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UniProtKB/Swiss-Prot entry P11079

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LMBD2_REOVD
Primary accession number P11079
Secondary accession number A4ZY21
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 22, 2008 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 57)
Name and origin of the protein
Protein name Outer capsid protein lambda-2
Synonyms Lambda2
Lambda2(Cap)
Includes mRNA guanylyltransferase
     (EC 2.7.7.50)
mRNA (guanine-N(7)-)-methyltransferase
     (EC 2.1.1.56)
Gene name
Name: L2
From
Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3) [TaxID: 10886] 
Taxonomy Viruses; dsRNA viruses; Reoviridae; Orthoreovirus.
Virus host Mammalia [TaxID: 40674]
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2824487 [NCBI, ExPASy, EBI, Israel, Japan]
Seliger L.S., Zheng K., Shatkin A.J.;
"Complete nucleotide sequence of reovirus L2 gene and deduced amino acid sequence of viral mRNA guanylyltransferase.";
J. Biol. Chem. 262:16289-16293(1987).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC RNA], SEQUENCE REVISION TO 609, CHARACTERIZATION OF GUANYLYLTRANSFERASE ACTIVITY, AND MUTAGENESIS OF LYS-44; LYS-89; LYS-94; LYS-171; LYS-190; LYS-197 AND LYS-226.
DOI=10.1074/jbc.275.4.2804; PubMed=10644745 [NCBI, ExPASy, EBI, Israel, Japan]
Luongo C.L., Reinisch K.M., Harrison S.C., Nibert M.L.;
"Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2.";
J. Biol. Chem. 275:2804-2810(2000).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Infectious clone;
PubMed=18005692 [NCBI, ExPASy, EBI, Israel, Japan]
Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M., Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D., Wilson G.J., Chappell J.D., Dermody T.S.;
"A plasmid-based reverse genetics system for animal double-stranded RNA viruses.";
Cell Host Microbe 1:147-157(2007).
[4]
 X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
STRAIN=Reassortant F18;
DOI=10.1038/35010041; PubMed=10801118 [NCBI, ExPASy, EBI, Israel, Japan]
Reinisch K.M., Nibert M.L., Harrison S.C.;
"Structure of the reovirus core at 3.6 A resolution.";
Nature 404:960-967(2000).
[5]
 STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS).
DOI=10.1016/j.str.2005.07.012; PubMed=16216585 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L., Baker T.S.;
"Features of reovirus outer capsid protein mu1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom resolution.";
Structure 13:1545-1557(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J03488; AAA47253.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
EF494436; ABP48914.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28471; RMXRR3.
3D structure databases
PDB
1EJ6; X-ray; 3.60 A; A=1-1289.[ExPASy / RCSB / EBI]
2CSE; EM; 7.00 A; U=1-1289.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EJ6; -.
2CSE; -.
ModBase P11079.
Ontologies
GO
GO:0019013; Cellular component: viral nucleocapsid (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004482; Molecular function: mRNA (guanine-N7-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0004484; Molecular function: mRNA guanylyltransferase activity (inferred from electronic annotation from EC).
GO:0005198; Molecular function: structural molecule activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006370; Biological process: mRNA capping (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR010311; Reovirus_L2.
Graphical view of domain structure.
Pfam PF06016; Reovirus_L2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000845; Reovirus_L2; 1.
Other
ProtoNet P11079.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Capsid protein; Complete proteome; Core protein; Methyltransferase; mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; S-adenosyl-L-methionine; Transferase; Virion.
Features
SEVIEWER logo Feature table viewer
KeyFrom    To Length Description FTId
CHAIN   1   1289  1289     Outer capsid protein lambda-2. PRO_0000222741
NP_BIND   893    900  8     ATP (Potential). 
COMPBIAS   181    184  4     Poly-Asp. 
COMPBIAS   894    897  4     Poly-Ala. 
SITE   190    190  1     Involved in formation of the phosphoamide bond. 
MUTAGEN   44     44        K->A: Almost no effect on autoguanylylation activity. 
MUTAGEN   89     89        K->A: Almost no effect on autoguanylylation activity. 
MUTAGEN   94     94        K->A: Almost no effect on autoguanylylation activity. 
MUTAGEN   171    171        K->A: Almost complete loss of autoguanylylation activity. 
MUTAGEN   190    190        K->A: Complete loss of autoguanylylation activity. 
MUTAGEN   197    197        K->A: 90% loss of autoguanylylation activity. 
MUTAGEN   226    226        K->A: No effect on autoguanylylation activity. 
CONFLICT   504    504        E -> G (in Ref. 2; ABP48914). 
CONFLICT   509    509        R -> G (in Ref. 2; ABP48914). 
CONFLICT   609    609        G -> F (in Ref. 1; AAA47253). 
STRAND   9     13  5      
HELIX   27     35  9      
STRAND   42     47  6      
TURN   49     51  3      
STRAND   54     59  6      
HELIX   70     73  4      
HELIX   79    100  22      
HELIX   103    106  4      
STRAND   109    111  3      
HELIX   113    123  11      
TURN   124    126  3      
HELIX   130    135  6      
HELIX   144    148  5      
TURN   154    156  3      
STRAND   157    160  4      
STRAND   163    167  5      
STRAND   171    174  4      
TURN   188    191  4      
STRAND   196    200  5      
HELIX   204    210  7      
HELIX   211    213  3      
STRAND   220    222  3      
STRAND   230    236  7      
HELIX   251    266  16      
STRAND   284    287  4      
HELIX   289    291  3      
HELIX   297    310  14      
STRAND   312    316  5      
HELIX   324    334  11      
STRAND   351    354  4      
HELIX   361    363  3      
STRAND   366    372  7      
STRAND   390    392  3      
STRAND   400    405  6      
HELIX   407    417  11      
STRAND   425    427  3      
STRAND   429    433  5      
STRAND   435    440  6      
HELIX   450    452  3      
TURN   458    461  4      
HELIX   463    475  13      
HELIX   481    493  13      
TURN   499    501  3      
STRAND   502    506  5      
STRAND   511    515  5      
TURN   520    523  4      
HELIX   530    535  6      
STRAND   545    551  7      
STRAND   555    558  4      
STRAND   571    576  6      
STRAND   583    585  3      
HELIX   588    605  18      
STRAND   606    618  13      
HELIX   621    630  10      
HELIX   632    634  3      
STRAND   635    648  14      
STRAND   651    659  9      
HELIX   668    688  21      
STRAND   702    713  12      
STRAND   717    719  3      
HELIX   722    734  13      
STRAND   740    746  7      
STRAND   749    758  10      
HELIX   760    767  8      
STRAND   769    775  7      
HELIX   778    781  4      
STRAND   793    795  3      
HELIX   803    818  16      
STRAND   825    829  5      
HELIX   835    838  4      
STRAND   846    852  7      
STRAND   861    863  3      
STRAND   865    870  6      
STRAND   874    876  3      
HELIX   878    880  3      
STRAND   884    888  5      
HELIX   892    898  7      
HELIX   903    915  13      
STRAND   920    925  6      
STRAND   930    932  3      
TURN   937    939  3      
STRAND   940    943  4      
TURN   944    947  4      
STRAND   948    951  4      
TURN   952    955  4      
STRAND   956    959  4      
HELIX   963    973  11      
STRAND   978    981  4      
HELIX   989    991  3      
HELIX   992    995  4      
TURN   996    998  3      
HELIX   1003   1013  11      
STRAND   1018   1022  5      
STRAND   1040   1046  7      
STRAND   1052   1064  13      
HELIX   1065   1067  3      
STRAND   1072   1080  9      
TURN   1082   1084  3      
STRAND   1086   1092  7      
STRAND   1097   1105  9      
TURN   1106   1109  4      
STRAND   1110   1120  11      
STRAND   1126   1129  4      
STRAND   1141   1147  7      
STRAND   1155   1159  5      
STRAND   1162   1165  4      
TURN   1168   1170  3      
STRAND   1171   1174  4      
STRAND   1182   1185  4      
HELIX   1189   1193  5      
STRAND   1196   1199  4      
STRAND   1202   1209  8      
STRAND   1211   1213  3      
HELIX   1215   1218  4      
STRAND   1228   1230  3      
STRAND   1233   1236  4      
STRAND   1238   1242  5      
STRAND   1245   1250  6      
STRAND   1269   1271  3      
STRAND   1277   1279  3      
STRAND   1284   1288  5      
Sequence information
Length: 1289 AA [This is the length of the unprocessed precursor] Molecular weight: 143976 Da [This is the MW of the unprocessed precursor] CRC64: D96FCEE31855F41C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MANVWGVRLA DSLSSPTIET RTRQYTLHDL CSDLDANPGR EPWKPLRNQR TNNIVAVQLF 

