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P15024

- LMBD1_REOVD

UniProt

P15024 - LMBD1_REOVD

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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: 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

Magnesium or manganese.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri181 – 20323C2H2-typeAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. helicase activity Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: UniProtKB-KW
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]
ProteomesiUP000006373: Genome

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Capsid protein, Inner capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12751275Inner capsid protein lambda-1PRO_0000222742Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
1275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi242 – 2487
Beta strandi265 – 2739
Beta strandi279 – 2813
Helixi283 – 2853
Helixi287 – 2904
Beta strandi299 – 3079
Beta strandi314 – 3163
Helixi332 – 3343
Beta strandi335 – 3395
Beta strandi346 – 3494
Helixi351 – 3533
Helixi354 – 36714
Beta strandi372 – 3743
Beta strandi378 – 3803
Turni384 – 3874
Beta strandi390 – 3923
Beta strandi396 – 3983
Helixi402 – 4065
Helixi408 – 4103
Helixi418 – 4247
Beta strandi432 – 4365
Beta strandi446 – 4538
Helixi456 – 47217
Helixi476 – 48611
Turni487 – 4893
Helixi510 – 52213
Turni523 – 5264
Helixi528 – 54518
Helixi553 – 5597
Helixi572 – 5809
Helixi588 – 5969
Turni600 – 6023
Beta strandi603 – 6075
Helixi609 – 6113
Helixi622 – 63413
Helixi635 – 6373
Helixi643 – 65513
Turni656 – 6583
Beta strandi664 – 6685
Helixi674 – 6763
Helixi680 – 6823
Helixi685 – 6884
Helixi690 – 6923
Turni695 – 6973
Helixi699 – 71113
Beta strandi716 – 7194
Helixi723 – 7264
Beta strandi731 – 7333
Beta strandi737 – 7426
Helixi759 – 77517
Turni778 – 7803
Helixi781 – 7833
Helixi786 – 80015
Helixi806 – 8127
Helixi814 – 8218
Helixi822 – 8243
Helixi839 – 8413
Beta strandi843 – 8508
Helixi859 – 8624
Helixi863 – 8653
Beta strandi872 – 8765
Helixi878 – 8869
Beta strandi887 – 8893
Helixi896 – 9049
Helixi905 – 9095
Helixi912 – 93726
Helixi958 – 97619
Turni984 – 9863
Beta strandi997 – 10026
Beta strandi1007 – 10104
Helixi1018 – 103316
Helixi1034 – 10374
Beta strandi1039 – 105214
Helixi1062 – 10643
Beta strandi1092 – 10943
Beta strandi1096 – 10983
Beta strandi1100 – 11034
Beta strandi1105 – 11106
Helixi1111 – 11155
Helixi1118 – 113013
Beta strandi1132 – 115019
Helixi1159 – 11679
Beta strandi1177 – 11826
Beta strandi1185 – 11873
Beta strandi1194 – 12029
Helixi1205 – 12073
Beta strandi1208 – 12125
Helixi1228 – 12314

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri181 – 20323C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 1 hit.
[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 AAA47271.1 differs from that shown. Reason: Frameshift at positions 1206 and 1259.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191Q → L in AAA47271. (PubMed:3267236)Curated
Sequence conflicti174 – 1741T → I in AAA47271. (PubMed:3267236)Curated
Sequence conflicti495 – 5006SPYAPI → ILPPS in AAA47271. (PubMed:3267236)Curated
Sequence conflicti583 – 5831P → R in AAA47271. (PubMed:3267236)Curated
Sequence conflicti648 – 6481A → V in AAA47271. (PubMed:3267236)Curated
Sequence conflicti735 – 7351P → S in AAA47271. (PubMed:3267236)Curated
Sequence conflicti852 – 8521Q → H in AAA47271. (PubMed:3267236)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23747 Genomic RNA. Translation: AAA47271.1. Frameshift.
AF129822 mRNA. Translation: AAD42306.1.
EF494437 Genomic RNA. Translation: ABP48915.1.
PIRiA31286. P3XRD3.
RefSeqiNP_694679.1. NC_004274.1.

Genome annotation databases

GeneIDi956468.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23747 Genomic RNA. Translation: AAA47271.1 . Frameshift.
AF129822 mRNA. Translation: AAD42306.1 .
EF494437 Genomic RNA. Translation: ABP48915.1 .
PIRi A31286. P3XRD3.
RefSeqi NP_694679.1. NC_004274.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EJ6 X-ray 3.60 B/C 1-1275 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 956468.

Miscellaneous databases

EvolutionaryTracei P15024.

Family and domain databases

InterProi IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

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: October 1, 2014
This is version 74 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

External Data

Dasty 3