LMBD2_REOVD
ID LMBD2_REOVD Reviewed; 1289 AA.
AC P11079; A4ZY21;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
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 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=2824487; DOI=10.1016/s0021-9258(18)49252-6;
RA Seliger L.S., Zheng K., Shatkin A.J.;
RT "Complete nucleotide sequence of reovirus L2 gene and deduced amino acid
RT sequence of viral mRNA guanylyltransferase.";
RL J. Biol. Chem. 262:16289-16293(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], SEQUENCE REVISION TO 609,
RP CHARACTERIZATION OF GUANYLYLTRANSFERASE ACTIVITY, AND MUTAGENESIS OF
RP LYS-44; LYS-89; LYS-94; LYS-171; LYS-190; LYS-197 AND LYS-226.
RX PubMed=10644745; DOI=10.1074/jbc.275.4.2804;
RA Luongo C.L., Reinisch K.M., Harrison S.C., Nibert M.L.;
RT "Identification of the guanylyltransferase region and active site in
RT reovirus mRNA capping protein lambda2.";
RL J. Biol. Chem. 275:2804-2810(2000).
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 X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
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).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS).
RX PubMed=16216585; DOI=10.1016/j.str.2005.07.012;
RA Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L.,
RA Baker T.S.;
RT "Features of reovirus outer capsid protein mu1 revealed by electron
RT cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom
RT resolution.";
RL Structure 13:1545-1557(2005).
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.
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; J03488; AAA47253.1; -; Genomic_RNA.
DR EMBL; EF494436; ABP48914.1; -; Genomic_RNA.
DR PIR; A28471; RMXRR3.
DR PDB; 1EJ6; X-ray; 3.60 A; A=1-1289.
DR PDB; 2CSE; EM; 7.00 A; U=1-1289.
DR PDB; 6ZTZ; EM; -; O=2-1289.
DR PDBsum; 1EJ6; -.
DR PDBsum; 2CSE; -.
DR PDBsum; 6ZTZ; -.
DR SMR; P11079; -.
DR EvolutionaryTrace; P11079; -.
DR Proteomes; UP000006373; Genome.
DR GO; GO:0019030; C:icosahedral viral capsid; IDA:CACAO.
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 3D-structure; ATP-binding; Capsid protein; GTP-binding; Methyltransferase;
KW mRNA capping; 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_0000222741"
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 MUTAGEN 44
FT /note="K->A: Almost no effect on autoguanylylation
FT activity."
FT /evidence="ECO:0000269|PubMed:10644745"
FT MUTAGEN 89
FT /note="K->A: Almost no effect on autoguanylylation
FT activity."
FT /evidence="ECO:0000269|PubMed:10644745"
FT MUTAGEN 94
FT /note="K->A: Almost no effect on autoguanylylation
FT activity."
FT /evidence="ECO:0000269|PubMed:10644745"
FT MUTAGEN 171
FT /note="K->A: Almost complete loss of autoguanylylation
FT activity."
FT /evidence="ECO:0000269|PubMed:10644745"
FT MUTAGEN 190
FT /note="K->A: Complete loss of autoguanylylation activity."
FT /evidence="ECO:0000269|PubMed:10644745"
FT MUTAGEN 197
FT /note="K->A: 90% loss of autoguanylylation activity."
FT /evidence="ECO:0000269|PubMed:10644745"
FT MUTAGEN 226
FT /note="K->A: No effect on autoguanylylation activity."
FT /evidence="ECO:0000269|PubMed:10644745"
FT CONFLICT 504
FT /note="E -> G (in Ref. 2; ABP48914)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="R -> G (in Ref. 2; ABP48914)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="G -> F (in Ref. 1; AAA47253)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 79..100
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 251..268
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 458..461
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 463..473
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 530..535
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 585..587
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 588..604
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 610..616
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 621..630
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 638..642
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 645..648
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 651..658
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 668..688
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 702..713
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 721..733
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 740..746
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 749..758
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 760..767
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 769..771
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 778..782
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 803..816
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 825..829
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 836..839
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 842..844
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 846..852
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 859..863
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 865..870
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 878..880
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 884..888
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 892..899
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 903..914
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 920..925
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 937..939
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 944..947
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 948..951
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 952..955
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 956..959
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 964..973
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 989..996
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 1004..1015
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1018..1022
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1040..1045
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1052..1057
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1060..1066
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1073..1075
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1078..1081
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 1082..1085
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1086..1092
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1097..1105
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT TURN 1106..1109
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1110..1120
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1126..1129
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1144..1147
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1153..1158
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1163..1165
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 1190..1193
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1196..1200
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1202..1205
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1211..1213
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT HELIX 1215..1218
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1224..1226
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1228..1231
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1238..1250
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1261..1263
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1269..1271
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1276..1279
FT /evidence="ECO:0007829|PDB:6ZTZ"
FT STRAND 1284..1288
FT /evidence="ECO:0007829|PDB:6ZTZ"
SQ SEQUENCE 1289 AA; 143976 MW; D96FCEE31855F41C CRC64;
MANVWGVRLA DSLSSPTIET RTRQYTLHDL CSDLDANPGR EPWKPLRNQR TNNIVAVQLF
RPLQGLVLDT QLYGFPGAFD DWERFMREKL RVLKYEVLRI YPISNYSNEH VNVFVANALV
GAFLSNQAFY DLLPLLIIND TMIGDLLGTG ASLSQFFQSH GDVLEVAAGR KYLQMENYSN
DDDDPPLFAK DLSDYAKAFY SDTYEVLDRF FWTHDSSAGV LVHYDKPTNG HHYLLGTLTQ
MVSAPPYIIN ATDAMLLESC LEQFSANVRA RPAQPVTRLD QCYHLRWGAQ YVGEDSLTYR
LGVLSLLATN GYQLARPIPR QLTNRWLSSF VSQIMSDGVN ETPLWPQERY VQIAYDSPSV
VDGATQYGYV RKNQLRLGMR ISALQSLSDT PSPVQWLPQY TIDQAAMDEG DLMVSRLTQL
PLRPDYGNIW VGDALSYYVD YNRSHRVVLS SELPQLPDTY FDGDEQYGRS LFSLARKIGD
RSLVKDTAVL KHAYQAIDPN TGKEYLRSRQ SVAYFGASAG HSGADQPLVI EPWIQGKISG
VPPPSSVRQF GYDVARGAIV DLARPFPSGD YQFVYSDVDQ VVDGHDDLSI SSGLVESLLS
SCMHATAPGG SFVVKINFPT RPVWHYIEQK ILPNITSYML IKPFVTNNVE LFFVAFGVHQ
HSSLTWTSGV YFFLVDHFYR YETLSTISRQ LPSFGYVDDG SSVTGIETIS IENPGFSNMT
QAARIGISGL CANVGNARKS IAIYESHGAR VLTITSRRSP ASARRKSRLR YLPLIDPRSL
EVQARTILPA DPVLFENVSG ASPHVCLTMM YNFEVSSAVY DGDVVLDLGT GPEAKILELI
PATSPVTCVD IRPTAQPSGC WNVRTTFLEL DYLSDGWITG VRGDIVTCML SLGAAAAGKS
MTFDAAFQQL IKVLSKSTAN VVLVQVNCPT DVVRSIKGYL EIDSTNKRYR FPKFGRDEPY
SDMDALEKIC RTAWPNCSIT WVPLSYDLRW TRLALLESTT LSSASIRIAE LMYKYMPIMR
IDIHGLPMEK RGNFIVGQNC SLVIPGFNAQ DVFNCYFNSA LAFSTEDVNA AMIPQVSAQF
DATKGEWTLD MVFSDAGIYT MQALVGSNAN PVSLGSFVVD SPDVDITDAW PAQLDFTIAG
TDVDITVNPY YRLMTFVRID GQWQIANPDK FQFFSSASGT LVMNVKLDIA DKYLLYYIRD
VQSRDVGFYI QHPLQLLNTI TLPTNEDLFL SAPDMREWAV KESGNTICIL NSQGFVLPQD
WDVLTDTISW SPSIPTYIVP PGDYTLTPL