        70         80         90        100        110        120 
RPLQGLVLDT QLYGFPGAFD DWERFMREKL RVLKYEVLRI YPISNYSNEH VNVFVANALV 

       130        140        150        160        170        180 
GAFLSNQAFY DLLPLLIIND TMIGDLLGTG ASLSQFFQSH GDVLEVAAGR KYLQMENYSN 

       190        200        210        220        230        240 
DDDDPPLFAK DLSDYAKAFY SDTYEVLDRF FWTHDSSAGV LVHYDKPTNG HHYLLGTLTQ 

       250        260        270        280        290        300 
MVSAPPYIIN ATDAMLLESC LEQFSANVRA RPAQPVTRLD QCYHLRWGAQ YVGEDSLTYR 

       310        320        330        340        350        360 
LGVLSLLATN GYQLARPIPR QLTNRWLSSF VSQIMSDGVN ETPLWPQERY VQIAYDSPSV 

       370        380        390        400        410        420 
VDGATQYGYV RKNQLRLGMR ISALQSLSDT PSPVQWLPQY TIDQAAMDEG DLMVSRLTQL 

       430        440        450        460        470        480 
PLRPDYGNIW VGDALSYYVD YNRSHRVVLS SELPQLPDTY FDGDEQYGRS LFSLARKIGD 

       490        500        510        520        530        540 
RSLVKDTAVL KHAYQAIDPN TGKEYLRSRQ SVAYFGASAG HSGADQPLVI EPWIQGKISG 

       550        560        570        580        590        600 
VPPPSSVRQF GYDVARGAIV DLARPFPSGD YQFVYSDVDQ VVDGHDDLSI SSGLVESLLS 

       610        620        630        640        650        660 
SCMHATAPGG SFVVKINFPT RPVWHYIEQK ILPNITSYML IKPFVTNNVE LFFVAFGVHQ 

       670        680        690        700        710        720 
HSSLTWTSGV YFFLVDHFYR YETLSTISRQ LPSFGYVDDG SSVTGIETIS IENPGFSNMT 

       730        740        750        760        770        780 
QAARIGISGL CANVGNARKS IAIYESHGAR VLTITSRRSP ASARRKSRLR YLPLIDPRSL 

       790        800        810        820        830        840 
EVQARTILPA DPVLFENVSG ASPHVCLTMM YNFEVSSAVY DGDVVLDLGT GPEAKILELI 

       850        860        870        880        890        900 
PATSPVTCVD IRPTAQPSGC WNVRTTFLEL DYLSDGWITG VRGDIVTCML SLGAAAAGKS 

       910        920        930        940        950        960 
MTFDAAFQQL IKVLSKSTAN VVLVQVNCPT DVVRSIKGYL EIDSTNKRYR FPKFGRDEPY 

       970        980        990       1000       1010       1020 
SDMDALEKIC RTAWPNCSIT WVPLSYDLRW TRLALLESTT LSSASIRIAE LMYKYMPIMR 

      1030       1040       1050       1060       1070       1080 
IDIHGLPMEK RGNFIVGQNC SLVIPGFNAQ DVFNCYFNSA LAFSTEDVNA AMIPQVSAQF 

      1090       1100       1110       1120       1130       1140 
DATKGEWTLD MVFSDAGIYT MQALVGSNAN PVSLGSFVVD SPDVDITDAW PAQLDFTIAG 

      1150       1160       1170       1180       1190       1200 
TDVDITVNPY YRLMTFVRID GQWQIANPDK FQFFSSASGT LVMNVKLDIA DKYLLYYIRD 

      1210       1220       1230       1240       1250       1260 
VQSRDVGFYI QHPLQLLNTI TLPTNEDLFL SAPDMREWAV KESGNTICIL NSQGFVLPQD 

      1270       1280 
WDVLTDTISW SPSIPTYIVP PGDYTLTPL
P11079 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter,