ID A0A023PHM4_9MONO Unreviewed; 2233 AA. AC A0A023PHM4; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 20-JUN-2018, entry version 32. DE RecName: Full=RNA-directed RNA polymerase L {ECO:0000256|PIRNR:PIRNR000830}; DE Short=Protein L {ECO:0000256|PIRNR:PIRNR000830}; DE AltName: Full=Large structural protein {ECO:0000256|PIRNR:PIRNR000830}; DE AltName: Full=Replicase {ECO:0000256|PIRNR:PIRNR000830}; DE AltName: Full=Transcriptase {ECO:0000256|PIRNR:PIRNR000830}; DE Includes: DE RecName: Full=RNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR000830}; DE EC=2.7.7.48 {ECO:0000256|PIRNR:PIRNR000830}; DE Includes: DE RecName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|PIRNR:PIRNR000830}; DE EC=2.1.1.56 {ECO:0000256|PIRNR:PIRNR000830}; DE Includes: DE RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000830}; DE EC=2.7.7.88 {ECO:0000256|PIRNR:PIRNR000830}; DE Includes: DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 {ECO:0000256|PIRNR:PIRNR000830}; DE EC=2.1.1.296 {ECO:0000256|PIRNR:PIRNR000830}; GN Name=L {ECO:0000313|EMBL:AHX22431.1}; GN ORFNames=AZ69_44294gpL {ECO:0000313|EMBL:AHX22519.1}, AZ69_44297gpL GN {ECO:0000313|EMBL:AHX22239.1}, AZ69_44304gpL GN {ECO:0000313|EMBL:AHX22071.1}, AZ69_44305gpL GN {ECO:0000313|EMBL:AHX22431.1}, AZ69_44306gpL GN {ECO:0000313|EMBL:AHX22303.1}; OS Human respirovirus 3. OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Mononegavirales; Paramyxoviridae; Respirovirus. OX NCBI_TaxID=11216 {ECO:0000313|EMBL:AHX22431.1, ECO:0000313|Proteomes:UP000117447}; RN [1] {ECO:0000313|Proteomes:UP000117447, ECO:0000313|Proteomes:UP000123088, ECO:0000313|Proteomes:UP000152372} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HPIV3/Homo sapiens/PER/FLA3621/2008 RC {ECO:0000313|EMBL:AHX22519.1}, HPIV3/Homo sapiens/PER/FLA4224/2008 RC {ECO:0000313|EMBL:AHX22239.1}, HPIV3/Homo sapiens/PER/FLA4571/2008 RC {ECO:0000313|EMBL:AHX22071.1}, HPIV3/Homo sapiens/PER/FLA4815/2008 RC {ECO:0000313|EMBL:AHX22431.1}, and HPIV3/Homo sapiens/PER/FLA4876/2008 RC {ECO:0000313|EMBL:AHX22303.1}; RA Wentworth D.E., Halpin R.A., Bera J., Lin X., Fedorova N., Tsitrin T., RA McLellan M., Stockwell T., Amedeo P., Bishop B., Gupta N., Hoover J., RA Katzel D., Schobel S., Shrivastava S., Garcia J., Laguna-Torres V.A., RA Leguia M., Benavides J.G., Halsey E.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the CC transcription of viral mRNAs, their capping and polyadenylation. CC The template is composed of the viral RNA tightly encapsidated by CC the nucleoprotein (N). The viral polymerase binds to the genomic CC RNA at the 3' leader promoter, and transcribes subsequently all CC viral mRNAs with a decreasing efficiency. The first gene is the CC most transcribed, and the last the least transcribed. The viral CC phosphoprotein acts as a processivity factor. Capping is CC concommitant with initiation of mRNA transcription. Indeed, a GDP CC polyribonucleotidyl transferase (PRNTase) adds the cap structure CC when the nascent RNA chain length has reached few nucleotides. CC Ribose 2'-O methylation of viral mRNA cap precedes and facilitates CC subsequent guanine-N-7 methylation, both activities being carried CC by the viral polymerase. Polyadenylation of mRNAs occur by a CC stuttering mechanism at a slipery stop site present at the end CC viral genes. After finishing transcription of a mRNA, the CC polymerase can resume transcription of the downstream gene. CC {ECO:0000256|PIRNR:PIRNR000830}. CC -!