ID   RDRP_REOVL              Reviewed;        1267 AA.
AC   P0CK32; A4ZY20; P17376; P17378; Q85665;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   08-NOV-2023, entry version 30.
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 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Spinareoviridae; Orthoreovirus; Mammalian orthoreovirus.
OX   NCBI_TaxID=10884;
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   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: 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; M24734; AAA47234.1; -; Genomic_RNA.
DR   PIR; A30121; MWXR31.
DR   PDB; 2CSE; EM; 7.00 A; 1=1-1267.
DR   PDBsum; 2CSE; -.
DR   SMR; P0CK32; -.
DR   EvolutionaryTrace; P0CK32; -.
DR   Proteomes; UP000007253; 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   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-directed RNA polymerase; Transferase;
KW   Viral RNA replication; Virion.
FT   CHAIN           1..1267
FT                   /note="RNA-directed RNA polymerase lambda-3"
FT                   /id="PRO_0000222745"
FT   DOMAIN          555..792
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   1267 AA;  142355 MW;  157EBFD4D664FCDB CRC64;
     MSSMILTQFR PFIESISGIT DQSNDVFEDA AKAFSMFTRS DVYKALDEIP FSDDAMLPIP
     PTIYTKPSHD SYYYIDALNR VRRKTYQGPD DVYVPNCSIV ELLEPHETLT SYGRLSEAIE
     NRAKDGDSQA RIATTYGRIA ESQARQIKAP LEKFVLALLV SEAGGSLYDP VLQKYDEIPD
     LSHNCPLWCF REICRHISGP LPDRAPYLYL SAGVFWLMSP RMTSAIPPLL SDLVNLAILQ
     QTAGLDPSLV KLGVQICLHA AASSSYAWFI LKTKSIFPQN TLHSMYESLE GGYCPNLEWL
     EPRSDYKFMY MGVMPLSTKY ARSAPSNDKK ARELGEKYGL SSVVSELRKR TKTYVKHDFA
     SVRYIRDAMA CTSGIFLVRT PTETVLQEYT QSPEIKVPIP QKDWTGPVGE IRILKDTTSS
     IARYLYRTWY LAAARMAAQP RTWDPLFQAI MRSQYVTARG GSGAALRESL YAINVSLPDF
     KGLPVKAATK IFQAAQLANL PFSHTSVAIL ADTSMGLRNQ VQRRPRSIMP LNVPQQQVSA
     PHTLTADYIN YHMNLSTTSG SAVIEKVIPL GVYASSPPNQ SINIDISACD ASITWDFFLS
     VIMAAIHEGV ASGSIGKPFM GVPASIVNDE SVVGVRAARP ISGMQNMIQH LSKLYKRGFS
     YRVNDSFSPG NDFTHMTTTF PSGSTATSTE HTANNSTMME TFLTVWGPEH TDDPDVLRLM
     KSLTIQRNYV CQGDDGLMII DGNTAGKVNS ETIQKMLELI SKYGEEFGWK YDIAYDGTAE
     YLKLYFIFGC RIPNLSRHPI VGKERANSSA EEPWPAILDQ IMGIFFNGVH DGLQWQRWIR
     YSWALCCAFS RQRTMIGESV GYLQYPMWSF VYWGLPLVKV FGSDPWIFSW YMPTGDLGMY
     SWISLIRPLM TRWMVANGYA TDRCSPVFGN ADYRRCFNEI KLYQGYYMAQ LPRNPTKSGR
     AAPREVREQF TQALSDYLMQ NPELKSRVLR GRSEWEKYGA GIIHNPPSLF DVPHKWYLGA
     QEAATATREE LAEMDETLMR ARRHSYSSFS KLLEAYLLVK WRMCEAREPS VDLRLPLCAG
     IDPLNSDPFL KMVSVGPMLQ STRKYFAQTL FMAKTVSGLD VNAIDSALLR LRTLGADKKA
     LTAQLLMVGL QESEADALAG KIMLQDVSTV QLARVVNLAV PDTWMSLDFD SMFKHHVKLL
     PKDGRHLNTD IPPRMGWLRA ILRFLGAGMV MTATGVAVDI YLEDIHGGGR ALGQRFMTWM
     RQEGRSA
//