Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P15024

- LMBD1_REOVD

UniProt

P15024 - LMBD1_REOVD

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    MKRIPRKTKG KSSGKGNDST ERADDGSSQL RDKQNNKAGP ATTEPGTSNR     50
    EQYKARPGIA SVQRATESAE MPMKNNDEGT PDKKGNTKGD LVNEHSEAKD 100
    EADEATKKQA KDTDKSKAQV TYSDTGINNA NELSRSGNVD NEGGSNQKPM 150
    STRIAEATSA IVSKHPARVG LPPTASSGHG YQCHVCSAVL FSPLDLDAHV 200
    ASHGLHGNMT LTSSDIQRHI TEFISSWQNH PIVQVSADVE NKKTAQLLHA 250
    DTPRLVTWDA GLCTSFKIVP IVPAQVPQDV LAYTFFTSSY AIQSPFPEAA 300
    VSRIVVHTRW ASNVDFDRDS SVIMAPPTEN NIHLFKQLLN TETLSVRGAN 350
    PLMFRANVLH MLLEFVLDNL YLNRHTGFSQ DHTPFTEGAN LRSLPGPDAE 400
    KWYSIMYPTR MGTPNVSKIC NFVASCVRNR VGRFDRAQMM NGAMSEWVDV 450
    FETSDALTVS IRGRWMARLA RMNINPTEIE WALTECAQGY VTVTSPYAPI 500
    VNRLMPYRIS NAERQISQII RIMNIGNNAT VIQPVLQDIS VLLQRISPLQ 550
    IDPTIISNTM STVSESTTQT LSPASSILGK LRPSNSDFSS FRVALAGWLY 600
    NGVVTTVIDD SSYPKDGGSV TSLENLWDFF ILALALPLTT DPCAPVKAFM 650
    TLANMMVGFE TIPMDNQIYT QSRRASAFST PHTWPRCFMN IQLISPIDAP 700
    ILRQWAEIIH RYWPNPSQIR YGAPNVFGSA NLFTPPEVLL LPIDHQPANV 750
    TTPTLDFTNE LTNWRARVCE LMKNLVDNQR YQPGWTQSLV SSMRGTLDKL 800
    KLIKSMTPMY LQQLAPVELA VIAPMLPFPP FQVPYVRLDR DRVPTMVGVT 850
    RQSRDTITQP ALSLSTTNTT VGVPLALDAR AITVALLSGK YPPDLVTNVW 900
    YADAIYPMYA DTEVFSNLQR DMITCEAVQT LVTLVAQISE TQYPVDRYLD 950
    WIPSLRASAA TAATFAEWVN TSMKTAFDLS DMLLEPLLSG DPRMTQLAIQ 1000
    YQQYNGRTFN IIPEMPGSVI ADCVQLTAEV FNHEYNLFGI ARGDIIIGRV 1050
    QSTHLWSPLA PPPDLVFDRD TPGVHIFGRD CRISFGMNGA APMIRDETGL 1100
    MVPFEGNWIF PLALWQMNTR YFNQQFDAWI KTGELRIRIE MGAYPYMLHY 1150
    YDPRQYANAW NLTSAWLEEI TPTSIPSVPF MVPISSDHDI SSAPAVQYII 1200
    STEYNDRSLF CTNSSSPQTI AGPDKHIPVE RYNILTNPDA PPTQIQLPEV 1250
    VDLYNVVTRY AYETPPITAV VMGVP 1275
    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