RDRP_REOVD
ID RDRP_REOVD Reviewed; 1267 AA.
AC P0CK31; A4ZY20; P17376; P17378; Q85665;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 29-SEP-2021, entry version 41.
DE RecName: Full=RNA-directed RNA polymerase lambda-3;
DE Short=Lambda3;
DE EC=2.7.7.48;
DE AltName: Full=Lambda3(Pol);
GN Name=L1;
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=2922925; DOI=10.1016/0042-6822(89)90055-x;
RA Wiener J.R., Joklik W.K.;
RT "The sequences of the reovirus serotype 1, 2, and 3 L1 genome segments and
RT analysis of the mode of divergence of the reovirus serotypes.";
RL Virology 169:194-203(1989).
RN [2]
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=12464184; DOI=10.1016/s0092-8674(02)01110-8;
RA Tao Y., Farsetta D.L., Nibert M.L., Harrison S.C.;
RT "RNA synthesis in a cage -- structural studies of reovirus polymerase
RT lambda3.";
RL Cell 111:733-745(2002).
CC -!- FUNCTION: RNA-directed RNA polymerase that is involved in transcription
CC and genome replication. Following infection, it catalyzes the synthesis
CC of fully conservative plus strands. After core assembly, which consists
CC in recruitment of one capped plus-strand for each genomic segments and
CC polymerase complexes, the polymerase switches mode and catalyzes the
CC synthesis of complementary minus-strands.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Found in the inner
CC capsid (12 copies).
CC -!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase
CC family. {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; M31058; AAA47255.1; -; Genomic_RNA.
DR EMBL; EF494435; ABP48913.1; -; Genomic_RNA.
DR PIR; C30121; MWXR33.
DR PDB; 1MUK; X-ray; 2.50 A; A=1-1267.
DR PDB; 1MWH; X-ray; 2.50 A; A=1-1267.
DR PDB; 1N1H; X-ray; 2.80 A; A=1-1267.
DR PDB; 1N35; X-ray; 2.50 A; A=1-1267.
DR PDB; 1N38; X-ray; 2.80 A; A=1-1267.
DR PDB; 1UON; EM; 7.60 A; A=1-1267.
DR PDBsum; 1MUK; -.
DR PDBsum; 1MWH; -.
DR PDBsum; 1N1H; -.
DR PDBsum; 1N35; -.
DR PDBsum; 1N38; -.
DR PDBsum; 1UON; -.
DR SMR; P0CK31; -.
DR DrugBank; DB03958; 7-methyl-guanosine-5'-triphosphate-5'-guanosine.
DR EvolutionaryTrace; P0CK31; -.
DR Proteomes; UP000006373; Genome.
DR Proteomes; UP000165799; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR012915; RdRP_5.
DR InterPro; IPR007097; RNA-dir_pol_reovirus.
DR Pfam; PF07925; RdRP_5; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Hydrolase; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-directed RNA polymerase;
KW Transferase; Viral RNA replication; Virion.
FT CHAIN 1..1267
FT /note="RNA-directed RNA polymerase lambda-3"
FT /id="PRO_0000222743"
FT DOMAIN 555..792
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT CONFLICT 267
FT /note="S -> A (in Ref. 2; ABP48913)"
FT /evidence="ECO:0000305"
FT CONFLICT 465..468
FT /note="ALRE -> DSAN (in Ref. 1; AAA47255)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="P -> T (in Ref. 2; ABP48913)"
FT /evidence="ECO:0000305"
FT CONFLICT 755..756
FT /note="ND -> KM (in Ref. 2; ABP48913)"
FT /evidence="ECO:0000305"
FT CONFLICT 926
FT /note="T -> P (in Ref. 2; ABP48913)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="S -> P (in Ref. 2; ABP48913)"
FT /evidence="ECO:0000305"
FT CONFLICT 1048
FT /note="S -> N (in Ref. 2; ABP48913)"
FT /evidence="ECO:0000305"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:1MUK"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1MUK"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:1N38"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 128..144
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:1MUK"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 226..242
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 247..262
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 307..315
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 341..352
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 359..369
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 422..438
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 445..453
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 463..471
FT /evidence="ECO:0007829|PDB:1MUK"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 506..510
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 523..528
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 533..552
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 568..575
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 580..587
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 589..592
FT /evidence="ECO:0007829|PDB:1MUK"
FT TURN 595..597
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 598..609
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 611..614
