Protein VP3
     (Virion protein 3)
     (P1C)
Protein VP1
     (Virion protein 1)
     (P1D)
Protein 2A
     (P2A)
     (P52)
Protein 2B
Picornain 3C
     (EC 3.4.22.28)
     (Protease 3C)
     (P3C)
     (Protease P20B)
RNA-directed RNA polymerase 3D-POL
     (P3D-POL)
     (EC 2.7.7.48)
     (P56A)

Gene name

None

From

Foot-and-mouth disease virus (strain C1-Santa Pau) (Aphthovirus C) (FMDV)

[TaxID: 12120]

Taxonomy

Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; Picornaviridae; Aphthovirus.

Virus hosts

Bos taurus (Bovine) [TaxID: 9913]
Capra hircus (Goat) [TaxID: 9925]
Cervidae (deer) [TaxID: 9850]
Erinaceidae (hedgehogs) [TaxID: 9363]
Loxodonta africana (African elephant) [TaxID: 9785]
Ovis aries (Sheep) [TaxID: 9940]
Rattus norvegicus (Rat) [TaxID: 10116]
Sus scrofa (Pig) [TaxID: 9823]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-332. DOI=10.1016/0378-1119(83)90050-1; PubMed=6311686 [NCBI, ExPASy, EBI, Israel, Japan] Villanueva N., Davila M., Ortin J., Domingo E.; "Molecular cloning of cDNA from foot-and-mouth disease virus C1-Santa Pau (C-S8). Sequence of protein-VP1-coding segment."; Gene 23:185-194(1983).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 333-861. DOI=10.1016/0378-1119(85)90157-X; PubMed=2993105 [NCBI, ExPASy, EBI, Israel, Japan] Martinez-Salas E., Ortin J., Domingo E.; "Sequence of the viral replicase gene from foot-and-mouth disease virus C1-Santa Pau (C-S8)."; Gene 35:55-61(1985).
[3]	STRUCTURE BY ELECTRON MICROSCOPY (30.0 ANGSTROMS) OF 178-201. DOI=10.1093/emboj/16.7.1492; PubMed=9130694 [NCBI, ExPASy, EBI, Israel, Japan] Hewat E.A., Verdaguer N., Fita I., Blakemore W., Brookes S., King A., Newman J., Domingo E., Mateu M.G., Stuart D.I.; "Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop."; EMBO J. 16:1492-1500(1997).

Comments

FUNCTION: Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).
FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
SUBCELLULAR LOCATION: Protein VP3: Virion. Cytoplasm (Potential).
SUBCELLULAR LOCATION: Picornain 3C: Cytoplasm (Potential).
SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins (By similarity).
SIMILARITY: Belongs to the picornaviruses polyprotein family.
SIMILARITY: Contains 1 peptidase C3 domain [view classification].
SIMILARITY: Contains 1 RdRp catalytic domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M11027; AAA42654.1; -; Genomic_RNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A03913; A03913.
A24031; A24031.

3D structure databases

PDB

1QGC; EM; 30.00 A; 5=178-201.

[ExPASy / RCSB / EBI]

PDBsum

1QGC; -.

SMR

P03311; 1-46, 47-252, 392-861.

ModBase

P03311.

Ontologies

GO:0031410;	Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0000166;	Molecular function: nucleotide binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006410;	Biological process: transcription, RNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR004080; FMDV_VP1_coat.
IPR000199; Pept_C3_picorn.
IPR001676; Picornavirus_capsid.
IPR001205; RNA_pol_P3D.
IPR007094; RNA_pol_PSvir.
Graphical view of domain structure.

Pfam

PF00548; Peptidase_C3; 1.
PF00680; RdRP_1; 1.
PF00073; Rhv; 1.
Pfam graphical view of domain structure.

PRINTS

PR01542; FMDVP1COAT.

PROSITE

PS50507; RDRP_SSRNA_POS; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Capsid protein; Cytoplasm; Cytoplasmic vesicle; Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase; Protease; RNA replication; RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 46`	`>46`	`Protein VP3.`	`PRO_0000039886`
`CHAIN`	`47 252`	`206`	`Protein VP1 (Potential).`	`PRO_0000039887`
`CHAIN`	`253 270`	`18`	`Protein 2A (Potential).`	`PRO_0000039888`
`CHAIN`	`271 >332`	`>62`	`Protein 2B (Potential).`	`PRO_0000310979`
`CHAIN`	`<333 391`	`>59`	`Picornain 3C (Potential).`	`PRO_0000039889`
`CHAIN`	`392 861`	`470`	`RNA-directed RNA polymerase 3D-POL (Potential).`	`PRO_0000039890`
`DOMAIN`	`625 743`	`119`	`RdRp catalytic.`
`ACT_SITE`	`341 341`		`For picornain 3C activity (Potential).`
`SITE`	`46 47`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`252 253`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`270 271`	`2`	`Cleavage; by ribosomal skip (Potential).`
`SITE`	`391 392`	`2`	`Cleavage; by picornain 3C (Potential).`
`NON_CONS`	`332 333`
`NON_TER`	`1 1`
`STRAND`	`185 187`	`3`
`HELIX`	`190 192`	`3`
`STRAND`	`194 197`	`4`

Sequence information

Length: 861 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 95556 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 507CD16E61C893D1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
AETTCVQGWV CVYQITHGKA EPTRSSSRIX AGKDFELRLP VDARQQTTTT GESADPVTTT 

        70         80         90        100        110        120 
VENYGGETQV QRRHHTDVAF VLDRFVKVTV SDNQHTLDVM QAHKDNIVGA LSRHTYYFSD 

       130        140        150        160        170        180 
LEIAVTHTGK LTWVPNGAPV SALNNTTNPT AYHKGPVTRL ALPYTAPHRV LATAYTGTTT 

       190        200        210        220        230        240 
YTASARGDLA HLTTTHARHL PTSFNFGAVK AETITELLVR MKRAELYCPR PILPIQPTGD 

       250        260        270        280        290        300 
RHKQPLVAPA KQLLNFDLLK LAGDVESNLG PFFFSDVRSN FSKLVETINQ MQEDMSTKHE 

       310        320        330        340        350        360 
PDFNRLVSAF EELASGVKAI RTGLDEAKPY KLKAATKVGY CGGAVLAKDG ADTFIVGTHS 

       370        380        390        400        410        420 
AGGNGVGYCS CVSRSMLLKM KAHIDPEPHH EGLIVDTRDV EERVHVMRKT KLAPTVAHGV 

       430        440        450        460        470        480 
FNPEFGPAAL SNKDPRLNEG VVLDEVIFSR HKGDTKMSAE DKALFRRCAA DYASRLHSVL 

       490        500        510        520        530        540 
GTANAPLSIY EVIKGVDGLD AMEPDTAPSL PWALQGKRRG ALIDFENGTV GPEAEAALKL 

       550        560        570        580        590        600 
MEKREYKFAC QTFLKDEIRP MEKVRAGKTR IVDVLPVEHI LYTRMMIGRF CAQMHSNNGP 

       610        620        630        640        650        660 
QIGSAVGCNP DVDRQRSGTH LAQYRNVWDV DYSAFDANHC SDAMNIMFEE VFRTEFGFHP 

       670        680        690        700        710        720 
NAEWILKTLV NTEYAYENKR ITVEGGMPSG CSATSIVNTI LNNIYVLYAL RRHYEGVELD 

       730        740        750        760        770        780 
TYTMISYGDD IVVASDYDLD FEALKPHFKS LGQTITPADK SDKGFVLGHS ITDVTFLKRH 

       790        800        810        820        830        840 
FHMDYGTGFY KPVMTSKTLE AILSFARRGT IQEKLISVAG LAVHSGPDEY RRFFEPFQGL 

       850        860 
FEIPSYRSLY LRWVNAVCGR A

P03311 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools