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Protein

Outer capsid protein lambda-2

Gene

L2

Organism
Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei190 – 1901Involved in formation of the phosphoamide bondBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi893 – 9008ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GTP binding Source: UniProtKB-KW
  3. mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB-EC
  4. mRNA guanylyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

ATP-binding, GTP-binding, Nucleotide-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Outer capsid protein lambda-2
Short name:
Lambda2
Alternative name(s):
Lambda2(Cap)
Including the following 2 domains:
mRNA guanylyltransferase (EC:2.7.7.50)
mRNA (guanine-N(7)-)-methyltransferase (EC:2.1.1.56)
Gene namesi
Name:L2
OrganismiReovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1)
Taxonomic identifieri10884 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostiMammalia [TaxID: 40674]
ProteomesiUP000007253: Genome

Subcellular locationi

Virion Curated

GO - Cellular componenti

  1. viral outer capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Outer capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12891289Outer capsid protein lambda-2PRO_0000345000Add
BLAST

Interactioni

Subunit structurei

Interacts with protein mu-NS; in viral inclusions.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ91RA6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi181 – 1844Poly-Asp
Compositional biasi894 – 8974Poly-Ala

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR010311. Reovirus_L2.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF06016. Reovirus_L2. 1 hit.
[Graphical view]
PIRSFiPIRSF000845. Reovirus_L2. 1 hit.
ProDomiPD149122. Reovirus_L2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Q91RA6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANVWGVRLA DSLSSPTIET RTRHYTLRDF CSDLDAVAGK EPWRPLRNQR
60 70 80 90 100
TNDIVAVQLF RPLQGLVLDT QFYGFPGIFS EWEQFIKEKL RVLKYEVLRI
110 120 130 140 150
YPISNYNHER VNVFVANALV GAFLSNQAFY DLLPLLVIND TMINDLLGTG
160 170 180 190 200
AALSQFFQSH GEVLEVAAGR KYLQMKNYSN DDDDPPLFAK DLSDYAKAFY
210 220 230 240 250
SDTFETLDRF FWTHDSSAGV LVHYDKPTNG NHYILGTLTQ MVSAPPHIIN
260 270 280 290 300
ATDALLLESC LEQFAANVRA RPAQPVARLD QCYHLRWGAQ YVGEDSLTYR
310 320 330 340 350
LGVLSLLATN GYQLARPIPK QLTNRWLSSF VSQVMSDGVN ETPLWPQERY
360 370 380 390 400
VQIAYDSPSV VDGATHYGYV RRNQLRLGMR VSALQSLSDT PAPIQWLPQY
410 420 430 440 450
TIEQAAVDEG DLMVSRLTQL PLRPDYGSIW VGDALSYYVD YNRSHRVVLS
460 470 480 490 500
SELPQLPDTY FDGDEQYGRS LFSLARKIGD RSLIKDTAVL KHAYQAIDPN
510 520 530 540 550
TGKEYLRAGQ SVAYFGASAG HSGADQPLVI EPWTQGKISG VPPPSSVRQF
560 570 580 590 600
GYDVAKGAIV DLARPFPSGD YQFVYSDVDQ VVDGHDDLSI SSGLVESLLD
610 620 630 640 650
SCMHATSPGG SFVMKINFPT RTVWHYIEQK ILPNITSYML IKPFVTNNVE
660 670 680 690 700
LFFVAFGVHQ QSALTWTSGV YFFLVDHFYR YETLSTISRQ LPSFGYVDDG
710 720 730 740 750
SSVTGIEMIS LENPGFSNMT QAARVGISGL CANVGNARKL ISIHESHGAR
760 770 780 790 800
VLTITSRRSP ASARRKARLR YLPLVDPRSL EVQARTILPS NPVLFDNVNG
810 820 830 840 850
ASPHVCLTMM YNFEVSSAVY DGDVVLDLGT GPEAKILELI PPTSPVTCVD
860 870 880 890 900
IRPTAQPSGC WNVRTTFLEL DYLSDGWITG IRGDIVTCML SLGAAAAGKS
910 920 930 940 950
MTFDAAFQQL VKVLTKSTAN VLLIQVNCPT DVIRTIKGYL EIDQTNKRYR
960 970 980 990 1000
FPKFGRDEPY SDMDSLERIC RAAWPNCSIT WVPLSYDLRW TKLALLESTT
1010 1020 1030 1040 1050
LSSASVRIAE LMYKYMPVMR IDIHGLPMEK QGNFIVGQNC SLTIPGFNAQ
1060 1070 1080 1090 1100
DVFNCYFNSA LAFSTEDVNS AMIPQVTAQF DANKGEWSLD MVFSDAGIYT
1110 1120 1130 1140 1150
MQALVGSNAN PVSLGSFVVD SPDVDITDAW PAQLDFTIAG TDVDITVNPY
1160 1170 1180 1190 1200
YRLMAFVRID GQWQIANPDK FQFFSSSTGT LVMNVKLDIA DRYLLYYIRD
1210 1220 1230 1240 1250
VQSRDVGFYI QHPLQLLNTI TLPTNEDLFL SAPDMREWAV KESGNTICIL
1260 1270 1280
NSQGFVPPQD WDVLTDTISW SPSLPTYVVP PGDYTLTPL
Length:1,289
Mass (Da):143,942
Last modified:December 1, 2001 - v1
Checksum:i44AC4D567FD8A72E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF378003 mRNA. Translation: AAK57507.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF378003 mRNA. Translation: AAK57507.1.

3D structure databases

ProteinModelPortaliQ91RA6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR010311. Reovirus_L2.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF06016. Reovirus_L2. 1 hit.
[Graphical view]
PIRSFiPIRSF000845. Reovirus_L2. 1 hit.
ProDomiPD149122. Reovirus_L2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

  1. "Mammalian reovirus L2 gene and lambda2 core spike protein sequences and whole-genome comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing."
    Breun L.A., Broering T.J., McCutcheon A.M., Harrison S.J., Luongo C.L., Nibert M.L.
    Virology 287:333-348(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Reovirus nonstructural protein mu NS recruits viral core surface proteins and entering core particles to factory-like inclusions."
    Broering T.J., Kim J., Miller C.L., Piggott C.D., Dinoso J.B., Nibert M.L., Parker J.S.L.
    J. Virol. 78:1882-1892(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PROTEIN MU-NS.

Entry informationi

Entry nameiLMBD2_REOVL
AccessioniPrimary (citable) accession number: Q91RA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: December 1, 2001
Last modified: January 7, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.