Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Genome polyprotein  

UniProtKB / Swiss-Prot ID :  POLG_BVDVC

Gene Name (Synonyms) :  -
 

Species :  Bovine viral diarrhea virus (strain CP7) (BVDV) (Mucosal diseasevirus). 

Subcellular Localization :  E(rns) glycoprotein: Host membrane; Peripheral membrane protein. Note=The C-terminus membrane anchor of Erns represents an amphipathic helix embedded in plane into the membrane (Probable). Envelope glycoprotein E2: Host cell surface (By similarity). Cyst 

Protein Function :  Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (By similarity). P7 forms a leader sequence to properly orient NS2 in the membrane (By similarity). Uncleaved NS2-3 is required for production of infectious virus. NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus. NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS4A is a cofactor for the NS3 protease activity (By similarity). RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome. 

Transmembrane Topology (topPTM) : POLG_BVDVC 

Protein Sequence MELITNELLYKTYKQKPAGVEEPVYDQAGNPLFGERGVIHPQSTLKLPHKRGEREVPTNLASLPKRGDCR...
Predicted Secondary Structure CCCCHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHCCCCHHCCCCCCCHHHHHCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
272N-linked (GlcNAc...); by hostTMGENITQW
HHCCCCEEE
36.56UniProtKB
Link-
281N-linked (GlcNAc...); by hostNLQDNGTEG
CCCCCCHHH
46.45UniProtKB
Link-
296N-linked (GlcNAc...); by hostQRGVNRSLH
HHCCCCCCC
30.55UniProtKB
Link-
335N-linked (GlcNAc...); by hostSEKTNYTCC
CCCCCEEEE
40.98UniProtKB
Link-
365N-linked (GlcNAc...); by hostILLMNKTQA
HHEECCCCC
44.16UniProtKB
Link-
370N-linked (GlcNAc...); by hostKTQANLTEG
CCCCCCCCC
37.36UniProtKB
Link-
413N-linked (GlcNAc...); by hostKKGKNFSFA
CCCCCEEEE
46.60UniProtKB
Link-
487N-linked (GlcNAc...); by hostKKLENKSKT
HHHCCCCCC
65.42UniProtKB
Link-
597N-linked (GlcNAc...); by hostKNQLNLTVE
CCEEEEEEE
24.73UniProtKB
Link-
809N-linked (GlcNAc...); by hostRGKFNTTLL
ECCCCEEEE
35.32UniProtKB
Link-
878N-linked (GlcNAc...); by hostALGGNWTCV
ECCCCEEEE
29.14UniProtKB
Link-
922N-linked (GlcNAc...); by hostCRLKNESGY
EEECCCCCC
53.94UniProtKB
Link-
990N-linked (GlcNAc...); by hostACTFNYTRT
EEEEHHHHH
21.07UniProtKB
Link-
1366N-linked (GlcNAc...); by hostKKNKNISIL
CCCCHHHHH
42.50UniProtKB
Link-
1428N-linked (GlcNAc...); by hostLIELNWSME
HHHHCCCCC
18.91UniProtKB
Link-
1460N-linked (GlcNAc...); by hostHKVRNQTVA
HHHCCCEEE
44.88UniProtKB
Link-
1722N-linked (GlcNAc...); by hostPEAVNISGS
CCCCCCCCC
29.74UniProtKB
Link-
2143N-linked (GlcNAc...); by hostEDGINVTKS
HHHHHHHHH
40.72UniProtKB
Link-
2226N-linked (GlcNAc...); by hostDTYENYSFL
CCCCCCCCC
27.60UniProtKB
Link-
2503N-linked (GlcNAc...); by hostWNYNNLSKV
CCCCCHHHH
35.02UniProtKB
Link-
2691N-linked (GlcNAc...); by hostGKIRNLSGN
CCEEECCHH
41.87UniProtKB
Link-
2900N-linked (GlcNAc...); by hostLTLSNLTRL
EEHHHHHHH
48.85UniProtKB
Link-
3697N-linked (GlcNAc...); by hostRWSDNTSSY
EECCCCEEE
36.02UniProtKB
Link-
3802N-linked (GlcNAc...); by hostLANLNLSLS
HHHCCCCHH
27.65UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures