADDADAV KFRSWWNSRS RLADDYEDVT VIGKGGVKHE
1060 1070 1080 1090 1100
KIRTNTLRAV DRGYDVSFAE ESGPGTKFHK NAIGSVTDVC GEHKGYCVHM
1110 1120 1130 1140 1150
GHGVYATVAH VAKGDSFFLG ERIFDLKTNG EFCCFRSTKI LPSAAPFFPG
1160 1170 1180 1190 1200
KPTRDPWGSP VATEWKPKPY TTTSGKIVGC FATTSTETHP GDCGLPYIDD
1210 1220 1230 1240 1250
NGRVTGLHTG SGGPKTPSAK LVVPYVHIDM KTKSVTAQKY DVTKPDISYK
1260 1270 1280 1290 1300
GLICKQLDEI RIIPKGTRLH VSPAHTEDFE ECSHQPASLG SGDPRCPKSL
1310 1320 1330 1340 1350
TAIVVDSLKP YCDKVEGPPH DILHRVQKML IDHLSGFVPV NISSETSMLS
1360 1370 1380 1390 1400
AFHKLNHDTS CGPYLGGRKK DHMTNGEPDK PLLDLLSAKW KLATQGIALP
1410 1420 1430 1440 1450
HEYTIGLKDE LRPVEKVAEG KRRMIWGCDV GVATVCAAAF KGVSDAITAN
1460 1470 1480 1490 1500
HQYGPVQVGI NMDSPSVEAL HQRIKSAAKV YAVDYSKWDS TQSPRVSAAS
1510 1520 1530 1540 1550
IDILRYFSDR SPIVDSAANT LKSPPIAIFN GVAVKVSSGL PSGMPLTSVI
1560 1570 1580 1590 1600
NSLNHCLYVG CAILQSLEAR GVPVTWNLFS TFDMMTYGDD GVYMFPMMFA
1610 1620 1630 1640 1650
SVSDQIFANL SAYGLKPTRV DKSVGSIEPI DPESVVFLKR TITRTPQGIR
1660 1670 1680 1690 1700
GLLDRSSIIR QFYYIKGENS DDWKTPPKSI DPTSRGQQLW NACLYASQHG
1710 1720 1730 1740 1750
VEFYNKIYKL AQKAVEYEEL HLEPPTYHSA LEHYNNQFNG VEARSDQIDS
1760
SGMTALHCDV FEV
Length:1,763
Mass (Da):194,911
Last modified:November 1, 1996 - v1
Checksum:i7F105592DF0BF821
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40021 Genomic RNA. Translation: AAA79323.1.
RefSeqiNP_783196.1. NC_001481.2.

Genome annotation databases

GeneIDi1502252.
KEGGivg:1502252.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40021 Genomic RNA. Translation: AAA79323.1.
RefSeqiNP_783196.1. NC_001481.2.

3D structure databases

ProteinModelPortaliQ66914.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC24.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1502252.
KEGGivg:1502252.

Enzyme and pathway databases

BRENDAi3.4.22.66. 8732.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR003593. AAA+_ATPase.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR000317. Peptidase_C24.
IPR009003. Peptidase_S1_PA.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
[Graphical view]
PfamiPF03510. Peptidase_C24. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
PRINTSiPR00916. 2CENDOPTASE.
PR00918. CALICVIRUSNS.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_FCVUR
AccessioniPrimary (citable) accession number: Q66914
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: November 1, 1996
Last modified: December 9, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference 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.