ID   LMBD2_REOVJ             Reviewed;        1288 AA.
AC   Q91RA4;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 66.
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 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX   NCBI_TaxID=10885;
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).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the orthoreovirus lambda-2 protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF378005; AAK57509.1; -; mRNA.
DR   SMR; Q91RA4; -.
DR   Proteomes; UP000006370; 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   2: Evidence at transcript level;
KW   ATP-binding; Capsid protein; GTP-binding; Methyltransferase; mRNA capping;
KW   mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Outer capsid protein; S-adenosyl-L-methionine;
KW   Transferase; Virion.
FT   CHAIN           1..1288
FT                   /note="Outer capsid protein lambda-2"
FT                   /id="PRO_0000344999"
FT   BINDING         892..899
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   1288 AA;  143152 MW;  DD4BC3C1488AA137 CRC64;
     MANVWGVRLA DSLSSPTLES RNRSYTLHDF CSDLDASAGK EPWKALRNQR TSEIVAVRLF
     RPLQGLILDT HMYGFPGEFD AWEVFVKEKL RVLKYEVLRV YPISGYSNSH VNVFVANALV
     GAFLSNQAFY DLLPLLIIND TMINDLLGAG VSLAQFFQAH GDVLEVAAGR KYIQMNGYSN
     DDDDPPLFAK DLSDYAKAFY CESFEVLDRF FWTHDASAGV LVHYDKPTNG NHYLLGTLTQ
     MVSAPPFIIN ATDAMMLESC VEQFAANAAA RPAQPATRLD QCYHLRWGAQ YVGEDSLTYR
     LGVLSLLATN GYQLARPIPK QLTNRWLSSF VSQIMSEGAN ETPLWPQERY VQIAYDSPSV
     VDGAVQYGYV RKNQLRLGMR ISPIQSLSDV PAPVAWLPQY TIDQTALEDG DMVGHMSQLP
     LRPEYGSMWV GEALSYYVDY NQSHRVVAAK ELPQLPDTYF DGDEQYGRSL FSLARRIGDR
     SLIKDTAVLK HAYQAIDPST GREYLRAGQS VAYFGASAGH SGADQPLVIE PWLQGKISGV
     PSPASIRQFG YDVAKGAIVD LARPFPSGDY QFVYSDVDQV VDGHDDLSIS SNLVESILSS
     CMQATSPGGS FVAKINFPTR SIWYYIEQKI LPNITSYMII KPFVTNNVEV FFVAFGVHRQ
     SSLTWTSGVY FFLVDHFYRY ETLSAISRQL PSYGYVDDGS SVTGLEVISI ENPGFSTMTQ
     ASRVAISALC ANTGNSRKTI SIYESHGARV LMLVSRRSPA SAKRKARLRY LPLIDPRSLE
     VQSRTIMPST PVLFENSNGA SPHVCLTMMY NYEVSSAVYD GDVVLDLGTG PEAKILELIP
     PTSPATCVDI RPTAQPTGCW NVRTTFLQLD YLSDGWITGV RGDIVTCMLS LGAAAAGKSM
     TFDAAFQQFV RVIAQSAANV VLVQVNCPTD VIRSVRGYLE IDQTSKRYRF PKFGRDEPYS
     DMESLERICR ATWPNCSITW VPLSYDLRWT RLALLEAATL NSASIRIAEL MYKYMPVMRV
     DIHGLPMNKS GNFVVGQNCS LTIPGFNAQD TFNCYYNSAL AFSTEDVNAA MIPSVTATFD
     NAKNEWTLDM VFSDAGIYTM QAVVGVNASP IALGSFVVDS PDVDITDAWP AQLDFTIAGT
     DVDITVNPYY RLMAFVKIDG QWQIANPDKF QFFASATGTL TMNVKLDIAD KYLLYYIRDV
     QSREVGFYIQ HPLQLLNTIT LPTNEDLFLS APDMREWAVK ESGNTICILN SQGFIPPQDW
     DVLTDTISWS PSLPTYVVPP GDYTLTPL