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 637..641
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 643..657
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 659..664
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 672..677
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 682..686
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 687..704
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 706..709
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 714..721
FT /evidence="ECO:0007829|PDB:1MUK"
FT TURN 725..727
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 735..740
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 750..765
FT /evidence="ECO:0007829|PDB:1MUK"
FT TURN 766..768
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 770..774
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 784..787
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 795..797
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 816..830
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 835..849
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 850..856
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 859..864
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 867..872
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 895..916
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 920..925
FT /evidence="ECO:0007829|PDB:1MUK"
FT TURN 926..928
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 929..931
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 933..939
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 942..949
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 966..978
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 982..998
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1009..1011
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1012..1022
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1028..1043
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1051..1056
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 1059..1066
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1086..1095
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1102..1106
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1107..1109
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1121..1133
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1138..1146
FT /evidence="ECO:0007829|PDB:1MUK"
FT TURN 1147..1149
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1152..1164
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1169..1173
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1174..1176
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1182..1184
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1189..1195
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 1196..1198
FT /evidence="ECO:0007829|PDB:1MUK"
FT TURN 1207..1209
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1213..1217
FT /evidence="ECO:0007829|PDB:1N1H"
FT HELIX 1218..1232
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 1233..1236
FT /evidence="ECO:0007829|PDB:1MUK"
FT STRAND 1238..1245
FT /evidence="ECO:0007829|PDB:1MUK"
FT HELIX 1248..1262
FT /evidence="ECO:0007829|PDB:1MUK"
SQ SEQUENCE 1267 AA; 142270 MW; FC9FD43CEF527148 CRC64;
MSSMILTQFG PFIESISGIT DQSNDVFEDA AKAFSMFTRS DVYKALDEIP FSDDAMLPIP
PTIYTKPSHD SYYYIDALNR VRRKTYQGPD DVYVPNCSIV ELLEPHETLT SYGRLSEAIE
NRAKDGDSQA RIATTYGRIA ESQARQIKAP LEKFVLALLV AEAGGSLYDP VLQKYDEIPD
LSHNCPLWCF REICRHISGP LPDRAPYLYL SAGVFWLMSP RMTSAIPPLL SDLVNLAILQ
QTAGLDPSLV KLGVQICLHA AASSSYSWFI LKTKSIFPQN TLHSMYESLE GGYCPNLEWL
EPRSDYKFMY MGVMPLSAKY ARSAPSNDKK ARELGEKYGL SSVVGELRKR TKTYVKHDFA
SVRYIRDAMA CTSGIFLVRT PTETVLQEYT QSPEIKVPIP QKDWTGPIGE IRILKDTTSS
IARYLYRTWY LAAARMAAQP RTWDPLFQAI MRSQYVTARG GSGAALRESL YAINVSLPDF
KGLPVKAATK IFQAAQLANL PFSHTSVAIL ADTSMGLRNQ VQRRPRSIMP LNVPQQQVSA
PHTLTADYIN YHMNLSPTSG SAVIEKVIPL GVYASSPPNQ SINIDISACD ASITWDFFLS
VIMAAIHEGV ASSSIGKPFM GVPASIVNDE SVVGVRAARP ISGMQNMIQH LSKLYKRGFS
YRVNDSFSPG NDFTHMTTTF PSGSTATSTE HTANNSTMME TFLTVWGPEH TDDPDVLRLM
KSLTIQRNYV CQGDDGLMII DGTTAGKVNS ETIQNDLELI SKYGEEFGWK YDIAYDGTAE
YLKLYFIFGC RIPNLSRHPI VGKERANSSA EEPWPAILDQ IMGVFFNGVH DGLQWQRWIR
YSWALCCAFS RQRTMIGESV GYLQYPMWSF VYWGLPLVKA FGSDPWIFSW YMPTGDLGMY
SWISLIRPLM TRWMVANGYV TDRCSTVFGN ADYRRCFNEL KLYQGYYMAQ LPRNPKKSGR
AASREVREQF TQALSDYLMQ NPELKSRVLR GRSEWEKYGA GIIHNPPSLF DVPHKWYQGA
QEAAIATREE LAEMDETLMR ARRHSYSSFS KLLEAYLLVK WRMCEAREPS VDLRLPLCAG
IDPLNSDPFL KMVSVGPMLQ STRKYFAQTL FMAKTVSGLD VNAIDSALLR LRTLGADKKA
LTAQLLMVGL QESEADALAG KIMLQDVNTV QLARVVNLAV PDTWMSLDFD SMFKHHVKLL
PKDGRHLNTD IPPRMGWLRA ILRFLGAGMV MTATGVAVDI YLEDIHGGGR SLGQRFMTWM
RQEGRSA