Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P11079 (LMBD2_REOVD) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

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

Names and origin

Protein namesRecommended name:
Outer capsid protein lambda-2

Short name=Lambda2
Alternative name(s):
Lambda2(Cap)

Including the following 2 domains:

  1. mRNA guanylyltransferase
    EC=2.7.7.50
  2. mRNA (guanine-N(7)-)-methyltransferase
    EC=2.1.1.56
Gene names
Name:L2
OrganismReovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3) [Complete proteome]
Taxonomic identifier10886 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostMammalia [TaxID: 40674]

Protein attributes

Sequence length1289 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Outer capsid protein involved in mRNA capping. Catalyzes the last 3 enzymatic activities for formation of the 5' cap structure on the viral plus-strand transcripts, namely the RNA guanylyltransferase, RNA-7N- and RNA-2'O-methyltransferase activities.

Catalytic activity

GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.

Subunit structure

Interacts with protein mu-NS; in viral inclusions By similarity.

Subcellular location

Virion Potential.

Sequence similarities

Belongs to the orthoreovirus lambda-2 protein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12891289Outer capsid protein lambda-2
PRO_0000222741

Regions

Nucleotide binding893 – 9008ATP Potential
Compositional bias181 – 1844Poly-Asp
Compositional bias894 – 8974Poly-Ala

Sites

Site1901Involved in formation of the phosphoamide bond

Experimental info

Mutagenesis441K → A: Almost no effect on autoguanylylation activity. Ref.2
Mutagenesis891K → A: Almost no effect on autoguanylylation activity. Ref.2
Mutagenesis941K → A: Almost no effect on autoguanylylation activity. Ref.2
Mutagenesis1711K → A: Almost complete loss of autoguanylylation activity. Ref.2
Mutagenesis1901K → A: Complete loss of autoguanylylation activity. Ref.2
Mutagenesis1971K → A: 90% loss of autoguanylylation activity. Ref.2
Mutagenesis2261K → A: No effect on autoguanylylation activity. Ref.2
Sequence conflict5041E → G in ABP48914. Ref.2
Sequence conflict5091R → G in ABP48914. Ref.2
Sequence conflict6091G → F in AAA47253. Ref.1

Secondary structure

.................................................................................................................................................................................................................................. 1289
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11079 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: D96FCEE31855F41C

FASTA1,289143,976
        10         20         30         40         50         60 
MANVWGVRLA DSLSSPTIET RTRQYTLHDL CSDLDANPGR EPWKPLRNQR TNNIVAVQLF 

        70         80         90        100        110        120 
RPLQGLVLDT QLYGFPGAFD DWERFMREKL RVLKYEVLRI YPISNYSNEH VNVFVANALV 

       130        140        150        160        170        180 
GAFLSNQAFY DLLPLLIIND TMIGDLLGTG ASLSQFFQSH GDVLEVAAGR KYLQMENYSN 

       190        200        210        220        230        240 
DDDDPPLFAK DLSDYAKAFY SDTYEVLDRF FWTHDSSAGV LVHYDKPTNG HHYLLGTLTQ 

       250        260        270        280        290        300 
MVSAPPYIIN ATDAMLLESC LEQFSANVRA RPAQPVTRLD QCYHLRWGAQ YVGEDSLTYR 

       310        320        330        340        350        360 
LGVLSLLATN GYQLARPIPR QLTNRWLSSF VSQIMSDGVN ETPLWPQERY VQIAYDSPSV 

       370        380        390        400        410        420 
VDGATQYGYV RKNQLRLGMR ISALQSLSDT PSPVQWLPQY TIDQAAMDEG DLMVSRLTQL 

       430        440        450        460        470        480 
PLRPDYGNIW VGDALSYYVD YNRSHRVVLS SELPQLPDTY FDGDEQYGRS LFSLARKIGD 

       490        500        510        520        530        540 
RSLVKDTAVL KHAYQAIDPN TGKEYLRSRQ SVAYFGASAG HSGADQPLVI EPWIQGKISG 

       550        560        570        580        590        600 
VPPPSSVRQF GYDVARGAIV DLARPFPSGD YQFVYSDVDQ VVDGHDDLSI SSGLVESLLS 

       610        620        630        640        650        660 
SCMHATAPGG SFVVKINFPT RPVWHYIEQK ILPNITSYML IKPFVTNNVE LFFVAFGVHQ 

       670        680        690        700        710        720 
HSSLTWTSGV YFFLVDHFYR YETLSTISRQ LPSFGYVDDG SSVTGIETIS IENPGFSNMT 

       730        740        750        760        770        780 
QAARIGISGL CANVGNARKS IAIYESHGAR VLTITSRRSP ASARRKSRLR YLPLIDPRSL 

       790        800        810        820        830        840 
EVQARTILPA DPVLFENVSG ASPHVCLTMM YNFEVSSAVY DGDVVLDLGT GPEAKILELI 

       850        860        870        880        890        900 
PATSPVTCVD IRPTAQPSGC WNVRTTFLEL DYLSDGWITG VRGDIVTCML SLGAAAAGKS 

       910        920        930        940        950        960 
MTFDAAFQQL IKVLSKSTAN VVLVQVNCPT DVVRSIKGYL EIDSTNKRYR FPKFGRDEPY 

       970        980        990       1000       1010       1020 
SDMDALEKIC RTAWPNCSIT WVPLSYDLRW TRLALLESTT LSSASIRIAE LMYKYMPIMR 

      1030       1040       1050       1060       1070       1080 
IDIHGLPMEK RGNFIVGQNC SLVIPGFNAQ DVFNCYFNSA LAFSTEDVNA AMIPQVSAQF 

      1090       1100       1110       1120       1130       1140 
DATKGEWTLD MVFSDAGIYT MQALVGSNAN PVSLGSFVVD SPDVDITDAW PAQLDFTIAG 

      1150       1160       1170       1180       1190       1200 
TDVDITVNPY YRLMTFVRID GQWQIANPDK FQFFSSASGT LVMNVKLDIA DKYLLYYIRD 

      1210       1220       1230       1240       1250       1260 
VQSRDVGFYI QHPLQLLNTI TLPTNEDLFL SAPDMREWAV KESGNTICIL NSQGFVLPQD 

      1270       1280 
WDVLTDTISW SPSIPTYIVP PGDYTLTPL 

« Hide

References

[1]"Complete nucleotide sequence of reovirus L2 gene and deduced amino acid sequence of viral mRNA guanylyltransferase."
Seliger L.S., Zheng K., Shatkin A.J.
J. Biol. Chem. 262:16289-16293(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2."
Luongo C.L., Reinisch K.M., Harrison S.C., Nibert M.L.
J. Biol. Chem. 275:2804-2810(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], SEQUENCE REVISION TO 609, CHARACTERIZATION OF GUANYLYLTRANSFERASE ACTIVITY, MUTAGENESIS OF LYS-44; LYS-89; LYS-94; LYS-171; LYS-190; LYS-197 AND LYS-226.
[3]"A plasmid-based reverse genetics system for animal double-stranded RNA viruses."
Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M., Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D., Wilson G.J., Chappell J.D., Dermody T.S.
Cell Host Microbe 1:147-157(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Infectious clone.
[4]"Structure of the reovirus core at 3.6 A resolution."
Reinisch K.M., Nibert M.L., Harrison S.C.
Nature 404:960-967(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
Strain: Reassortant F18.
[5]"Features of reovirus outer capsid protein mu1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom resolution."
Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L., Baker T.S.
Structure 13:1545-1557(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03488 Genomic RNA. Translation: AAA47253.1.
EF494436 Genomic RNA. Translation: ABP48914.1.
PIRRMXRR3. A28471.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ6X-ray3.60A1-1289[»]
2CSEelectron microscopy7.00U1-1289[»]
ProteinModelPortalP11079.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.40.50.150. 1 hit.
InterProIPR013783. Ig-like_fold.
IPR010311. Reovirus_L2.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF06016. Reovirus_L2. 1 hit.
[Graphical view]
PIRSFPIRSF000845. Reovirus_L2. 1 hit.
ProDomPD149122. Reovirus_L2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceP11079.

Entry information

Entry nameLMBD2_REOVD
AccessionPrimary (citable) accession number: P11079
Secondary accession number(s): A4ZY21
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references