Skip Header

Contribute Send feedback
Read comments (?) or add your own

P27407 (POLG_FCVC6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 6 chains:

  1. Protein p5.6
  2. Protein p32
  3. NTPase
    EC=3.6.1.15
    Alternative name(s):
    p39
  4. Protein p30
  5. Viral genome-linked protein
    Alternative name(s):
    VPg
    p13
  6. Protease-polymerase p76
    Short name=Pro-Pol
    EC=2.7.7.48
    EC=3.4.22.66
Gene names
ORF Names:ORF1
OrganismFeline calicivirus (strain CFI/68 FIV) (FCV) [Complete proteome]
Taxonomic identifier11979 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae › Vesivirus ›
Virus hostFelidae (cat family) [TaxID: 9681]

Protein attributes

Sequence length1762 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity By similarity.

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.

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 and eIF4G2 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 a 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 encodes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs By similarity.

Catalytic activity

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).

Subunit structure

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 By similarity.

Domain

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

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins. Pro-Pol is first autocatalytically cleaved, then processes the whole polyprotein By similarity.

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.

Sequence similarities

Contains 1 peptidase C24 domain.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17621762Genome polyprotein
PRO_0000341990
Chain1 – 4646Protein p5.6 By similarity
PRO_0000036892
Chain47 – 331285Protein p32 By similarity
PRO_0000036893
Chain332 – 684353NTPase By similarity
PRO_0000036894
Chain685 – 959275Protein p30 By similarity
PRO_0000036895
Chain960 – 1070111Viral genome-linked protein By similarity
PRO_0000036896
Chain1071 – 1762692Protease-polymerase p76 By similarity
PRO_0000036897

Regions

Domain458 – 614157SF3 helicase
Domain1094 – 1198105Peptidase C24
Domain1477 – 1602126RdRp catalytic
Nucleotide binding484 – 4918ATP Potential

Sites

Active site11091For protease activity By similarity
Active site11301For protease activity By similarity
Active site11921For protease activity By similarity
Site46 – 472Cleavage; by Pro-Pol By similarity
Site331 – 3322Cleavage; by Pro-Pol By similarity
Site684 – 6852Cleavage; by Pro-Pol By similarity
Site959 – 9602Cleavage; by Pro-Pol By similarity
Site1070 – 10712Cleavage; by Pro-Pol By similarity

Amino acid modifications

Modified residue9831O-(5'-phospho-RNA)-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P27407 [UniParc].

Last modified May 30, 2000. Version 3.
Checksum: 61C010202984AF40

FASTA1,762195,339
        10         20         30         40         50         60 
MSQTLSFVLK THNVRKDFVR SVKLTLARRR DLQYFYNKLS RSMRAEACPS CASYDVCPNC 

        70         80         90        100        110        120 
TSSDIPDDGS STELIPSWEE VTKTSTYSLL LSEDTSDELC PDDLANVAAH IRKAISTQSH 

       130        140        150        160        170        180 
PANSDMCKEQ LTSLLVMAEA MLPQRSRASI PLHQQHQAAR LEWREKFFSK PLDFLLERIG 

       190        200        210        220        230        240 
VSKDILQITA IWKIILEKAC YCKSYGEQWF TTAKQKLREM RSYESNTLKP LIGAFIDGLR 

       250        260        270        280        290        300 
FMTVDNPYPM GFLPKLIGLI KPLNLAMIID NHENTLSGWV ITLTAIMELY NITECTIDLM 

       310        320        330        340        350        360 
TSLITAFYDK IGKATKFYSH VKALFTGFRT EDVSNSFWYM AAAILCYLVT GLIPNNGRFL 

       370        380        390        400        410        420 
KIKCLLVRAT TLVSGIIATQ KLAAMFATWN SESIVNELSA RTVAISELNN PTTTSDTESV 

       430        440        450        460        470        480 
ERLLELAKIL HEEIKVHTLN PIMQSYNLIL RNLMSTLDGV ITCCNKRKAI ARKRQVPVCY 

       490        500        510        520        530        540 
ILTGPPGCGK TTAAQALAKK LSDQEPSVIN LDVDHHDTYT GNEVCIIDEF DSSDKVDYAN 

       550        560        570        580        590        600 
FVIGMVNSAP MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSKRAGAF YRRVTYHDVA 

       610        620        630        640        650        660 
TLVESHKRAR PGTAVPRSCY KKNFSHLSLA KRGAECWCKE YVLDPKGLQH QSTKAPPPTF 

       670        680        690        700        710        720 
LNIDSLAQTM KQDFALKNMA FEAEVGCSEH RYGFVCQQSE VETVRRLLNA IRMRLNATFT 

       730        740        750        760        770        780 
VCVGLEASNS VGCTAHVLTP DEPFNGKRFV VSRCNEASLS ALEGNCVQTA LGVCMSNKDL 

       790        800        810        820        830        840 
THLCHFIKGK IVNDSVRLDE LPANQHVVTV NSVFDLAWAL RRHSTLTGQF QAIRAAYDVL 

       850        860        870        880        890        900 
HVPDKVPAML RHWMDETSFS DEHVVTQFIT PGGVVILESC GGARIWALGN NVIRAGGVTA 

       910        920        930        940        950        960 
IPTGGCVRLM GLSAQTMPWS EILSELFSLL GKIWSSVKVS TLILTALSMY ASRFRPKTEA 

       970        980        990       1000       1010       1020 
KGKTKSKIGP YRGRGVALTD DEYDEWKEHN AARKLDLSVE DFLMLRHRAA LGADDTDAVK 

      1030       1040       1050       1060       1070       1080 
FRSWWNSRSR LADDFEDVTV IGKGGVKHEK IRTNTLRAVD RGYDVSFAEE SGPGAKFHKN 

      1090       1100       1110       1120       1130       1140 
AIGSVTDVCG EHKGYCVHMG HGVYASVAHV VKGDSFFLGE RIFDLKTNGE FCCFRSTKIL 

      1150       1160       1170       1180       1190       1200 
PSAAPFFSGR PTRDPWGSPV ATDWKPKPYS TTSGKIVGCF ATTSTETHPG DCGLPYIDDN 

      1210       1220       1230       1240       1250       1260 
GRVTGLHTGS GGPKTPSAKL VVPYVHIDMK TKSVTAQKYD VTKPDISYKG LVCKQLDEIR 

      1270       1280       1290       1300       1310       1320 
IIPKGTRLHV SPAHLEDFEE CSHQPASLGS GDPRCPKSLT AIVVDSLKPY CVVVNGPPHD 

      1330       1340       1350       1360       1370       1380 
ILHRVQKMLI DHLSGFVPMN ISSDTSMLSA FHKLNHDTSC GPYLGGRKKD HMVNGEPDKA 

      1390       1400       1410       1420       1430       1440 
LLDLLSSKWK LATQGIALPH EYTIGLKDEL RPIEKVQEGK RRMIWGCDVG VATVCAAAFK 

      1450       1460       1470       1480       1490       1500 
GVSDAITANH QYGPIQVGIN MDSPSVEALF QRIKSARKVF AVDYSKWDST QSPRVSAASI 

      1510       1520       1530       1540       1550       1560 
DILRYFSDRT PIVDSATNTL KSPPIAVFNG VAVKVSSGLP SGMPLTSVIN SLNHCLYVGC 

      1570       1580       1590       1600       1610       1620 
AILQSLEARN VPVTWNLFST FDMMTYGDDG VYMFPTMYAS ISDQIFANLS AYGLKPTRVD 

      1630       1640       1650       1660       1670       1680 
KSVGSIEPID PNSVVFLKRT ITRTPQGIRG LLDRSSILRQ FYYIKGENTD NWKEPPKTID 

      1690       1700       1710       1720       1730       1740 
PMSRGQQLWN ACLYASQHGI DFYNKVYKLA EKAVEYEGLH LEPPSYSTAL EHYNSQFNGV 

      1750       1760 
EARTDQIDTS GMAALHCDVF EV

« Hide

References

[1]Neill J.D.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Nucleotide sequence of a region of the feline calicivirus genome which encodes picornavirus-like RNA-dependent RNA polymerase, cysteine protease and 2C polypeptides."
Neill J.D.
Virus Res. 17:145-160(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 479-1762.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U13992 Genomic RNA. Translation: AAC13992.1.
M32296 Genomic RNA. Translation: AAA42927.1.
PIRA43488.
T09245.

3D structure databases

ProteinModelPortalP27407.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR003593. AAA+_ATPase.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR000317. Peptidase_C24.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF03510. Peptidase_C24. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
PRINTSPR00916. 2CENDOPTASE.
PR00918. CALICVIRUSNS.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_FCVC6
AccessionPrimary (citable) accession number: P27407
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 30, 2000
Last modified: May 1, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents