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P32503 (GAG_SCVLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Major capsid protein
Alternative name(s):
Gag protein
Major coat protein
Gene names
Name:gag
OrganismSaccharomyces cerevisiae virus L-A (ScV-L-A) (ScVL1) [Reference proteome]
Taxonomic identifier11008 [NCBI]
Taxonomic lineageViruses › dsRNA viruses › Totiviridae › Totivirus
Virus hostSaccharomyces cerevisiae (Baker's yeast) [TaxID: 4932]

Protein attributes

Sequence length680 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Capsid protein self-assembles to form an icosahedral capsid with a T=2 symmetry, 40 nm in diameter, and consisting of 60 capsid proteins asymmetric dimers. The capsid encapsulates the genomic dsRNA and the polymerase and remains intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nacent transcripts are transcribed within the structural confines of the virion and are extruded into the cytoplasm. Ref.3 Ref.4

Binds and removes 5' cap structures from cellular mRNA. Forms a covalent bond with m7GMP through His-154 of the capsid protein while releasing the mRNA body. Ref.3 Ref.4

Subcellular location

Virion Potential.

Post-translational modification

Acetylation is necessary for viral assembly.

Sequence similarities

Belongs to the totivirus major capsid protein family.

Ontologies

Keywords
   Cellular componentVirion
   Coding sequence diversityRibosomal frameshifting
   Molecular functionCapsid protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentviral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]
Isoform Major capsid protein (identifier: P32503-1)

Also known as: Gag protein;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by conventional translation.
Isoform RNA-directed RNA polymerase (identifier: Q87022-1)

Also known as: Pol protein;

The sequence of this isoform can be found in the external entry Q87022.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 680680Major capsid protein
PRO_0000222991

Amino acid modifications

Modified residue11N-acetylmethionine; by host N-acetyltransferase MAK3
Modified residue5801Phosphoserine Ref.5

Experimental info

Sequence conflict26 – 272FV → LL Ref.2

Secondary structure

1 ................................................................................................................ 680
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Major capsid protein (Gag protein) [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 32353D8B7F05C943

FASTA68075,994
        10         20         30         40         50         60 
MLRFVTKNSQ DKSSDLFSIC SDRGTFVAHN RVRTDFKFDN LVFNRVYGVS QKFTLVGNPT 

        70         80         90        100        110        120 
VCFNEGSSYL EGIAKKYLTL DGGLAIDNVL NELRSTCGIP GNAVASHAYN ITSWRWYDNH 

       130        140        150        160        170        180 
VALLMNMLRA YHLQVLTEQG QYSAGDIPMY HDGHVKIKLP VTIDDTAGPT QFAWPSDRST 

       190        200        210        220        230        240 
DSYPDWAQFS ESFPSIDVPY LDVRPLTVTE VNFVLMMMSK WHRRTNLAID YEAPQLADKF 

       250        260        270        280        290        300 
AYRHALTVQD ADEWIEGDRT DDQFRPPSSK VMLSALRKYV NHNRLYNQFY TAAQLLAQIM 

       310        320        330        340        350        360 
MKPVPNCAEG YAWLMHDALV NIPKFGSIRG RYPFLLSGDA ALIQATALED WSAIMAKPEL 

       370        380        390        400        410        420 
VFTYAMQVSV ALNTGLYLRR VKKTGFGTTI DDSYEDGAFL QPETFVQAAL ACCTGQDAPL 

       430        440        450        460        470        480 
NGMSDVYVTY PDLLEFDAVT QVPITVIEPA GYNIVDDHLV VVGVPVACSP YMIFPVAAFD 

       490        500        510        520        530        540 
TANPYCGNFV IKAANKYLRK GAVYDKLEAW KLAWALRVAG YDTHFKVYGD THGLTKFYAD 

       550        560        570        580        590        600 
NGDTWTHIPE FVTDGDVMEV FVTAIERRAR HFVELPRLNS PAFFRSVEVS TTIYDTHVQA 

       610        620        630        640        650        660 
GAHAVYHASR INLDYVKPVS TGIQVINAGE LKNYWGSVRR TQQGLGVVGL TMPAVMPTGE 

       670        680 
PTAGAAHEEL IEQADNVLVE

« Hide

Isoform RNA-directed RNA polymerase (Pol protein) [UniParc].

See Q87022.

––

References

« Hide 'large scale' references
[1]"The double-stranded RNA genome of yeast virus L-A encodes its own putative RNA polymerase by fusing two open reading frames."
Icho T., Wickner R.B.
J. Biol. Chem. 264:6716-6723(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Multiple L double-stranded RNA species of Saccharomyces cerevisiae: evidence for separate encapsidation."
Thiele D.J., Hannig E.M., Leibowitz M.J.
Mol. Cell. Biol. 4:92-100(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-27.
[3]"The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA."
Blanc A., Goyer C., Sonenberg N.
Mol. Cell. Biol. 12:3390-3398(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Decoying the cap- mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system."
Masison D.C., Blanc A., Ribas J.C., Carroll K., Sonenberg N., Wickner R.B.
Mol. Cell. Biol. 15:2763-2771(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, MASS SPECTROMETRY.
Strain: ADR376.
[6]"L-A virus at 3.4 A resolution reveals particle architecture and mRNA decapping mechanism."
Naitow H., Tang J., Canady M., Wickner R.B., Johnson J.E.
Nat. Struct. Biol. 9:725-728(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04692 Genomic RNA. Translation: AAA50506.1.
PIRS26764.
RefSeqNP_620494.1. NC_003745.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M1CX-ray3.50A/B1-680[»]
ProteinModelPortalP32503.
SMRP32503. Positions 1-651.
ModBaseSearch...

Proteomic databases

PRIDEP32503.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID940477.

Family and domain databases

InterProIPR015302. Major_coat_LA-virus.
[Graphical view]
PfamPF09220. LA-virus_coat. 1 hit.
[Graphical view]
SUPFAMSSF82856. Major_coat_LA-virus. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP32503.

Entry information

Entry nameGAG_SCVLA
AccessionPrimary (citable) accession number: P32503
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 3, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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