CSFVA:POLG

Species (Taxon ID)	Classical swine fever virus (strain Alfort) (CSFV) (Hog choleravirus). (11097)
Gene Name(s)	No Information Provided.
Protein Name(s)	Genome polyprotein N-terminal protease N-pro Autoprotease p20 Capsid protein C Core protein E(rns) glycoprotein gp44/48 Envelope glycoprotein E1 gp33 Envelope glycoprotein E2 gp55 p7 Non-structural protein 2-3 NS2-3 Cysteine protease NS2 Non-structural protein 2 Serine protease NS3 Non-structural protein 3 Non-structural protein 4A NS4A Non-structural protein 4B NS4B Non-structural protein 5A NS5A RNA-directed RNA polymerase NS5B
External Links
UniProt	P19712
EMBL	J04358
PDB	4CBG 4CBH 4CBI 4CBL 4CBM 5MZ4
PDBsum	4CBG 4CBH 4CBI 4CBL 4CBM 5MZ4
ProteinModelPortal	P19712
SMR	P19712
IntAct	P19712
MEROPS	C53.001
PRIDE	P19712
PMAP-CutDB	P19712
Proteomes	UP000008568
GO	GO:0030430 GO:0044165 GO:0042025 GO:0020002 GO:0044228 GO:0016021 GO:0044385 GO:0019013 GO:0055036 GO:0005524 GO:0008026 GO:0004197 GO:0008234 GO:0005216 GO:0004540 GO:0033897 GO:0003723 GO:0003968 GO:0004252 GO:0070008 GO:0039654 GO:0039520 GO:1990214 GO:0032688 GO:0039707 GO:1990219 GO:1901800 GO:0051259 GO:1903608 GO:0006508 GO:0010468 GO:0090501 GO:0039548 GO:0039644 GO:0039547 GO:0039501 GO:0039502 GO:0019082 GO:0039694 GO:0019062
CDD	cd00079
Gene3D	3.90.730.10
InterPro	IPR021824 IPR011492 IPR014001 IPR001650 IPR022120 IPR030399 IPR027417 IPR008751 IPR032521 IPR000280 IPR007094 IPR002166 IPR036430 IPR033130
Pfam	PF11889 PF07652 PF00271 PF05550 PF12387 PF05578 PF16329 PF00998
PRINTS	PR00729
SMART	SM00487 SM00490
SUPFAM	SSF52540 SSF55895
PROSITE	PS51192 PS51194 PS51692 PS51535 PS51876 PS50507 PS00531

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003968	P		Seeded From UniProt
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003968	P		Seeded From UniProt
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003968	P		Seeded From UniProt
involved_in	GO:0034220	ion transmembrane transport	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0005216	P		Seeded From UniProt
involved_in	GO:0090502	RNA phosphodiester bond hydrolysis, endonucleolytic	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0033897	P		Seeded From UniProt
enables	GO:0003723	RNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002166 InterPro:IPR036430	F		Seeded From UniProt
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002166 InterPro:IPR007094 InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
enables	GO:0004175	endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030399	F		Seeded From UniProt
enables	GO:0004197	cysteine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000280 InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011492	F		Seeded From UniProt
enables	GO:0008026	ATP-dependent helicase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011492	F		Seeded From UniProt
involved_in	GO:0016032	viral process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008751	P		Seeded From UniProt
enables	GO:0016817	hydrolase activity, acting on acid anhydrides	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
enables	GO:0017111	nucleoside-triphosphatase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
involved_in	GO:0019082	viral protein processing	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008751	P		Seeded From UniProt
enables	GO:0033897	ribonuclease T2 activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR036430	F		Seeded From UniProt
involved_in	GO:0039694	viral RNA genome replication	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002166 InterPro:IPR007094	P		Seeded From UniProt
enables	GO:0070008	serine-type exopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
enables	GO:0017111	nucleoside-triphosphatase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.6.1.15	F		Seeded From UniProt
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.7.48	F		Seeded From UniProt
involved_in	GO:0006508	proteolysis	PMID:24606708^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
enables	GO:0008234	cysteine-type peptidase activity	PMID:24606708^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt
involved_in	GO:0039548	suppression by virus of host IRF3 activity	PMID:17215286^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
part_of	GO:0030430	host cell cytoplasm	PMID:17215286^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
involved_in	GO:1901800	positive regulation of proteasomal protein catabolic process	PMID:25809915^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q764M6)	Seeded From UniProt
involved_in	GO:1990214	negative regulation by symbiont of host protein levels	PMID:25809915^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q764M6)	Seeded From UniProt
involved_in	GO:0039501	suppression by virus of host type I interferon production	PMID:25809915^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0039548	suppression by virus of host IRF3 activity	PMID:19540847^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q764M6)	Seeded From UniProt
involved_in	GO:0032688	negative regulation of interferon-beta production	PMID:19540847^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:1990214	negative regulation by symbiont of host protein levels	PMID:17215286^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q764M6)	Seeded From UniProt
involved_in	GO:1990219	positive regulation by symbiont of host protein levels	PMID:24965446^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P67809)	Seeded From UniProt
part_of	GO:0030430	host cell cytoplasm	PMID:24965446^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
part_of	GO:0042025	host cell nucleus	PMID:24965446^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
involved_in	GO:1903608	protein localization to cytoplasmic stress granule	PMID:24965446^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:19767841^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:28290554^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
part_of	GO:0019013	viral nucleocapsid	PMID:1870198^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
involved_in	GO:0010468	regulation of gene expression	PMID:9617770^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0090501	RNA phosphodiester bond hydrolysis	PMID:8356450^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
enables	GO:0004540	ribonuclease activity	PMID:8356450^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt
involved_in	GO:0039707	pore formation by virus in membrane of host cell	PMID:24189547^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0039547	suppression by virus of host TRAF activity	PMID:28751780^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0039644	suppression by virus of host NF-kappaB transcription factor activity	PMID:28751780^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
part_of	GO:0044165	host cell endoplasmic reticulum	PMID:26748656^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt
involved_in	GO:0039654	fusion of virus membrane with host endosome membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1170	P		Seeded From UniProt
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt
part_of	GO:0030430	host cell cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1035 UniProtKB-SubCell:SL-0381	C		Seeded From UniProt
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt
enables	GO:0008234	cysteine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0788	F		Seeded From UniProt
involved_in	GO:0051259	protein complex oligomerization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	P		Seeded From UniProt
part_of	GO:0033644	host cell membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1043 UniProtKB-SubCell:SL-0380	C		Seeded From UniProt
involved_in	GO:0039548	suppression by virus of host IRF3 activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1092	P		Seeded From UniProt
enables	GO:0016779	nucleotidyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0548	F		Seeded From UniProt
part_of	GO:0044385	integral to membrane of host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	C		Seeded From UniProt
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt
involved_in	GO:0030683	evasion or tolerance by virus of host immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0899	P		Seeded From UniProt
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0696	F		Seeded From UniProt
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1032 UniProtKB-SubCell:SL-0375	C		Seeded From UniProt
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1160 UniProtKB-KW:KW-1162	P		Seeded From UniProt
involved_in	GO:0039503	suppression by virus of host innate immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1090	P		Seeded From UniProt
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F		Seeded From UniProt
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt
involved_in	GO:0006811	ion transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0406	P		Seeded From UniProt
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt
involved_in	GO:0039707	pore formation by virus in membrane of host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	P		Seeded From UniProt
part_of	GO:0019012	virion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0946 UniProtKB-SubCell:SL-0274	C		Seeded From UniProt
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0720	F		Seeded From UniProt
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt
involved_in	GO:0039663	membrane fusion involved in viral entry into host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1168	P		Seeded From UniProt
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt
involved_in	GO:0019062	virion attachment to host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1161	P		Seeded From UniProt
involved_in	GO:0039520	induction by virus of host autophagy	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1072	P		Seeded From UniProt
enables	GO:0005216	ion channel activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	F		Seeded From UniProt
part_of	GO:0055036	virion membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0275	C		Seeded From UniProt
part_of	GO:0044228	host cell surface	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0378	C		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:26748656^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:F1S912	F	occurs_in:(GO:0005783)	Seeded From UniProt
enables	GO:0005515	protein binding	PMID:24965446^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q08211	F	occurs_in:(GO:0010494)	Seeded From UniProt
enables	GO:0005515	protein binding	PMID:24965446^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P67809	F	occurs_in:(GO:0030430)	Seeded From UniProt
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003968	P		Seeded From UniProt
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003968	P		Seeded From UniProt
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003968	P		Seeded From UniProt
involved_in	GO:0034220	ion transmembrane transport	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0005216	P		Seeded From UniProt
involved_in	GO:0090502	RNA phosphodiester bond hydrolysis, endonucleolytic	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0033897	P		Seeded From UniProt
enables	GO:0003723	RNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002166 InterPro:IPR036430	F		Seeded From UniProt
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002166 InterPro:IPR007094 InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
enables	GO:0004175	endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030399	F		Seeded From UniProt
enables	GO:0004197	cysteine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000280 InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011492	F		Seeded From UniProt
enables	GO:0008026	ATP-dependent helicase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011492	F		Seeded From UniProt
involved_in	GO:0016032	viral process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008751	P		Seeded From UniProt
enables	GO:0016817	hydrolase activity, acting on acid anhydrides	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
enables	GO:0017111	nucleoside-triphosphatase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
involved_in	GO:0019082	viral protein processing	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008751	P		Seeded From UniProt
enables	GO:0033897	ribonuclease T2 activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR036430	F		Seeded From UniProt
involved_in	GO:0039694	viral RNA genome replication	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002166 InterPro:IPR007094	P		Seeded From UniProt
enables	GO:0070008	serine-type exopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR021824 InterPro:IPR022120	F		Seeded From UniProt
enables	GO:0017111	nucleoside-triphosphatase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.6.1.15	F		Seeded From UniProt
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.7.48	F		Seeded From UniProt
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt
involved_in	GO:0039654	fusion of virus membrane with host endosome membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1170	P		Seeded From UniProt
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt
part_of	GO:0030430	host cell cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1035 UniProtKB-SubCell:SL-0381	C		Seeded From UniProt
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt
enables	GO:0008234	cysteine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0788	F		Seeded From UniProt
involved_in	GO:0051259	protein complex oligomerization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	P		Seeded From UniProt
part_of	GO:0033644	host cell membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1043 UniProtKB-SubCell:SL-0380	C		Seeded From UniProt
involved_in	GO:0039548	suppression by virus of host IRF3 activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1092	P		Seeded From UniProt
enables	GO:0016779	nucleotidyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0548	F		Seeded From UniProt
part_of	GO:0044385	integral to membrane of host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	C		Seeded From UniProt
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt
involved_in	GO:0030683	evasion or tolerance by virus of host immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0899	P		Seeded From UniProt
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0696	F		Seeded From UniProt
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1032 UniProtKB-SubCell:SL-0375	C		Seeded From UniProt
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1160 UniProtKB-KW:KW-1162	P		Seeded From UniProt
involved_in	GO:0039503	suppression by virus of host innate immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1090	P		Seeded From UniProt
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F		Seeded From UniProt
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt
involved_in	GO:0006811	ion transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0406	P		Seeded From UniProt
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt
involved_in	GO:0039707	pore formation by virus in membrane of host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	P		Seeded From UniProt
part_of	GO:0019012	virion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0946 UniProtKB-SubCell:SL-0274	C		Seeded From UniProt
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0720	F		Seeded From UniProt
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1162	P		Seeded From UniProt
involved_in	GO:0039663	membrane fusion involved in viral entry into host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1168	P		Seeded From UniProt
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt
involved_in	GO:0019062	virion attachment to host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1161	P		Seeded From UniProt
involved_in	GO:0039520	induction by virus of host autophagy	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1072	P		Seeded From UniProt
enables	GO:0005216	ion channel activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	F		Seeded From UniProt
part_of	GO:0055036	virion membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0275	C		Seeded From UniProt
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0375	C		Seeded From UniProt
part_of	GO:0030430	host cell cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0381	C		Seeded From UniProt
part_of	GO:0033644	host cell membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0380	C		Seeded From UniProt
part_of	GO:0044228	host cell surface	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0378	C		Seeded From UniProt
part_of	GO:0019012	virion	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0274	C		Seeded From UniProt
involved_in	GO:0006508	proteolysis	PMID:24606708^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
enables	GO:0008234	cysteine-type peptidase activity	PMID:24606708^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt
involved_in	GO:0039548	suppression by virus of host IRF3 activity	PMID:17215286^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
part_of	GO:0030430	host cell cytoplasm	PMID:17215286^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:25809915^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q764M6	F		Seeded From UniProt
involved_in	GO:1901800	positive regulation of proteasomal protein catabolic process	PMID:25809915^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q764M6)	Seeded From UniProt
involved_in	GO:1990214	negative regulation by symbiont of host protein levels	PMID:25809915^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q764M6)	Seeded From UniProt
involved_in	GO:0039501	suppression by virus of host type I interferon production	PMID:25809915^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0039548	suppression by virus of host IRF3 activity	PMID:19540847^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q764M6)	Seeded From UniProt
enables	GO:0005515	protein binding	PMID:19540847^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q764M6	F		Seeded From UniProt
involved_in	GO:0032688	negative regulation of interferon-beta production	PMID:19540847^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:17215286^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q764M6	F		Seeded From UniProt
involved_in	GO:1990214	negative regulation by symbiont of host protein levels	PMID:17215286^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q764M6)	Seeded From UniProt
enables	GO:0005515	protein binding	PMID:24965446^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60832,UniProtKB:P05455,UniProtKB:P08579,UniProtKB:P09211,UniProtKB:P11940,UniProtKB:P15880,UniProtKB:P18124,UniProtKB:P18621,UniProtKB:P19338,UniProtKB:P22626,UniProtKB:P26373,UniProtKB:P27635,UniProtKB:P31943,UniProtKB:P36578,UniProtKB:P38159,UniProtKB:P39019,UniProtKB:P39023,UniProtKB:P46782,UniProtKB:P61247,UniProtKB:P61254,UniProtKB:P61313,UniProtKB:P61978,UniProtKB:P62081,UniProtKB:P62244,UniProtKB:P62263,UniProtKB:P62277,UniProtKB:P62424,UniProtKB:P62750,UniProtKB:P62899,UniProtKB:P67809,UniProtKB:P83731,UniProtKB:P83881,UniProtKB:P84098,UniProtKB:Q00839,UniProtKB:Q08211,UniProtKB:Q12906,UniProtKB:Q53HK9,UniProtKB:Q59ES8,UniProtKB:Q59FI9,UniProtKB:Q59GL1,UniProtKB:Q5JR94,UniProtKB:Q8NC51,UniProtKB:Q9BU76,UniProtKB:Q9BVP2,UniProtKB:Q9Y3D9	F		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:24965446^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:B3KNR3,UniProtKB:B5BTY4,UniProtKB:C7DJS2,UniProtKB:F8W7C6,UniProtKB:O43143,UniProtKB:O76094,UniProtKB:P04844,UniProtKB:P05455,UniProtKB:P07910,UniProtKB:P11940,UniProtKB:P12956,UniProtKB:P17844,UniProtKB:P18077,UniProtKB:P22626,UniProtKB:P23396,UniProtKB:P26640,UniProtKB:P28161,UniProtKB:P37108,UniProtKB:P46778,UniProtKB:P46782,UniProtKB:P49458,UniProtKB:P52272,UniProtKB:P54577,UniProtKB:P61011,UniProtKB:P61247,UniProtKB:P62081,UniProtKB:P62266,UniProtKB:P62277,UniProtKB:P62701,UniProtKB:P62851,UniProtKB:P62913,UniProtKB:Q02543,UniProtKB:Q08211,UniProtKB:Q0VAC0,UniProtKB:Q12906,UniProtKB:Q13347,UniProtKB:Q13435,UniProtKB:Q53F35,UniProtKB:Q53GX7,UniProtKB:Q59GL1,UniProtKB:P52292,UniProtKB:Q8NC51,UniProtKB:Q92841,UniProtKB:Q92900,UniProtKB:Q96EY7,UniProtKB:Q99729,UniProtKB:Q9BUJ2,UniProtKB:Q9H6T3,UniProtKB:Q9NZI8,UniProtKB:Q9UHB9,UniProtKB:Q9Y262,UniProtKB:Q9Y285,UniProtKB:Q9Y5A9	F		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:24965446^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:B3KNR3,UniProtKB:B5BTY4,UniProtKB:C7DJS2,UniProtKB:P07910,UniProtKB:P11940,UniProtKB:P12956,UniProtKB:P14923,UniProtKB:P23396,UniProtKB:P28161,UniProtKB:P46782,UniProtKB:P52272,UniProtKB:P61011,UniProtKB:P61247,UniProtKB:P62081,UniProtKB:P62266,UniProtKB:P62701,UniProtKB:P62913,UniProtKB:Q02413,UniProtKB:Q08211,UniProtKB:Q0VAC0,UniProtKB:Q12906,UniProtKB:Q13435,UniProtKB:Q8NC51,UniProtKB:Q92841,UniProtKB:Q92900,UniProtKB:Q9NZI8,UniProtKB:Q9Y262	F		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:24965446^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q08211	F		Seeded From UniProt
involved_in	GO:1990219	positive regulation by symbiont of host protein levels	PMID:24965446^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P67809)	Seeded From UniProt
enables	GO:0005515	protein binding	PMID:24965446^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P67809	F		Seeded From UniProt
part_of	GO:0030430	host cell cytoplasm	PMID:24965446^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
part_of	GO:0042025	host cell nucleus	PMID:24965446^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
involved_in	GO:1903608	protein localization to cytoplasmic stress granule	PMID:24965446^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:25809915^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q764M6	F		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:19540847^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q764M6	F		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:17215286^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q764M6	F		Seeded From UniProt
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:19767841^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:28290554^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
part_of	GO:0019013	viral nucleocapsid	PMID:1870198^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
involved_in	GO:0010468	regulation of gene expression	PMID:9617770^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0090501	RNA phosphodiester bond hydrolysis	PMID:8356450^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
enables	GO:0004540	ribonuclease activity	PMID:8356450^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt
involved_in	GO:0039707	pore formation by virus in membrane of host cell	PMID:24189547^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0039547	suppression by virus of host TRAF activity	PMID:28751780^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
involved_in	GO:0039644	suppression by virus of host NF-kappaB transcription factor activity	PMID:28751780^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt
part_of	GO:0044165	host cell endoplasmic reticulum	PMID:26748656^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:26748656^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:F1S912	F		Seeded From UniProt
enables	GO:0005515	protein binding	PMID:25593157^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19620	F		Seeded From UniProt
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Gottipati, K et al. (2014) Autocatalytic activity and substrate specificity of the pestivirus N-terminal protease Npro. Virology 452-453 303-9 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 Bauhofer, O et al. (2007) Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation. J. Virol. 81 3087-96 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 Mine, J et al. (2015) The N-terminal domain of Npro of classical swine fever virus determines its stability and regulates type I IFN production. J. Gen. Virol. 96 1746-56 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Szymanski, MR et al. (2009) Zinc binding in pestivirus N(pro) is required for interferon regulatory factor 3 interaction and degradation. J. Mol. Biol. 391 438-49 PubMed GONUTS page
↑ ^5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 ^5.12 ^5.13 ^5.14 Jefferson, M et al. (2014) Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex. J. Virol. 88 10340-53 PubMed GONUTS page
↑ ^6.0 ^6.1 Luo, X et al. (2009) Classical swine fever virus Erns glycoprotein antagonizes induction of interferon-beta by double-stranded RNA. Can. J. Microbiol. 55 698-704 PubMed GONUTS page
↑ ^7.0 ^7.1 Riedel, C et al. (2017) The core protein of a pestivirus protects the incoming virus against IFN-induced effectors. Sci Rep 7 44459 PubMed GONUTS page
↑ ^8.0 ^8.1 Thiel, HJ et al. (1991) Hog cholera virus: molecular composition of virions from a pestivirus. J. Virol. 65 4705-12 PubMed GONUTS page
↑ ^9.0 ^9.1 Liu, JJ et al. (1998) The recombinant nucleocapsid protein of classical swine fever virus can act as a transcriptional regulator. Virus Res. 53 75-80 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Schneider, R et al. (1993) Identification of a structural glycoprotein of an RNA virus as a ribonuclease. Science 261 1169-71 PubMed GONUTS page
↑ ^11.0 ^11.1 Largo, E et al. (2014) Pore-forming activity of pestivirus p7 in a minimal model system supports genus-specific viroporin function. Antiviral Res. 101 30-6 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Lv, H et al. (2017) TRAF6 is a novel NS3-interacting protein that inhibits classical swine fever virus replication. Sci Rep 7 6737 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Li, H et al. (2016) FKBP8 interact with classical swine fever virus NS5A protein and promote virus RNA replication. Virus Genes 52 99-106 PubMed GONUTS page
↑ Sheng, C et al. (2015) Annexin A2 is involved in the production of classical swine fever virus infectious particles. J. Gen. Virol. 96 1027-32 PubMed GONUTS page

