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Q66914

- POLG_FCVUR

UniProt

Q66914 - POLG_FCVUR

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Protein

Genome polyprotein

Gene

ORF1

Organism
Feline calicivirus (strain Cat/United States/Urbana/1960) (FCV)
Status
Reviewed - 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 similarity
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei46 – 472Cleavage; by Pro-Pol
Sitei331 – 3322Cleavage; by Pro-Pol
Sitei685 – 6862Cleavage; by Pro-Pol
Sitei960 – 9612Cleavage; by Pro-Pol
Sitei1071 – 10722Cleavage; by Pro-Pol
Active sitei1110 – 11101For protease activityBy similarity
Active sitei1131 – 11311For protease activityBy similarity
Active sitei1193 – 11931For protease activity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi484 – 4918ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. RNA binding Source: InterPro
  4. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  5. RNA helicase activity Source: InterPro

GO - Biological processi

  1. RNA-protein covalent cross-linking Source: UniProtKB-KW
  2. suppression by virus of host gene expression Source: UniProtKB-KW
  3. transcription, DNA-templated Source: InterPro
  4. viral RNA genome replication Source: InterPro
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 positive-strand viruses, no DNA stageCaliciviridaeVesivirus
Virus hostiFelis catus (Cat) (Felis silvestris catus) [TaxID: 9685]
ProteomesiUP000001098: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461E → A: Complete loss of proteolytic processing between P5.6 and P32; Complete loss of infectious clone recovery. 1 Publication
Mutagenesisi331 – 3311E → A: Complete loss of infectious clone recovery. 1 Publication
Mutagenesisi683 – 6831E → A: Complete loss of infectious clone recovery. 1 Publication
Mutagenesisi685 – 6851E → A: Complete loss of infectious clone recovery. 1 Publication
Mutagenesisi960 – 9601E → A: Complete loss of infectious clone recovery. 1 Publication
Mutagenesisi1071 – 10711E → A: Complete loss of infectious clone recovery. 1 Publication
Mutagenesisi1193 – 11931C → G: Complete loss of proteolytic processing. 1 Publication
Mutagenesisi1345 – 13451E → A: No effect on infectious clone recovery. 1 Publication
Mutagenesisi1419 – 14191E → A: No effect on infectious clone recovery. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17631763Genome polyproteinPRO_0000341636Add
BLAST
Chaini1 – 4646Protein p5.6PRO_0000036907Add
BLAST
Chaini47 – 331285Protein p32PRO_0000036908Add
BLAST
Chaini332 – 685354NTPasePRO_0000036909Add
BLAST
Chaini686 – 960275Protein p30PRO_0000036910Add
BLAST
Chaini961 – 1071111Viral genome-linked proteinPRO_0000036911Add
BLAST
Chaini1072 – 1763692Protease-polymerase p76PRO_0000036912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei984 – 9841O-(5'-phospho-RNA)-tyrosineBy similarity

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

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)LengthDescriptionGraphical viewFeature identifierActions
Domaini458 – 614157SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1095 – 1199105Peptidase C24Add
BLAST
Domaini1478 – 1603126RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

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.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
[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

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        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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40021 Genomic RNA. Translation: AAA79323.1 .
RefSeqi NP_783196.1. NC_001481.2.

3D structure databases

ProteinModelPortali Q66914.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C24.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1502252.

Enzyme and pathway databases

BRENDAi 3.4.22.66. 8732.

Family and domain databases

Gene3Di 3.40.50.300. 4 hits.
InterProi IPR003593. 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.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF03510. Peptidase_C24. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00910. RNA_helicase. 1 hit.
[Graphical view ]
PRINTSi PR00916. 2CENDOPTASE.
PR00918. CALICVIRUSNS.
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "RNA transcripts derived from a cloned full-length copy of the feline calicivirus genome do not require VpG for infectivity."
    Sosnovtsev S.V., Green K.Y.
    Virology 210:383-390(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Processing map and essential cleavage sites of the nonstructural polyprotein encoded by ORF1 of the feline calicivirus genome."
    Sosnovtsev S.V., Garfield M., Green K.Y.
    J. Virol. 76:7060-7072(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 686-695, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF GLU-46; GLU-331; GLU-683; GLU-685; GLU-960; GLU-1071; GLU-1345 AND GLU-1419.
  3. "Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein."
    Sosnovtseva S.A., Sosnovtsev S.V., Green K.Y.
    J. Virol. 73:6626-6633(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 961-969 AND 1072-1080, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF CYS-1193.
  4. "Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions."
    Sosnovtsev S.V., Green K.Y.
    Virology 277:193-203(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 961-980.
  5. "Calicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein."
    Kuyumcu-Martinez M., Belliot G., Sosnovtsev S.V., Chang K.O., Green K.Y., Lloyd R.E.
    J. Virol. 78:8172-8182(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF PROTEASE-POLYMERASE P76.
  6. "Cleavage of eukaryotic initiation factor eIF4G and inhibition of host-cell protein synthesis during feline calicivirus infection."
    Willcocks M.M., Carter M.J., Roberts L.O.
    J. Gen. Virol. 85:1125-1130(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF PROTEASE-POLYMERASE P76.
  7. "Analysis of protein-protein interactions in the feline calicivirus replication complex."
    Kaiser W.J., Chaudhry Y., Sosnovtsev S.V., Goodfellow I.G.
    J. Gen. Virol. 87:363-368(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION IN VIRAL REPLICATION COMPLEX.

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: October 1, 2014
This is version 94 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

External Data

Dasty 3