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P27407

- POLG_FCVC6

UniProt

P27407 - POLG_FCVC6

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Protein
Genome polyprotein
Gene
ORF1
Organism
Feline calicivirus (strain CFI/68 FIV) (FCV)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

Functioni

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, 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 By similarity.

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei46 – 472Cleavage; by Pro-Pol By similarity
Sitei331 – 3322Cleavage; by Pro-Pol By similarity
Sitei684 – 6852Cleavage; by Pro-Pol By similarity
Sitei959 – 9602Cleavage; by Pro-Pol By similarity
Sitei1070 – 10712Cleavage; by Pro-Pol By similarity
Active sitei1109 – 11091For protease activity By similarity
Active sitei1130 – 11301For protease activity By similarity
Active sitei1192 – 11921For protease activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi484 – 4918ATP Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

  1. RNA-protein covalent cross-linking Source: UniProtKB-KW
  2. suppression by virus of host translation 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

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 CFI/68 FIV) (FCV)
Taxonomic identifieri11979 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageCaliciviridaeVesivirus
Virus hostiFelidae (cat family) [TaxID: 9681]
ProteomesiUP000008667: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17621762Genome polyprotein
PRO_0000341990Add
BLAST
Chaini1 – 4646Protein p5.6 By similarity
PRO_0000036892Add
BLAST
Chaini47 – 331285Protein p32 By similarity
PRO_0000036893Add
BLAST
Chaini332 – 684353NTPase By similarity
PRO_0000036894Add
BLAST
Chaini685 – 959275Protein p30 By similarity
PRO_0000036895Add
BLAST
Chaini960 – 1070111Viral genome-linked protein By similarity
PRO_0000036896Add
BLAST
Chaini1071 – 1762692Protease-polymerase p76 By similarity
PRO_0000036897Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei983 – 9831O-(5'-phospho-RNA)-tyrosine By similarity

Post-translational modificationi

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.

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 By similarity.

Structurei

3D structure databases

ProteinModelPortaliP27407.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini458 – 614157SF3 helicase
Add
BLAST
Domaini1094 – 1198105Peptidase C24
Add
BLAST
Domaini1477 – 1602126RdRp catalytic
Add
BLAST

Domaini

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

Sequence similaritiesi

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. 4 hits.
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.

P27407-1 [UniParc]FASTAAdd to Basket

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MSQTLSFVLK THNVRKDFVR SVKLTLARRR DLQYFYNKLS RSMRAEACPS     50
CASYDVCPNC TSSDIPDDGS STELIPSWEE VTKTSTYSLL LSEDTSDELC 100
PDDLANVAAH IRKAISTQSH PANSDMCKEQ LTSLLVMAEA MLPQRSRASI 150
PLHQQHQAAR LEWREKFFSK PLDFLLERIG VSKDILQITA IWKIILEKAC 200
YCKSYGEQWF TTAKQKLREM RSYESNTLKP LIGAFIDGLR FMTVDNPYPM 250
GFLPKLIGLI KPLNLAMIID NHENTLSGWV ITLTAIMELY NITECTIDLM 300
TSLITAFYDK IGKATKFYSH VKALFTGFRT EDVSNSFWYM AAAILCYLVT 350
GLIPNNGRFL KIKCLLVRAT TLVSGIIATQ KLAAMFATWN SESIVNELSA 400
RTVAISELNN PTTTSDTESV ERLLELAKIL HEEIKVHTLN PIMQSYNLIL 450
RNLMSTLDGV ITCCNKRKAI ARKRQVPVCY ILTGPPGCGK TTAAQALAKK 500
LSDQEPSVIN LDVDHHDTYT GNEVCIIDEF DSSDKVDYAN FVIGMVNSAP 550
MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSKRAGAF YRRVTYHDVA 600
TLVESHKRAR PGTAVPRSCY KKNFSHLSLA KRGAECWCKE YVLDPKGLQH 650
QSTKAPPPTF LNIDSLAQTM KQDFALKNMA FEAEVGCSEH RYGFVCQQSE 700
VETVRRLLNA IRMRLNATFT VCVGLEASNS VGCTAHVLTP DEPFNGKRFV 750
VSRCNEASLS ALEGNCVQTA LGVCMSNKDL THLCHFIKGK IVNDSVRLDE 800
LPANQHVVTV NSVFDLAWAL RRHSTLTGQF QAIRAAYDVL HVPDKVPAML 850
RHWMDETSFS DEHVVTQFIT PGGVVILESC GGARIWALGN NVIRAGGVTA 900
IPTGGCVRLM GLSAQTMPWS EILSELFSLL GKIWSSVKVS TLILTALSMY 950
ASRFRPKTEA KGKTKSKIGP YRGRGVALTD DEYDEWKEHN AARKLDLSVE 1000
DFLMLRHRAA LGADDTDAVK FRSWWNSRSR LADDFEDVTV IGKGGVKHEK 1050
IRTNTLRAVD RGYDVSFAEE SGPGAKFHKN AIGSVTDVCG EHKGYCVHMG 1100
HGVYASVAHV VKGDSFFLGE RIFDLKTNGE FCCFRSTKIL PSAAPFFSGR 1150
PTRDPWGSPV ATDWKPKPYS TTSGKIVGCF ATTSTETHPG DCGLPYIDDN 1200
GRVTGLHTGS GGPKTPSAKL VVPYVHIDMK TKSVTAQKYD VTKPDISYKG 1250
LVCKQLDEIR IIPKGTRLHV SPAHLEDFEE CSHQPASLGS GDPRCPKSLT 1300
AIVVDSLKPY CVVVNGPPHD ILHRVQKMLI DHLSGFVPMN ISSDTSMLSA 1350
FHKLNHDTSC GPYLGGRKKD HMVNGEPDKA LLDLLSSKWK LATQGIALPH 1400
EYTIGLKDEL RPIEKVQEGK RRMIWGCDVG VATVCAAAFK GVSDAITANH 1450
QYGPIQVGIN MDSPSVEALF QRIKSARKVF AVDYSKWDST QSPRVSAASI 1500
DILRYFSDRT PIVDSATNTL KSPPIAVFNG VAVKVSSGLP SGMPLTSVIN 1550
SLNHCLYVGC AILQSLEARN VPVTWNLFST FDMMTYGDDG VYMFPTMYAS 1600
ISDQIFANLS AYGLKPTRVD KSVGSIEPID PNSVVFLKRT ITRTPQGIRG 1650
LLDRSSILRQ FYYIKGENTD NWKEPPKTID PMSRGQQLWN ACLYASQHGI 1700
DFYNKVYKLA EKAVEYEGLH LEPPSYSTAL EHYNSQFNGV EARTDQIDTS 1750
GMAALHCDVF EV 1762
Length:1,762
Mass (Da):195,339
Last modified:May 30, 2000 - v3
Checksum:i61C010202984AF40
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U13992 Genomic RNA. Translation: AAC13992.1.
M32296 Genomic RNA. Translation: AAA42927.1.
PIRiA43488.
T09245.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U13992 Genomic RNA. Translation: AAC13992.1 .
M32296 Genomic RNA. Translation: AAA42927.1 .
PIRi A43488.
T09245.

3D structure databases

ProteinModelPortali P27407.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. 4 hits.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPOLG_FCVC6
AccessioniPrimary (citable) accession number: P27407
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 103 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

Complete 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

Similar proteinsi