[PMID:24606708-1] 1.0 ^1.1 ^1.2 ^1.3 Gottipati, K et al. (2014) Autocatalytic activity and substrate specificity of the pestivirus N-terminal protease Npro. Virology 452-453 303-9 PubMed GONUTS page

[PMID:17215286-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 Bauhofer, O et al. (2007) Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation. J. Virol. 81 3087-96 PubMed GONUTS page

[PMID:25809915-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 Mine, J et al. (2015) The N-terminal domain of Npro of classical swine fever virus determines its stability and regulates type I IFN production. J. Gen. Virol. 96 1746-56 PubMed GONUTS page

[PMID:19540847-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Szymanski, MR et al. (2009) Zinc binding in pestivirus N(pro) is required for interferon regulatory factor 3 interaction and degradation. J. Mol. Biol. 391 438-49 PubMed GONUTS page

[PMID:24965446-5] 5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 ^5.12 ^5.13 ^5.14 Jefferson, M et al. (2014) Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex. J. Virol. 88 10340-53 PubMed GONUTS page

[PMID:19767841-6] 6.0 ^6.1 Luo, X et al. (2009) Classical swine fever virus Erns glycoprotein antagonizes induction of interferon-beta by double-stranded RNA. Can. J. Microbiol. 55 698-704 PubMed GONUTS page

[PMID:28290554-7] 7.0 ^7.1 Riedel, C et al. (2017) The core protein of a pestivirus protects the incoming virus against IFN-induced effectors. Sci Rep 7 44459 PubMed GONUTS page

[PMID:1870198-8] 8.0 ^8.1 Thiel, HJ et al. (1991) Hog cholera virus: molecular composition of virions from a pestivirus. J. Virol. 65 4705-12 PubMed GONUTS page

[PMID:9617770-9] 9.0 ^9.1 Liu, JJ et al. (1998) The recombinant nucleocapsid protein of classical swine fever virus can act as a transcriptional regulator. Virus Res. 53 75-80 PubMed GONUTS page

[PMID:8356450-10] 10.0 ^10.1 ^10.2 ^10.3 Schneider, R et al. (1993) Identification of a structural glycoprotein of an RNA virus as a ribonuclease. Science 261 1169-71 PubMed GONUTS page

[PMID:24189547-11] 11.0 ^11.1 Largo, E et al. (2014) Pore-forming activity of pestivirus p7 in a minimal model system supports genus-specific viroporin function. Antiviral Res. 101 30-6 PubMed GONUTS page

[PMID:28751780-12] 12.0 ^12.1 ^12.2 ^12.3 Lv, H et al. (2017) TRAF6 is a novel NS3-interacting protein that inhibits classical swine fever virus replication. Sci Rep 7 6737 PubMed GONUTS page

[PMID:26748656-13] 13.0 ^13.1 ^13.2 ^13.3 Li, H et al. (2016) FKBP8 interact with classical swine fever virus NS5A protein and promote virus RNA replication. Virus Genes 52 99-106 PubMed GONUTS page

[PMID:25593157-14] Sheng, C et al. (2015) Annexin A2 is involved in the production of classical swine fever virus infectious particles. J. Gen. Virol. 96 1027-32 PubMed GONUTS page

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CSFVA:POLG

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