ID A0A023PHM4_9MONO Unreviewed; 2233 AA. AC A0A023PHM4; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 29-SEP-2021, entry version 53. 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=GTP phosphohydrolase {ECO:0000256|PIRNR:PIRNR000830}; DE EC=3.6.1.- {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 AltName: Full=PRNTase {ECO:0000256|PIRNR:PIRNR000830}; DE Includes: DE RecName: Full=mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000256|PIRNR:PIRNR000830}; DE Short=N1-2'-O-MTase {ECO:0000256|PIRNR:PIRNR000830}; DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR000830}; DE Includes: DE RecName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|PIRNR:PIRNR000830}; DE Short=G-N7-MTase {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; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae; OC Respirovirus. OX NCBI_TaxID=11216 {ECO:0000313|EMBL:AHX22431.1, ECO:0000313|Proteomes:UP000117447}; RN [1] {ECO:0000313|Proteomes:UP000117447, ECO:0000313|Proteomes:UP000123088} 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 replication of CC viral genomic RNA. The template is composed of the viral RNA tightly CC encapsidated by the nucleoprotein (N). The replicase mode is dependent CC on intracellular N protein concentration. In this mode, the polymerase CC replicates the whole viral genome without recognizing transcriptional CC signals, and the replicated genome is not caped or polyadenylated. CC {ECO:0000256|ARBA:ARBA00003132}. CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription CC of viral mRNAs, their capping and polyadenylation. The template is CC composed of the viral RNA tightly encapsidated by the nucleoprotein CC (N). The viral polymerase binds to the genomic RNA at the 3' leader CC promoter, and transcribes subsequently all viral mRNAs with a CC decreasing efficiency. The first gene is the most transcribed, and the CC last the least transcribed. The viral phosphoprotein acts as a CC processivity factor. Capping is concommitant with initiation of mRNA CC transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) CC adds the cap structure when the nascent RNA chain length has reached CC few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and CC facilitates subsequent guanine-N-7 methylation, both activities being CC carried by the viral polymerase. Polyadenylation of mRNAs occur by a CC stuttering mechanism at a slipery stop site present at the end viral CC genes. After finishing transcription of a mRNA, the polymerase can CC resume transcription of the downstream gene. CC {ECO:0000256|PIRNR:PIRNR000830}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000256|ARBA:ARBA00001270, CC ECO:0000256|PIRNR:PIRNR000830}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)- CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a CC 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)- CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482, CC ChEBI:CHEBI:156483; Evidence={ECO:0000256|ARBA:ARBA00023924, CC ECO:0000256|PIRNR:PIRNR000830}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl- CC adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl CC 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl- CC adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; CC Evidence={ECO:0000256|ARBA:ARBA00023946, CC ECO:0000256|PIRNR:PIRNR000830}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl- CC adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'- CC triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl- CC adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:156482, ChEBI:CHEBI:156484; CC Evidence={ECO:0000256|ARBA:ARBA00023913, CC ECO:0000256|PIRNR:PIRNR000830}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in CC mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl- CC adenylyl-cytidylyl-adenosine in mRNA + diphosphate; CC Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, CC ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; CC Evidence={ECO:0000256|PIRNR:PIRNR000830}; 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:0000256|PIRNR:PIRNR000830}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host CC cytoplasm {ECO:0000256|ARBA:ARBA00004192, CC ECO:0000256|PIRNR:PIRNR000830}. Virion {ECO:0000256|PIRNR:PIRNR000830}. CC -!- SIMILARITY: Belongs to the paramyxovirus L protein family. CC {ECO:0000256|ARBA:ARBA00007934, 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:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:RHEA. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR InterPro; IPR024352; L_methyltrans_paramyxo. DR InterPro; IPR039736; L_poly_C. 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 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|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000830}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, KW ECO:0000256|PIRNR:PIRNR000830}; Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, KW ECO:0000256|PIRNR:PIRNR000830}; KW mRNA capping {ECO:0000256|ARBA:ARBA00023042, KW ECO:0000256|PIRNR:PIRNR000830}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664, KW ECO:0000256|PIRNR:PIRNR000830}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR000830}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000256|PIRNR:PIRNR000830}; KW Reference proteome {ECO:0000313|Proteomes:UP000172444}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484, KW ECO:0000256|PIRNR:PIRNR000830}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, KW ECO:0000256|PIRNR:PIRNR000830}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000830}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953, KW ECO:0000256|PIRNR:PIRNR000830}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|PIRNR:PIRNR000830}. FT DOMAIN 656..840 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50526" FT DOMAIN 1775..1982 FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase" FT /evidence="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 //