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P15024 (LMBD1_REOVD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 68. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inner capsid protein lambda-1
Short name=Lambda1
EC=3.6.4.13
Alternative name(s):
ATP-dependent DNA helicase lambda-1
Lambda1(Hel)
Gene names
Name:L3
OrganismReovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3) [Complete proteome]
Taxonomic identifier10886 [NCBI]
Taxonomic lineageViruses › dsRNA viruses › Reoviridae › Spinareovirinae › Orthoreovirus ›
Virus hostMammalia [TaxID: 40674]

Protein attributes

Sequence length1275 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

ATP + H2O = ADP + phosphate.

Cofactor

Magnesium or manganese.

Subunit structure

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

Subcellular location

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

Sequence similarities

Belongs to the orthoreovirus lambda-1 protein family.

Contains 1 C2H2-type zinc finger.

Sequence caution

The sequence AAA47271.1 differs from that shown. Reason: Frameshift at positions 1206 and 1259.

Ontologies

Keywords
   Biological processmRNA capping
mRNA processing
   Cellular componentVirion
   DomainZinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionCapsid protein
Helicase
Hydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintracellular

Inferred from electronic annotation. Source: InterPro

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12751275Inner capsid protein lambda-1
PRO_0000222742

Regions

Zinc finger181 – 20323C2H2-type

Experimental info

Sequence conflict1191Q → L in AAA47271. Ref.1
Sequence conflict1741T → I in AAA47271. Ref.1
Sequence conflict495 – 5006SPYAPI → ILPPS in AAA47271. Ref.1
Sequence conflict5831P → R in AAA47271. Ref.1
Sequence conflict6481A → V in AAA47271. Ref.1
Sequence conflict7351P → S in AAA47271. Ref.1
Sequence conflict8521Q → H in AAA47271. Ref.1

Secondary structure

1 .................................................................................................................................................................. 1275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15024 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 766392415AF80847

FASTA1,275141,834
        10         20         30         40         50         60 
MKRIPRKTKG KSSGKGNDST ERADDGSSQL RDKQNNKAGP ATTEPGTSNR EQYKARPGIA 

        70         80         90        100        110        120 
SVQRATESAE MPMKNNDEGT PDKKGNTKGD LVNEHSEAKD EADEATKKQA KDTDKSKAQV 

       130        140        150        160        170        180 
TYSDTGINNA NELSRSGNVD NEGGSNQKPM STRIAEATSA IVSKHPARVG LPPTASSGHG 

       190        200        210        220        230        240 
YQCHVCSAVL FSPLDLDAHV ASHGLHGNMT LTSSDIQRHI TEFISSWQNH PIVQVSADVE 

       250        260        270        280        290        300 
NKKTAQLLHA DTPRLVTWDA GLCTSFKIVP IVPAQVPQDV LAYTFFTSSY AIQSPFPEAA 

       310        320        330        340        350        360 
VSRIVVHTRW ASNVDFDRDS SVIMAPPTEN NIHLFKQLLN TETLSVRGAN PLMFRANVLH 

       370        380        390        400        410        420 
MLLEFVLDNL YLNRHTGFSQ DHTPFTEGAN LRSLPGPDAE KWYSIMYPTR MGTPNVSKIC 

       430        440        450        460        470        480 
NFVASCVRNR VGRFDRAQMM NGAMSEWVDV FETSDALTVS IRGRWMARLA RMNINPTEIE 

       490        500        510        520        530        540 
WALTECAQGY VTVTSPYAPI VNRLMPYRIS NAERQISQII RIMNIGNNAT VIQPVLQDIS 

       550        560        570        580        590        600 
VLLQRISPLQ IDPTIISNTM STVSESTTQT LSPASSILGK LRPSNSDFSS FRVALAGWLY 

       610        620        630        640        650        660 
NGVVTTVIDD SSYPKDGGSV TSLENLWDFF ILALALPLTT DPCAPVKAFM TLANMMVGFE 

       670        680        690        700        710        720 
TIPMDNQIYT QSRRASAFST PHTWPRCFMN IQLISPIDAP ILRQWAEIIH RYWPNPSQIR 

       730        740        750        760        770        780 
YGAPNVFGSA NLFTPPEVLL LPIDHQPANV TTPTLDFTNE LTNWRARVCE LMKNLVDNQR 

       790        800        810        820        830        840 
YQPGWTQSLV SSMRGTLDKL KLIKSMTPMY LQQLAPVELA VIAPMLPFPP FQVPYVRLDR 

       850        860        870        880        890        900 
DRVPTMVGVT RQSRDTITQP ALSLSTTNTT VGVPLALDAR AITVALLSGK YPPDLVTNVW 

       910        920        930        940        950        960 
YADAIYPMYA DTEVFSNLQR DMITCEAVQT LVTLVAQISE TQYPVDRYLD WIPSLRASAA 

       970        980        990       1000       1010       1020 
TAATFAEWVN TSMKTAFDLS DMLLEPLLSG DPRMTQLAIQ YQQYNGRTFN IIPEMPGSVI 

      1030       1040       1050       1060       1070       1080 
ADCVQLTAEV FNHEYNLFGI ARGDIIIGRV QSTHLWSPLA PPPDLVFDRD TPGVHIFGRD 

      1090       1100       1110       1120       1130       1140 
CRISFGMNGA APMIRDETGL MVPFEGNWIF PLALWQMNTR YFNQQFDAWI KTGELRIRIE 

      1150       1160       1170       1180       1190       1200 
MGAYPYMLHY YDPRQYANAW NLTSAWLEEI TPTSIPSVPF MVPISSDHDI SSAPAVQYII 

      1210       1220       1230       1240       1250       1260 
STEYNDRSLF CTNSSSPQTI AGPDKHIPVE RYNILTNPDA PPTQIQLPEV VDLYNVVTRY 

      1270 
AYETPPITAV VMGVP

« Hide

References

[1]"The sequence of the reovirus serotype 3 L3 genome segment which encodes the major core protein lambda 1."
Bartlett J.A., Joklik W.K.
Virology 167:31-37(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Mammalian reovirus L3 gene sequences and evidence for a distinct amino-terminal region of the lambda1 protein."
Harrison S.J., Farsetta D.L., Kim J., Noble S., Broering T.J., Nibert M.L.
Virology 258:54-64(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF FRAMESHIFTS.
[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]"Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda1 protein."
Bisaillon M., Bergeron J., Lemay G.
J. Biol. Chem. 272:18298-18303(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF HELICASE ACTIVITY.
[5]"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) OF 1-1233.
Strain: Reassortant F18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M23747 Genomic RNA. Translation: AAA47271.1. Frameshift.
AF129822 mRNA. Translation: AAD42306.1.
EF494437 Genomic RNA. Translation: ABP48915.1.
PIRP3XRD3. A31286.
RefSeqNP_694679.1. NC_004274.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ6X-ray3.60B/C1-1275[»]
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID956468.

Family and domain databases

InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15024.

Entry information

Entry nameLMBD1_REOVD
AccessionPrimary (citable) accession number: P15024
Secondary accession number(s): Q9WAB0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 22, 2008
Last modified: April 3, 2013
This is version 68 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents