LMBD1_REOVD
ID LMBD1_REOVD Reviewed; 1275 AA.
AC P15024; Q9WAB0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 23-FEB-2022, entry version 101.
DE RecName: Full=Inner capsid protein lambda-1;
DE Short=Lambda1;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent DNA helicase lambda-1;
DE AltName: Full=Lambda1(Hel);
GN Name=L3;
OS Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX NCBI_TaxID=10886;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3267236; DOI=10.1016/0042-6822(88)90051-7;
RA Bartlett J.A., Joklik W.K.;
RT "The sequence of the reovirus serotype 3 L3 genome segment which encodes
RT the major core protein lambda 1.";
RL Virology 167:31-37(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION OF FRAMESHIFTS.
RX PubMed=10329567; DOI=10.1006/viro.1999.9707;
RA Harrison S.J., Farsetta D.L., Kim J., Noble S., Broering T.J., Nibert M.L.;
RT "Mammalian reovirus L3 gene sequences and evidence for a distinct amino-
RT terminal region of the lambda1 protein.";
RL Virology 258:54-64(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Infectious clone;
RX PubMed=18005692; DOI=10.1016/j.chom.2007.03.003;
RA Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M.,
RA Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D.,
RA Wilson G.J., Chappell J.D., Dermody T.S.;
RT "A plasmid-based reverse genetics system for animal double-stranded RNA
RT viruses.";
RL Cell Host Microbe 1:147-157(2007).
RN [4]
RP CHARACTERIZATION OF HELICASE ACTIVITY.
RX PubMed=9218469; DOI=10.1074/jbc.272.29.18298;
RA Bisaillon M., Bergeron J., Lemay G.;
RT "Characterization of the nucleoside triphosphate phosphohydrolase and
RT helicase activities of the reovirus lambda1 protein.";
RL J. Biol. Chem. 272:18298-18303(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1-1233.
RC STRAIN=Reassortant F18;
RX PubMed=10801118; DOI=10.1038/35010041;
RA Reinisch K.M., Nibert M.L., Harrison S.C.;
RT "Structure of the reovirus core at 3.6 A resolution.";
RL Nature 404:960-967(2000).
CC -!- FUNCTION: Inner capsid (core) component. Displays NTPase, RNA 5'-
CC triphosphatase (RTPase) and RNA helicase activities and probably
CC participates in transcription of the viral genome. Helicase activity
CC might be involved in unwinding or reannealing dsRNA during RNA
CC synthesis. RTPase enzymatic activity represents the first step in RNA
CC capping, which yields a 5'-diphosphorylated plus-strand RNA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- SUBUNIT: Interacts with protein mu-NS; in viral inclusions.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Found in the inner
CC capsid (120 copies).
CC -!- SIMILARITY: Belongs to the orthoreovirus lambda-1 protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47271.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M23747; AAA47271.1; ALT_FRAME; Genomic_RNA.
DR EMBL; AF129822; AAD42306.1; -; mRNA.
DR EMBL; EF494437; ABP48915.1; -; Genomic_RNA.
DR PIR; A31286; P3XRD3.
DR PDB; 1EJ6; X-ray; 3.60 A; B/C=1-1275.
DR PDBsum; 1EJ6; -.
DR SMR; P15024; -.
DR EvolutionaryTrace; P15024; -.
DR Proteomes; UP000006373; Genome.
DR Proteomes; UP000165799; Genome.
DR GO; GO:0039625; C:viral inner capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1830.10; -; 1.
DR InterPro; IPR044949; Lambda-1/VP3.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Capsid protein; Helicase; Hydrolase;
KW Inner capsid protein; Metal-binding; mRNA capping; mRNA processing;
KW Nucleotide-binding; Reference proteome; Virion; Zinc; Zinc-finger.
FT CHAIN 1..1275
FT /note="Inner capsid protein lambda-1"
FT /id="PRO_0000222742"
FT ZN_FING 181..203
FT /note="C2H2-type"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 119
FT /note="Q -> L (in Ref. 1; AAA47271)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="T -> I (in Ref. 1; AAA47271)"
FT /evidence="ECO:0000305"
FT CONFLICT 495..500
FT /note="SPYAPI -> ILPPS (in Ref. 1; AAA47271)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="P -> R (in Ref. 1; AAA47271)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="A -> V (in Ref. 1; AAA47271)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="P -> S (in Ref. 1; AAA47271)"
FT /evidence="ECO:0000305"
FT CONFLICT 852
FT /note="Q -> H (in Ref. 1; AAA47271)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1275 AA; 141834 MW; 766392415AF80847 CRC64;
MKRIPRKTKG KSSGKGNDST ERADDGSSQL RDKQNNKAGP ATTEPGTSNR EQYKARPGIA
SVQRATESAE MPMKNNDEGT PDKKGNTKGD LVNEHSEAKD EADEATKKQA KDTDKSKAQV
TYSDTGINNA NELSRSGNVD NEGGSNQKPM STRIAEATSA IVSKHPARVG LPPTASSGHG
YQCHVCSAVL FSPLDLDAHV ASHGLHGNMT LTSSDIQRHI TEFISSWQNH PIVQVSADVE
NKKTAQLLHA DTPRLVTWDA GLCTSFKIVP IVPAQVPQDV LAYTFFTSSY AIQSPFPEAA
VSRIVVHTRW ASNVDFDRDS SVIMAPPTEN NIHLFKQLLN TETLSVRGAN PLMFRANVLH
MLLEFVLDNL YLNRHTGFSQ DHTPFTEGAN LRSLPGPDAE KWYSIMYPTR MGTPNVSKIC
NFVASCVRNR VGRFDRAQMM NGAMSEWVDV FETSDALTVS IRGRWMARLA RMNINPTEIE
WALTECAQGY VTVTSPYAPI VNRLMPYRIS NAERQISQII RIMNIGNNAT VIQPVLQDIS
VLLQRISPLQ IDPTIISNTM STVSESTTQT LSPASSILGK LRPSNSDFSS FRVALAGWLY
NGVVTTVIDD SSYPKDGGSV TSLENLWDFF ILALALPLTT DPCAPVKAFM TLANMMVGFE
TIPMDNQIYT QSRRASAFST PHTWPRCFMN IQLISPIDAP ILRQWAEIIH RYWPNPSQIR
YGAPNVFGSA NLFTPPEVLL LPIDHQPANV TTPTLDFTNE LTNWRARVCE LMKNLVDNQR
YQPGWTQSLV SSMRGTLDKL KLIKSMTPMY LQQLAPVELA VIAPMLPFPP FQVPYVRLDR
DRVPTMVGVT RQSRDTITQP ALSLSTTNTT VGVPLALDAR AITVALLSGK YPPDLVTNVW
YADAIYPMYA DTEVFSNLQR DMITCEAVQT LVTLVAQISE TQYPVDRYLD WIPSLRASAA
TAATFAEWVN TSMKTAFDLS DMLLEPLLSG DPRMTQLAIQ YQQYNGRTFN IIPEMPGSVI
ADCVQLTAEV FNHEYNLFGI ARGDIIIGRV QSTHLWSPLA PPPDLVFDRD TPGVHIFGRD
CRISFGMNGA APMIRDETGL MVPFEGNWIF PLALWQMNTR YFNQQFDAWI KTGELRIRIE
MGAYPYMLHY YDPRQYANAW NLTSAWLEEI TPTSIPSVPF MVPISSDHDI SSAPAVQYII
STEYNDRSLF CTNSSSPQTI AGPDKHIPVE RYNILTNPDA PPTQIQLPEV VDLYNVVTRY
AYETPPITAV VMGVP
