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 08-NOV-2023, entry version 46. 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; Spinareoviridae; Orthoreovirus; Mammalian 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-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; Hydrolase; Nucleotide-binding; KW Nucleotidyltransferase; 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_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 //