Q8V736 (POLG_CACV4) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Genome polyprotein

Cleaved into the following 6 chains:

1. Protein p18
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
   Short name=Pro-Pol
   EC=2.7.7.48
   EC=3.4.22.66

Gene names

ORF Names:

ORF1

Organism

Canine calicivirus (strain 48) (CaCV)

Taxonomic identifier

292348 [NCBI]

Taxonomic lineage

Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae › unclassified Caliciviridae › Canine calicivirus

Virus host

Canis familiaris (Dog) (Canis lupus familiaris) [TaxID: 9615]

Protein attributes

Sequence length	1929 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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 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).
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.

Ontologies

Keywords
Biological process	Host-virus interaction Viral RNA replication
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Nucleotidyltransferase Protease RNA-directed RNA polymerase Thiol protease Transferase
PTM	Covalent protein-RNA linkage Phosphoprotein
Gene Ontology (GO)
Biological_process	RNA-protein covalent cross-linking Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral genome replication Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro RNA helicase activity Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1929	1929	Genome polyprotein		PRO_0000341984
	Chain	1 – 176	176	Protein p18		PRO_0000341985
	Chain	177 – 468	292	Protein p32 By similarity		PRO_0000036886
	Chain	469 – 825	357	NTPase By similarity		PRO_0000036887
	Chain	826 – 1112	287	Protein p30 By similarity		PRO_0000036888
	Chain	1113 – 1232	120	Viral genome-linked protein By similarity		PRO_0000036889
	Chain	1233 – 1879	647	Protease-polymerase By similarity		PRO_0000036891
Regions
	Domain	597 – 753	157	SF3 helicase
	Domain	1256 – 1361	106	Peptidase C24
	Domain	1643 – 1768	126	RdRp catalytic
	Nucleotide binding	623 – 630	8	ATP Potential
Sites
	Active site	1271	1	For protease activity By similarity
	Active site	1292	1	For protease activity By similarity
	Active site	1355	1	For protease activity By similarity
	Site	176 – 177	2	Cleavage; by Pro-Pol By similarity
	Site	468 – 469	2	Cleavage; by Pro-Pol By similarity
	Site	825 – 826	2	Cleavage; by Pro-Pol By similarity
	Site	1111 – 1112	2	Cleavage; by Pro-Pol By similarity
	Site	1232 – 1233	2	Cleavage; by Pro-Pol By similarity
Amino acid modifications
	Modified residue	1137	1	O-(5'-phospho-RNA)-tyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8V736 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 9F8A92FC0657A623	FASTA	1,929	214,806
	10 20 30 40 50 60 MASAIALSSS TAQNKITLKS VASRLQQTDD PDIRVWSQSV GFHLQFSNWK CANAFCRFVT 70 80 90 100 110 120 DAYNLTPYKE CARSITRQLT SLSNYLSAQT GVSVSGTQFL LSPSDVEVPV AKTGESVSDI 130 140 150 160 170 180 MVPSYSVNGT SMEFDSMAQL AQALTTGFTF SVNDAQIGNA PAQTGESVSG TGFIAEACPS 190 200 210 220 230 240 CALYDKCPNC TSELINDDGS SQSPGDIPHW THHKIASGIV NILSSDMSSM EDDDFANIAA 250 260 270 280 290 300 HVKKALGTNS HPANNDMSKD QLNWLLNIAE ASLIRKADRT ALPMNAARIA ARRGWREKLF 310 320 330 340 350 360 NEPADKLYTL LRKSKDSFQK SAIWGILFEK ASNAKHYTEI VFQDIVKLIK EECNPSNNFY 370 380 390 400 410 420 FKVMAQSFLD HFRMLVIDNP DPVANLPKFI LKLKPLNLKM IIENHENTAE GWIVTLTAVA 430 440 450 460 470 480 ELYGWLEFAV DLVPKIVSEL YDLLTSATQK CFSMVRELLT NLNILKAESF DFTNPFWYAL 490 500 510 520 530 540 AALLSYFVTG FLPNNAKCSA IKQTLNGATT LVAGITAIQK LAAMFSAWSN ESVVDDLSTK 550 560 570 580 590 600 VIGLTEADNP TVTQDIDAVT NLQIMAEQLK DQIKLKTLDP TFQPYLPVLR NLMSTTDSVI 610 620 630 640 650 660 SHCAKRKALA TQRTAPVCII LTGPAGCGKT TLAYAIANRL SAQKPSVLNL NIDHHDAYTG 670 680 690 700 710 720 NEVCIIDEFD SNPDSKFVEF VVEMVNTNPM LLNCDLIENK GKTFSSKYVI MTSNNETPVK 730 740 750 760 770 780 PNSTRAPPFY RRVRIIDVTN PGVMSFKYEN PGQEVPSYLF SNDFNHLSMS MRGFGAFSKT 790 800 810 820 830 840 RVIDPEGRKT CGLEGPPGQR VDVDDIVRYM QRMYRENQMN FKSEAGNNRL KTPRFAFVTQ 850 860 870 880 890 900 RKHVDTVYKI LAAAKTTYNG YYSLTKDSFD VNEGHNIGSS VFVVGDDKEI PHNCKIFRCN 910 920 930 940 950 960 HLAMFRHPEL AHIEGDNFRA ALGVTMSDQD VTLMFYHIRG KHIQDEVRLD ELPANHHIVT 970 980 990 1000 1010 1020 VHSVYDMAWA LNRHLSLTGK WQALKAVYDL YMTPDILPAA LRHWMDNTKF SSDHVVTQFI 1030 1040 1050 1060 1070 1080 VPGGTIILET CNGARMWATS RRLIRAGGIS NNNGPEGGFR FGSIAPRDIP WSEILREFLN 1090 1100 1110 1120 1130 1140 LISLIWSRVK GATIVLTALL LYMKRYKPRS EAKGKTKGGR GAIRHGGKGI VLSDDEYDEW 1150 1160 1170 1180 1190 1200 REFNMEKRMD MSVDEFLMLK HRAALGSDDT GAIQFRSWWT ARQMRESTGL DHDDVTVIGK 1210 1220 1230 1240 1250 1260 GGVRHEVHRT EIMKAPKQKK KSFAWGEDMY AEGDGKIVNH VNAIVPVTGL CGEHIGYAVH 1270 1280 1290 1300 1310 1320 IGHGKCISLK HVLKTGSYVF NQKPIDVTFD GELAHFQIQQ PPSSAAPVTF SSKPTRDPWG 1330 1340 1350 1360 1370 1380 RSVSTEWKHD TYNTTAGKMY GSICWTATRT QPGDCGLPYV DRAGQVVGLH AGSGGDSAPG 1390 1400 1410 1420 1430 1440 RKIVIPVTKF KLPSNTVLSN RFWKEEAPTI SYKGLTVQET GVNKAVLKGT NYHVSPAHVD 1450 1460 1470 1480 1490 1500 DYQDCTHQPA NLGAQDERYP VSLTSIVINN LEPYKQPTQG PPTEVLNKAY NMLVQHYEPL 1510 1520 1530 1540 1550 1560 IPKATTHLEM GDAFAALNVK TSCGPYITGR KKDHIDPETG KWDETLRNHI NARWSLATQG 1570 1580 1590 1600 1610 1620 VPIPHEYQLG LKDELRPKDK IAVGKRRLIW GCDVGVAVVA ASAFKEVSSA IMAMSEFDFI 1630 1640 1650 1660 1670 1680 QVGINMDGTA VETLYKRLYT PGTHRYCVDY SKWDSTQPPN VTRMSLELLR HFTDKSPVVD 1690 1700 1710 1720 1730 1740 SAVATLSSPS IAVFGGVSFK TNGGLPSGMP LTSILNSLNH CLLVGSAIIQ VLESKGVDVN 1750 1760 1770 1780 1790 1800 WNIYDTIDLF TYGDDGVYIV PNFVHSVMPE VFSCLSSYGL KPTRTDKSSA PITEIPLSEP 1810 1820 1830 1840 1850 1860 IEFLKRQFVR NQFGVRALLD RSSLIRQFYY IKGKNTMEWT KPPEQIDLTS RTAQLQVVML 1870 1880 1890 1900 1910 1920 YASQHGREFY KKCLDYYQLA MEYEGIKLDA PTYDEALAKY NANFNGVEDC DLLPAGYDEH RLDKIVFEN

References

[1]	"Complete nucleotide sequence, genome organization and phylogenic analysis of the canine calicivirus." Matsuura Y., Tohya Y., Nakamura K., Shimojima M., Roerink F., Mochizuki M., Takase K., Akashi H., Sugimura T. Virus Genes 25:67-73(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Organization of the canine calicivirus genome from the RNA polymerase gene to the poly(A) tail." Roerink F., Hashimoto M., Tohya Y., Mochizuki M. J. Gen. Virol. 80:929-935(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1571-1929.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB070225 Genomic RNA. Translation: BAB83601.1. AF053720 Genomic RNA. Translation: AAC16445.1.
RefSeq	NP_777373.1. NC_004542.1.
3D structure databases
ProteinModelPortal	Q8V736.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR003593. 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]
Pfam	PF03510. Peptidase_C24. 1 hit. PF00680. RdRP_1. 1 hit. PF00910. RNA_helicase. 1 hit. [Graphical view]
PRINTS	PR00916. 2CENDOPTASE. PR00918. CALICVIRUSNS.
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50507. RDRP_SSRNA_POS. 1 hit. PS51218. SF3_HELICASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POLG_CACV4

Accession

Primary (citable) accession number: Q8V736
Secondary accession number(s): O72119

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program