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Protein

Outer capsid protein lambda-2

Gene

L2

Organism
Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Status
Reviewed-Annotation score: Annotation score: 5 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.

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)DescriptionActionsGraphical viewLength
Sitei190Involved in formation of the phosphoamide bond1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi893 – 900ATPSequence analysis8

GO - Molecular functioni

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 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Taxonomic identifieri10886 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostiMammalia [TaxID: 40674]
Proteomesi
  • UP000006373 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • icosahedral viral capsid Source: CACAO
  • viral outer capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Outer capsid protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi44K → A: Almost no effect on autoguanylylation activity. 1 Publication1
Mutagenesisi89K → A: Almost no effect on autoguanylylation activity. 1 Publication1
Mutagenesisi94K → A: Almost no effect on autoguanylylation activity. 1 Publication1
Mutagenesisi171K → A: Almost complete loss of autoguanylylation activity. 1 Publication1
Mutagenesisi190K → A: Complete loss of autoguanylylation activity. 1 Publication1
Mutagenesisi197K → A: 90% loss of autoguanylylation activity. 1 Publication1
Mutagenesisi226K → A: No effect on autoguanylylation activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002227411 – 1289Outer capsid protein lambda-2Add BLAST1289

Interactioni

Subunit structurei

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJ6X-ray3.60A1-1289[»]
2CSEelectron microscopy7.00U1-1289[»]
ProteinModelPortaliP11079.
SMRiP11079.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11079.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi181 – 184Poly-Asp4
Compositional biasi894 – 897Poly-Ala4

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.

P11079-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANVWGVRLA DSLSSPTIET RTRQYTLHDL CSDLDANPGR EPWKPLRNQR
60 70 80 90 100
TNNIVAVQLF RPLQGLVLDT QLYGFPGAFD DWERFMREKL RVLKYEVLRI
110 120 130 140 150
YPISNYSNEH VNVFVANALV GAFLSNQAFY DLLPLLIIND TMIGDLLGTG
160 170 180 190 200
ASLSQFFQSH GDVLEVAAGR KYLQMENYSN DDDDPPLFAK DLSDYAKAFY
210 220 230 240 250
SDTYEVLDRF FWTHDSSAGV LVHYDKPTNG HHYLLGTLTQ MVSAPPYIIN
260 270 280 290 300
ATDAMLLESC LEQFSANVRA RPAQPVTRLD QCYHLRWGAQ YVGEDSLTYR
310 320 330 340 350
LGVLSLLATN GYQLARPIPR QLTNRWLSSF VSQIMSDGVN ETPLWPQERY
360 370 380 390 400
VQIAYDSPSV VDGATQYGYV RKNQLRLGMR ISALQSLSDT PSPVQWLPQY
410 420 430 440 450
TIDQAAMDEG DLMVSRLTQL PLRPDYGNIW VGDALSYYVD YNRSHRVVLS
460 470 480 490 500
SELPQLPDTY FDGDEQYGRS LFSLARKIGD RSLVKDTAVL KHAYQAIDPN
510 520 530 540 550
TGKEYLRSRQ SVAYFGASAG HSGADQPLVI EPWIQGKISG VPPPSSVRQF
560 570 580 590 600
GYDVARGAIV DLARPFPSGD YQFVYSDVDQ VVDGHDDLSI SSGLVESLLS
610 620 630 640 650
SCMHATAPGG SFVVKINFPT RPVWHYIEQK ILPNITSYML IKPFVTNNVE
660 670 680 690 700
LFFVAFGVHQ HSSLTWTSGV YFFLVDHFYR YETLSTISRQ LPSFGYVDDG
710 720 730 740 750
SSVTGIETIS IENPGFSNMT QAARIGISGL CANVGNARKS IAIYESHGAR
760 770 780 790 800
VLTITSRRSP ASARRKSRLR YLPLIDPRSL EVQARTILPA DPVLFENVSG
810 820 830 840 850
ASPHVCLTMM YNFEVSSAVY DGDVVLDLGT GPEAKILELI PATSPVTCVD
860 870 880 890 900
IRPTAQPSGC WNVRTTFLEL DYLSDGWITG VRGDIVTCML SLGAAAAGKS
910 920 930 940 950
MTFDAAFQQL IKVLSKSTAN VVLVQVNCPT DVVRSIKGYL EIDSTNKRYR
960 970 980 990 1000
FPKFGRDEPY SDMDALEKIC RTAWPNCSIT WVPLSYDLRW TRLALLESTT
1010 1020 1030 1040 1050
LSSASIRIAE LMYKYMPIMR IDIHGLPMEK RGNFIVGQNC SLVIPGFNAQ
1060 1070 1080 1090 1100
DVFNCYFNSA LAFSTEDVNA AMIPQVSAQF DATKGEWTLD MVFSDAGIYT
1110 1120 1130 1140 1150
MQALVGSNAN PVSLGSFVVD SPDVDITDAW PAQLDFTIAG TDVDITVNPY
1160 1170 1180 1190 1200
YRLMTFVRID GQWQIANPDK FQFFSSASGT LVMNVKLDIA DKYLLYYIRD
1210 1220 1230 1240 1250
VQSRDVGFYI QHPLQLLNTI TLPTNEDLFL SAPDMREWAV KESGNTICIL
1260 1270 1280
NSQGFVLPQD WDVLTDTISW SPSIPTYIVP PGDYTLTPL
Length:1,289
Mass (Da):143,976
Last modified:July 22, 2008 - v2
Checksum:iD96FCEE31855F41C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti504E → G in ABP48914 (PubMed:10644745).Curated1
Sequence conflicti509R → G in ABP48914 (PubMed:10644745).Curated1
Sequence conflicti609G → F in AAA47253 (PubMed:2824487).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03488 Genomic RNA. Translation: AAA47253.1.
EF494436 Genomic RNA. Translation: ABP48914.1.
PIRiA28471. RMXRR3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03488 Genomic RNA. Translation: AAA47253.1.
EF494436 Genomic RNA. Translation: ABP48914.1.
PIRiA28471. RMXRR3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJ6X-ray3.60A1-1289[»]
2CSEelectron microscopy7.00U1-1289[»]
ProteinModelPortaliP11079.
SMRiP11079.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP11079.

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...

Entry informationi

Entry nameiLMBD2_REOVD
AccessioniPrimary (citable) accession number: P11079
Secondary accession number(s): A4ZY21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 22, 2008
Last modified: November 2, 2016
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.