LMBD2_REOVL
ID LMBD2_REOVL Reviewed; 1289 AA.
AC Q91RA6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Outer capsid protein lambda-2;
DE Short=Lambda2;
DE AltName: Full=Lambda2(Cap);
DE Includes:
DE RecName: Full=mRNA guanylyltransferase;
DE EC=2.7.7.50;
DE Includes:
DE RecName: Full=mRNA (guanine-N(7))-methyltransferase;
DE EC=2.1.1.56;
GN Name=L2;
OS Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX NCBI_TaxID=10884;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11531411; DOI=10.1006/viro.2001.1052;
RA Breun L.A., Broering T.J., McCutcheon A.M., Harrison S.J., Luongo C.L.,
RA Nibert M.L.;
RT "Mammalian reovirus L2 gene and lambda2 core spike protein sequences and
RT whole-genome comparisons of reoviruses type 1 Lang, type 2 Jones, and type
RT 3 Dearing.";
RL Virology 287:333-348(2001).
RN [2]
RP INTERACTION WITH PROTEIN MU-NS.
RX PubMed=14747553; DOI=10.1128/jvi.78.4.1882-1892.2004;
RA Broering T.J., Kim J., Miller C.L., Piggott C.D., Dinoso J.B., Nibert M.L.,
RA Parker J.S.L.;
RT "Reovirus nonstructural protein mu NS recruits viral core surface proteins
RT and entering core particles to factory-like inclusions.";
RL J. Virol. 78:1882-1892(2004).
CC -!- FUNCTION: Outer capsid protein involved in mRNA capping. Catalyzes the
CC last 3 enzymatic activities for formation of the 5' cap structure on
CC the viral plus-strand transcripts, namely the RNA guanylyltransferase,
CC RNA-7N- and RNA-2'O-methyltransferase activities (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56;
CC -!- SUBUNIT: Interacts with protein mu-NS; in viral inclusions.
CC {ECO:0000269|PubMed:14747553}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the orthoreovirus lambda-2 protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF378003; AAK57507.1; -; mRNA.
DR SMR; Q91RA6; -.
DR Proteomes; UP000007253; Genome.
DR GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR010311; Reovirus_L2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF06016; Reovirus_L2; 1.
DR PIRSF; PIRSF000845; Reovirus_L2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Capsid protein; GTP-binding; Methyltransferase; mRNA capping;
KW mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Outer capsid protein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Virion.
FT CHAIN 1..1289
FT /note="Outer capsid protein lambda-2"
FT /id="PRO_0000345000"
FT BINDING 893..900
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 190
FT /note="Involved in formation of the phosphoamide bond"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1289 AA; 143942 MW; 44AC4D567FD8A72E CRC64;
MANVWGVRLA DSLSSPTIET RTRHYTLRDF CSDLDAVAGK EPWRPLRNQR TNDIVAVQLF
RPLQGLVLDT QFYGFPGIFS EWEQFIKEKL RVLKYEVLRI YPISNYNHER VNVFVANALV
GAFLSNQAFY DLLPLLVIND TMINDLLGTG AALSQFFQSH GEVLEVAAGR KYLQMKNYSN
DDDDPPLFAK DLSDYAKAFY SDTFETLDRF FWTHDSSAGV LVHYDKPTNG NHYILGTLTQ
MVSAPPHIIN ATDALLLESC LEQFAANVRA RPAQPVARLD QCYHLRWGAQ YVGEDSLTYR
LGVLSLLATN GYQLARPIPK QLTNRWLSSF VSQVMSDGVN ETPLWPQERY VQIAYDSPSV
VDGATHYGYV RRNQLRLGMR VSALQSLSDT PAPIQWLPQY TIEQAAVDEG DLMVSRLTQL
PLRPDYGSIW VGDALSYYVD YNRSHRVVLS SELPQLPDTY FDGDEQYGRS LFSLARKIGD
RSLIKDTAVL KHAYQAIDPN TGKEYLRAGQ SVAYFGASAG HSGADQPLVI EPWTQGKISG
VPPPSSVRQF GYDVAKGAIV DLARPFPSGD YQFVYSDVDQ VVDGHDDLSI SSGLVESLLD
SCMHATSPGG SFVMKINFPT RTVWHYIEQK ILPNITSYML IKPFVTNNVE LFFVAFGVHQ
QSALTWTSGV YFFLVDHFYR YETLSTISRQ LPSFGYVDDG SSVTGIEMIS LENPGFSNMT
QAARVGISGL CANVGNARKL ISIHESHGAR VLTITSRRSP ASARRKARLR YLPLVDPRSL
EVQARTILPS NPVLFDNVNG ASPHVCLTMM YNFEVSSAVY DGDVVLDLGT GPEAKILELI
PPTSPVTCVD IRPTAQPSGC WNVRTTFLEL DYLSDGWITG IRGDIVTCML SLGAAAAGKS
MTFDAAFQQL VKVLTKSTAN VLLIQVNCPT DVIRTIKGYL EIDQTNKRYR FPKFGRDEPY
SDMDSLERIC RAAWPNCSIT WVPLSYDLRW TKLALLESTT LSSASVRIAE LMYKYMPVMR
IDIHGLPMEK QGNFIVGQNC SLTIPGFNAQ DVFNCYFNSA LAFSTEDVNS AMIPQVTAQF
DANKGEWSLD MVFSDAGIYT MQALVGSNAN PVSLGSFVVD SPDVDITDAW PAQLDFTIAG
TDVDITVNPY YRLMAFVRID GQWQIANPDK FQFFSSSTGT LVMNVKLDIA DRYLLYYIRD
VQSRDVGFYI QHPLQLLNTI TLPTNEDLFL SAPDMREWAV KESGNTICIL NSQGFVPPQD
WDVLTDTISW SPSLPTYVVP PGDYTLTPL