- CATALYTIC ACTIVITY: 5'-triphospho-mRNA + GDP = diphosphate + CC guanosine 5'-triphospho-mRNA. {ECO:0000256|PIRNR:PIRNR000830}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|PIRNR:PIRNR000830, CC ECO:0000256|SAAS:SAAS00361115}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S- CC adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. CC {ECO:0000256|PIRNR:PIRNR000830, ECO:0000256|SAAS:SAAS00847042}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl CC 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)- CC (ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)- CC methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine- CC ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]. CC {ECO:0000256|PIRNR:PIRNR000830}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm CC {ECO:0000256|PIRNR:PIRNR000830, ECO:0000256|SAAS:SAAS00847043}. CC Virion {ECO:0000256|PIRNR:PIRNR000830}. CC -!- SIMILARITY: Belongs to the paramyxovirus L protein family. CC {ECO:0000256|PIRNR:PIRNR000830}. 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; KJ672529; AHX22071.1; -; Viral_cRNA. DR EMBL; KJ672556; AHX22239.1; -; Viral_cRNA. DR EMBL; KJ672573; AHX22303.1; -; Viral_cRNA. DR EMBL; KJ672601; AHX22431.1; -; Viral_cRNA. DR EMBL; KJ672615; AHX22519.1; -; Viral_cRNA. DR Proteomes; UP000117447; Genome. DR Proteomes; UP000123088; Genome. DR Proteomes; UP000152372; Genome. DR Proteomes; UP000162202; Genome. DR Proteomes; UP000172444; Genome. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR InterPro; IPR026890; Mononeg_mRNAcap. DR InterPro; IPR014023; Mononeg_RNA_pol_cat. DR InterPro; IPR025786; Mononega_L_MeTrfase. DR InterPro; IPR016269; RNA-dir_pol_paramyxovirus. DR InterPro; IPR024352; RNA-pol_paramyxovirus_C_dom. DR Pfam; PF12803; G-7-MTase; 1. DR Pfam; PF14318; Mononeg_mRNAcap; 1. DR Pfam; PF00946; Mononeg_RNA_pol; 1. DR PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 1. DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 1. DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1. DR PROSITE; PS51590; SAM_MT_MNV_L; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00503432}; KW Complete proteome {ECO:0000313|Proteomes:UP000117447, KW ECO:0000313|Proteomes:UP000123088, ECO:0000313|Proteomes:UP000152372, KW ECO:0000313|Proteomes:UP000162202}; KW Host cytoplasm {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00847045}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00847038}; KW mRNA capping {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00503423}; KW mRNA processing {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00503435}; KW Multifunctional enzyme {ECO:0000256|SAAS:SAAS00503427}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00503450}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00503444}; KW RNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00503441, ECO:0000313|EMBL:AHX22431.1}; KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00503438}; KW Transferase {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00503460}; KW Viral RNA replication {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00503417}; KW Virion {ECO:0000256|PIRNR:PIRNR000830, ECO:0000256|SAAS:SAAS00847034}. FT DOMAIN 656 840 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50526}. FT DOMAIN 1775 1982 Mononegavirus-type SAM-dependent 2'-O- FT MTase. {ECO:0000259|PROSITE:PS51590}. SQ SEQUENCE 2233 AA; 255929 MW; 5E90C20316341280 CRC64; MDTESNNGTV SDILYPECHL NSPIVKGKIA QLHTIMSLPQ PYDMDDDSIL VITRQKIKLN KLDKRQRSIR RLKLILIEKV SDLGKYTFIR YPEMSKEMFK LHIPGINSKV TELLLKADRT YSQMTDGLRD LWINVLSKLA SKNDGSNYDL NEEINNISKV HTTYKSDKWY NPFKTWFTIK YDMRRLQKAR NEVTFNMGKD YNLLEDQKNL LLIHPELVLI LDKQNYNGYL ITPELVLMYC DVIEGRWNIS ACAKLDPKLQ SMYQKGNNLW EVIDKLFPIM GEKTFDVISL LEPLALSLIQ THDPVKQLRG AFLNHVLSEM ELIFESRESI KEFLSVDYID KILDIFDKST IDEIAEIFSF FRTFGHPPLE ASIAAEKVRK YMYIEKQLKF DTINKCHAIF CTIIINGYRE RHGGQWPPVT LPDHAHEFII NAYGSNSAIS YENAVDYYQS FIGIKFNKFI EPQLDEDLTI YMKDKALSPK KSNWDTVYPA SNLLYRTNAS NESRRLVEVF IADSKFDPHQ ILDYVESGDW LDDPEFNISY SLKEKEIKQE GRLFAKMTYK MRATQVLSET LLANNIGKFF QENGMVKGEI ELLKRLTTIS ISGVPRYNEV YNNSKSHTDD LKTYNKISNL NLSSNQKSKK FEFKSTDIYN DGYETVSCFL TTDLKKYCLN WRYESTALFG ETCNQIFGLN KLFNWLHPRL EGSTIYVGDP YCPPSDKEHI SLEDHPDSGF YVHNPRGGIE GFCQKLWTLI SISAIHLAAV RIGVRVTAMV QGDNQAIAVT TRVPNNYDYR VKKEIVYKDV VRFFDSLREV MDDLGHELKL NETIISSKMF IYSKRIYYDG RILPQALKAL SRCVFWSETV IDETRSASSN LATSFAKAIE NGYSPVLGYA CSIFKNIQQL YIALGMNINP TITQNIKDQY FRNPNWMQYA SLIPASVGGF NYMAMSRCFV RNIGDPSVAA LADIKRFIKA NLLDRSVLYR IMNQEPGESS FLDWASDPYS CNLPQSQNIT TMIKNITARN VLQDSPNPLL SGLFTNTMIE EDEELAEFLM DRKVILPRVA HDILDNSLTG IRNAIAGMLD TTKSLIRVGI NRGGLTYSLL RKISNYDLAQ YETLSRTLRL IVSDKIRYED MCSVDLAIAL RQKMWIHLSG GRMISGLETP DPLELLSGVV ITGSEHCKIC YSSDGTNPYT WMYLPGNIKI GSAETGISSL RVPYFGSVTD ERSEAQLGYI KNLSKPAKAA IRIAMIYTWA FGNDEISWME ASQIAQTRAN FTLDNLKILT PVATSTNLSH RLKDTATQMK FSSTSLIRVS RFITMSNDNM SIKEANETKD TNLIYQQIML TGLSVFEYLF RLKETTGHNP IVMHLHIEDE CCIKESFNDE HINPESTLEL IRYPESNEFI YDKDPLKDVD LSRLMVIKDH SYTIDMNYWD DTDIIHAISI CTAITIADTM SQLDRDNLKE IIVIANDDDI NSLITEFLTL DILVFLKTFG GLLVNQFAYT LYSLKIEGRD LIWDYIMRTL RDTSHSILKV LSNALSHPKV FKRFWDCGVL NPIYGPNTAS QDQIKLALSI CEYSLDLFMR EWLNGVSLEI YICDSDMEVA NDRKQAFISR HLSFVCCLAE IASFGPNLLN LTYLERLDLL KQYLELNIKE DPTLKYVQIS GLLIKSFPST VTYVRKTAIK YLRIRGISPP EVIDDWDPIE DENMLDNIVK SINDNCNKDN KGNKINNFWG LALKNYQVLK IRSITSDSDN NDGLDVSTGG LTLPQGGNYL SHQLRLFGIN STSCLKALEL SQILMKEVNK DKDRLFLGEG AGAMLACYDA TLGPAVNYYN SGLNITDVIG QRELKIFPSE VSLVGKKLGN VTQILNRVKV LFNGNPNSTW IGNMECESLI WSELNDKSIG LVHCDMEGAI GKSEETVLHE HYSVIRITYL IGDDDVVLVS KIIPTITPNW SRILYLYKLY WKDVSVISLK TSNPASTELY LVSKDAYCTI MEPSEVVLSK LKRLSLLEEN NLLKWIILSK KRNNEWLHHE IKEGERDYGV MRPYHMALQI FGFQINLNHL AKEFLSTPDL TNINNIIQSF QRTVKDVLFE WINITHDDKR HKLGGRYNIF PLKNKGKLRL LSRRLVLSWI SLSLSTRLLT GRFPDEKFEH RAQTGYVSLA DTDLESLKLL SKNIIKNYKE CIGSISYWFL TKEIKILMKL IGGAKLLGIP RQYKEPEEQL LENYNQHDEF DID //