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Protein

Inner capsid protein lambda-1

Gene

L3

Organism
Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Inner capsid (core) component. Displays NTPase, RNA 5'-triphosphatase (RTPase) and RNA helicase activities and probably participates in transcription of the viral genome. Helicase activity might be involved in unwinding or reannealing dsRNA during RNA synthesis. RTPase enzymatic activity represents the first step in RNA capping, which yields a 5'-diphosphorylated plus-strand RNA.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri181 – 203C2H2-typeAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Inner capsid protein lambda-1 (EC:3.6.4.13)
Short name:
Lambda1
Alternative name(s):
ATP-dependent DNA helicase lambda-1
Lambda1(Hel)
Gene namesi
Name:L3
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

  • Virion Curated

  • Note: Found in the inner capsid (120 copies).

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Inner capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002227421 – 1275Inner capsid protein lambda-1Add BLAST1275

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-ray3.60B/C1-1275[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15024.

Family & Domainsi

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri181 – 203C2H2-typeAdd BLAST23

Keywords - Domaini

Zinc-finger

Family and domain databases

InterProiIPR007087. Znf_C2H2.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRIPRKTKG KSSGKGNDST ERADDGSSQL RDKQNNKAGP ATTEPGTSNR
60 70 80 90 100
EQYKARPGIA SVQRATESAE MPMKNNDEGT PDKKGNTKGD LVNEHSEAKD
110 120 130 140 150
EADEATKKQA KDTDKSKAQV TYSDTGINNA NELSRSGNVD NEGGSNQKPM
160 170 180 190 200
STRIAEATSA IVSKHPARVG LPPTASSGHG YQCHVCSAVL FSPLDLDAHV
210 220 230 240 250
ASHGLHGNMT LTSSDIQRHI TEFISSWQNH PIVQVSADVE NKKTAQLLHA
260 270 280 290 300
DTPRLVTWDA GLCTSFKIVP IVPAQVPQDV LAYTFFTSSY AIQSPFPEAA
310 320 330 340 350
VSRIVVHTRW ASNVDFDRDS SVIMAPPTEN NIHLFKQLLN TETLSVRGAN
360 370 380 390 400
PLMFRANVLH MLLEFVLDNL YLNRHTGFSQ DHTPFTEGAN LRSLPGPDAE
410 420 430 440 450
KWYSIMYPTR MGTPNVSKIC NFVASCVRNR VGRFDRAQMM NGAMSEWVDV
460 470 480 490 500
FETSDALTVS IRGRWMARLA RMNINPTEIE WALTECAQGY VTVTSPYAPI
510 520 530 540 550
VNRLMPYRIS NAERQISQII RIMNIGNNAT VIQPVLQDIS VLLQRISPLQ
560 570 580 590 600
IDPTIISNTM STVSESTTQT LSPASSILGK LRPSNSDFSS FRVALAGWLY
610 620 630 640 650
NGVVTTVIDD SSYPKDGGSV TSLENLWDFF ILALALPLTT DPCAPVKAFM
660 670 680 690 700
TLANMMVGFE TIPMDNQIYT QSRRASAFST PHTWPRCFMN IQLISPIDAP
710 720 730 740 750
ILRQWAEIIH RYWPNPSQIR YGAPNVFGSA NLFTPPEVLL LPIDHQPANV
760 770 780 790 800
TTPTLDFTNE LTNWRARVCE LMKNLVDNQR YQPGWTQSLV SSMRGTLDKL
810 820 830 840 850
KLIKSMTPMY LQQLAPVELA VIAPMLPFPP FQVPYVRLDR DRVPTMVGVT
860 870 880 890 900
RQSRDTITQP ALSLSTTNTT VGVPLALDAR AITVALLSGK YPPDLVTNVW
910 920 930 940 950
YADAIYPMYA DTEVFSNLQR DMITCEAVQT LVTLVAQISE TQYPVDRYLD
960 970 980 990 1000
WIPSLRASAA TAATFAEWVN TSMKTAFDLS DMLLEPLLSG DPRMTQLAIQ
1010 1020 1030 1040 1050
YQQYNGRTFN IIPEMPGSVI ADCVQLTAEV FNHEYNLFGI ARGDIIIGRV
1060 1070 1080 1090 1100
QSTHLWSPLA PPPDLVFDRD TPGVHIFGRD CRISFGMNGA APMIRDETGL
1110 1120 1130 1140 1150
MVPFEGNWIF PLALWQMNTR YFNQQFDAWI KTGELRIRIE MGAYPYMLHY
1160 1170 1180 1190 1200
YDPRQYANAW NLTSAWLEEI TPTSIPSVPF MVPISSDHDI SSAPAVQYII
1210 1220 1230 1240 1250
STEYNDRSLF CTNSSSPQTI AGPDKHIPVE RYNILTNPDA PPTQIQLPEV
1260 1270
VDLYNVVTRY AYETPPITAV VMGVP
Length:1,275
Mass (Da):141,834
Last modified:July 22, 2008 - v2
Checksum:i766392415AF80847
GO

Sequence cautioni

The sequence AAA47271 differs from that shown. Reason: Frameshift at positions 1206 and 1259.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti119Q → L in AAA47271 (PubMed:3267236).Curated1
Sequence conflicti174T → I in AAA47271 (PubMed:3267236).Curated1
Sequence conflicti495 – 500SPYAPI → ILPPS in AAA47271 (PubMed:3267236).Curated6
Sequence conflicti583P → R in AAA47271 (PubMed:3267236).Curated1
Sequence conflicti648A → V in AAA47271 (PubMed:3267236).Curated1
Sequence conflicti735P → S in AAA47271 (PubMed:3267236).Curated1
Sequence conflicti852Q → H in AAA47271 (PubMed:3267236).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23747 Genomic RNA. Translation: AAA47271.1. Frameshift.
AF129822 mRNA. Translation: AAD42306.1.
EF494437 Genomic RNA. Translation: ABP48915.1.
PIRiA31286. P3XRD3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23747 Genomic RNA. Translation: AAA47271.1. Frameshift.
AF129822 mRNA. Translation: AAD42306.1.
EF494437 Genomic RNA. Translation: ABP48915.1.
PIRiA31286. P3XRD3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJ6X-ray3.60B/C1-1275[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP15024.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLMBD1_REOVD
AccessioniPrimary (citable) accession number: P15024
Secondary accession number(s): Q9WAB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 22, 2008
Last modified: November 2, 2016
This is version 81 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

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.