ID   RDRP_REOVJ              Reviewed;        1267 AA.
AC   P17377;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   27-MAR-2024, entry version 90.
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 2 (strain D5/Jones) (T2J) (Mammalian orthoreovirus 2).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Spinareoviridae; Orthoreovirus; Mammalian orthoreovirus.
OX   NCBI_TaxID=10885;
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).
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}.
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DR   EMBL; M31057; AAA47245.1; -; Genomic_RNA.
DR   PIR; B30121; MWXR32.
DR   SMR; P17377; -.
DR   Proteomes; UP000006370; Genome.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro.
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-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR   Gene3D; 3.90.1850.10; RNA-directed RNA polymerase lambda-3; 1.
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; DNA/RNA polymerases; 1.
DR   PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Nucleotide-binding; Nucleotidyltransferase;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..1267
FT                   /note="RNA-directed RNA polymerase lambda-3"
FT                   /id="PRO_0000222744"
FT   DOMAIN          555..792
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   1267 AA;  142289 MW;  B3F74EEBF257B604 CRC64;
     MSSTILTQFG PFIESISGII DQSNDIFEEA AKAFSAFTRS DVYKALDEIP FHDHATVHIP
     PTIYSKPSHD SYYYVDALNR VRRRTYQGDD DVYVPNCSIV ELLEPHETLT SYGRLSSAIE
     ARAKEGDPQA RIATTYARIS ESQARQIKAP LEKFVLALLV AESGDALYDP ILQKYDDVAD
     LTHNCPLWCF REICRHVSGP LPDRAPYLYL SAGVFWLMSP RMTSAIPPLL SDLVNLAILQ
     QTAGLDPSLV KMGVQVCLQA AASASYAWYV LKTKSVFPQN TLHSMYETLE GGFCPNLAWL
     EPRSDYKFMY MGATPLSGKY ARTAPSNETR ARQLGEKYGL STIIGDLRQR TRQFTKHDFA
     SVRYIRDAMA CTSGIFLVRT PTETVLQEYT QSPEIKVPIP QKDWTGPIGE IRVLKDTTSS
     IARYLYRTWY LAAARMASQP RTWDPLFQAI MRSQYVTARG GSGAALRESL YAINVSLPDF
     KGLPVKAATK IFQAAQLANL PFSHTSVAIL ADTSMGLRNQ VQRRPRSIMP LNVPQQQVSA
     PHTLTADYIN YHMNLSTTSG SAVIEKVIPL GVYASSPPNQ SINIDISACD ASITWDFFLS
     VIMAAIHEGV ASSSIGKPFM GVPASIVNDE SVVGVRAARP ISGMQNMVQH LSKLYKRGFS
     YRVNDSFSPG NDFTHMTTTF PSGSTATSTE HTANNSTMME TFLNVWGPEH TNDPDVLRLM
     RSLTIQRNYV CQGDDGLMII DGTTAGKVSS ETIQKMLELI SAYGEEFGWK YDIAYDGTAE
     YLKLYFIFGC RIPNLSRHPI VGKERANSSA EEPWPAILDQ VMGIFFNGVH DGLQWQRWIR
     YCSSLCCAFS RQRTMIGEEV RYLQYPMWSF VYWGLPPVKL FGSDPWIFSW YMPTGDLGMY
     SWISLIRPLM TRWMVANGYV SERCSSIFGN ADYRRCFNDI RLYQGYYMAR LPRNPKKSGR
     AAPRETREQF TQALSDYLMQ NPELKSRVLR GRSEWEKYGA GIIHNPPSLF DVPHKWYQGA
     QEAATATREE LSDMDDTLLR SRRHTYSSFS KLLEAYLRVR WRMCEAREPS VDLRLPLCAG
     IDPLNSDPFL KMVSVGPMLQ STRKYFAQTL FMAKTVSGLD VNAIDSALLR LRTLGADKKA
     LTAQLLMVGL QESEADALAG KIMLQDVNTV QLARVVNLAV PDTWMSLDFD SMFKHHVNLL
     PKDGRHLNTD IPPRMGWLRA ILRFLGAGVA MTATGVAVNV YLEDIDGGGR SLGQRFMTWM
     RQEGRSA
//