ID A0A023PHM4_9PARA Unreviewed; 2233 AA. AC A0A023PHM4; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 17-FEB-2016, entry version 15. 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}; 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 parainfluenza virus 3. OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Mononegavirales; Paramyxoviridae; Paramyxovirinae; Respirovirus. OX NCBI_TaxID=11216 {ECO:0000313|EMBL:AHX22431.1}; RN [1] {ECO:0000313|EMBL:AHX22431.1} RP NUCLEOTIDE SEQUENCE. 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: Displays RNA-directed RNA polymerase, mRNA guanylyl CC transferase, mRNA (guanine-N(7)-)-methyltransferase and poly(A) CC synthetase activities. The viral mRNA guanylyl transferase CC displays a different biochemical reaction than the cellular CC enzyme. The template is composed of the viral RNA tightly CC encapsidated by the nucleoprotein (N). Functions either as CC transcriptase or as replicase. {ECO:0000256|PIRNR:PIRNR000830}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|SAAS:SAAS00503439}. 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|SAAS:SAAS00503447}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|PIRNR:PIRNR000830}. Host CC cytoplasm {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 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:InterPro. DR GO; GO:0003968; F:RNA-directed 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 Host cytoplasm {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00496142}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR000830, KW ECO:0000256|SAAS:SAAS00503413}; 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:SAAS00496152}. 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 //