ID   L_PI2HT                 Reviewed;        2262 AA.
AC   P26676;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 53.
DE   RecName: Full=Large structural protein;
DE            Short=Protein L;
DE   AltName: Full=Transcriptase;
DE   AltName: Full=Replicase;
DE   Includes:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Includes:
DE     RecName: Full=mRNA (guanine-N(7)-)-methyltransferase;
DE              EC=2.1.1.56;
DE   Includes:
DE     RecName: Full=mRNA guanylyltransferase;
DE              EC=2.7.7.-;
GN   Name=L;
OS   Human parainfluenza 2 virus (strain Toshiba) (HPIV-2).
OC   Viruses; ssRNA negative-strand viruses; Mononegavirales;
OC   Paramyxoviridae; Paramyxovirinae; Rubulavirus.
OX   NCBI_TaxID=11214;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=91252221; PubMed=1645865; DOI=10.1093/nar/19.10.2739;
RA   Kawano M., Okamoto K., Bando H., Kondo K., Tsurudome M., Komada H.,
RA   Nishio M., Ito Y.;
RT   "Characterizations of the human parainfluenza type 2 virus gene
RT   encoding the L protein and the intergenic sequences.";
RL   Nucleic Acids Res. 19:2739-2746(1991).
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. The transcriptase synthesizes
CC       subsequently the subgenomic RNAs, assuring their capping and
CC       polyadenylation by a stuttering mechanism. The transcriptase
CC       stutters on a specific sequence, resulting on a cotranscriptional
CC       editing of the phosphoprotein (P) mRNA. The replicase mode is
CC       dependent on intracellular N protein concentration. In this mode,
CC       the polymerase replicates the whole viral genome without
CC       recognizing the transcriptional signals (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
CC       adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
CC   -!- SUBUNIT: Interacts with the P protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Virion (Potential). Cytoplasm (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the paramyxoviruses L protein family.
CC   -!- SIMILARITY: Contains 1 RdRp catalytic domain.
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DR   EMBL; X57559; CAA40788.1; -; Genomic_RNA.
DR   PIR; S16664; S16664.
DR   RefSeq; NP_598406.1; -.
DR   GeneID; 935189; -.
DR   DrugBank; DB00811; Ribavirin.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0006370; P:mRNA capping; IEA:UniProtKB-KW.
DR   GO; GO:0006410; P:transcription, RNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR016269; RNA-dir_RNA_pol_paramyxovir.
DR   InterPro; IPR014023; RNA_pol_cat.
DR   InterPro; IPR001016; RNA_pol_L_viral.
DR   Pfam; PF00946; Paramyx_RNA_pol; 1.
DR   PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 1.
DR   PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Methyltransferase; mRNA capping;
KW   mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA replication; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Transferase; Virion.
FT   CHAIN         1   2262       Large structural protein.
FT                                /FTId=PRO_0000142734.
FT   DOMAIN      661    844       RdRp catalytic.
FT   NP_BIND    1810   1819       ATP (Potential).
SQ   SEQUENCE   2262 AA;  256383 MW;  82468303F4453B48 CRC64;
     MAASSEILLP EVHLNSPIVK HKLIYYLLLG HFPHDLDISE ISPLHNNDWD QIAREESNLA
     ERLGVAKSEL IKRVPAFRAT RWRSHAAVLI WPSCIPFLVK FLPHSKLQPV EQWYKLINAS
     CNTISDSIDR CMENISIKLT GKNNLFSRSR GTAGAGKNSK ITLNDIQSIW ESNKWQPNVS
     LWLTIKYQMR QLIMHQSSRQ PTDLVHIVDT RSGLIVITPE LVICFDRLNS VLMYFTFEMT
     LMVSDMFEGR MNVTALCTIS HYLSPLGPRI DRLFSIVDEL AQLLGDTVYK VIASLESLVY
     GCLQLKDPVV ELAGSFHSFI TQEIIDILIG SKALDKDESI TVTTQLLDIF SNLSPDLIAE
     MLCLMRLWGH PTLTAAQVGK VRESMCAGKL LDFPTIMKTL AFFHTILING YRRKKNGMWP
     PLILPKNASK SLIEFQHDNA EISYEYTLKH WKEISLIEFR KCFDFDPGEE LSIFMKDKAI
     SAPRSDWMSV FRRSLIKQRH QRHHIPMPNP FNRRLLLNFL EDDSFDPVAE LRYVTGGEYL
     QDDTFCASYS LKEKEIKPDG RIFAKLTNRM RSCQVIAEAI LANHAGTLMK ENGVVLNQLS
     LTKSLLTMSQ IGIISEKAKR YTRDNISSQG FHTIKTDSKN KRKSKTASSY LTDPDDTFEL
     SACFITTDLA KYCLQWRYQT IIHFARTLNR MYGVPHLFEW IHLRLIRSTL YVGDPFNPPA
     ATDAFDLDKV LNGDIFIVSK GGIEGLCQKM WTMISISVII LSSAESKTRV MSMVQGDNQA
     IAVTTRVPRS LPSIQKKELA YAASKLFFER LRANNYGLGH QLKAQETIIS STFFIYSKRV
     FYQGRILTQA LKNASKLCLT ADVLGECTQA SCSNSATTIM RLTENGVEKD TCYKLNIYQS
     IRQLTYDLIF PQYSIPGETI SEIFLQHPRL ISRIVLLPSQ LGGLNYLACS RLFNRNIGDP
     LGTAVADLKR LIKCGALESW ILYNLLARKP GKGSWATLAA DPYSLNQEYL YPPTTILKRH
     TQNTLMEICR NPMLKGVFTD NAKEEENLLA KFLLDRDIVL PRVAHIIIDQ SSIGRKKQIQ
     GFFDTTRTIM RRSFEIKPLS TKKTLSVIEY NTNYLSYNYP VILNPLPIPG YLNYITDQTC
     SIDISRSLRK LSWSSLLNGR TLEGLETPDP IEVVNGFLIV GTGDCDFCMQ GDDKFTWFFL
     PMGIIIDGNP ETNPPIRVPY IGSRTEERRV ASMAYIKGAT HSLKAALRGA GVYIWAFGDT
     VVNWNDALDI ANTRVKISLE QLQTLTPLPT SANITHRLDD GATTLKFTPA SSYAFSSYTH
     ISNDQQYLEI DQRVVDSNII YQQLMITGLG IIETYHNPPI RTSTQEITLH LHTSSSCCVR
     SVDGCLICES NGEVPQITVP YTNTFVYDPD PLADYEIAHL DYLSYQAKIG STDYYSLTDK
     IDLLAHLTAK QMINSIIGLD ETVSIVNDAV ILSDYTNNWI SECSYTKIDL VFKLMAWNFL
     LELAFQMYYL RISSWTNIFD YTYMTLRRIP GTALNNIAAT ISHPKLLRRA MNLDIITPIH
     APYLASLDYV KLSIDAIQWG VKQVLADLSN GIDLEILILS EDSMEISDRA MNLIARKLTL
     LALVKGENYT FPKIKGMPPE EKCLVLTEYL AMCYQNTHHL DPDLQKYLYN LTNPKLTAFP
     SNNFYLTRKI LNQIRESDEG QYIITSYYES FEQLETDIIL HSTLTAPYDN SENSNKVRFI
     PFDIFPHPES LEKYPLPVDH DSQSAISTLI PGPPSHHVLR PLGVSSTAWY KGISYCRYLE
     TQKIQTGDHL YLAEGSGASM SLLELLFPGD TVYYNSLFSS GENPPQRNYA PLPTQFVQSV
     PYKLWQADLA DDSNLIKDFV PLWNGNGAVT DLSTKDAVAF IIHKVGAEKA SLVHIDLEST
     ANINQQTLSR SQIHSLIIAT TVLKRGGILI YKTSWLPFSR FSQLAGLLWC FFDRIHLIRS
     SYSDPHSHEV YLVCRLAADF RTIGFSAALV TATTLHNDGF TTIHPDVVCS YWQHHLENVG
     RVGKVIDEIL DGLATNFFAG DNGLILRCGG TPSSRKWLEI DQLASFDLVQ DALVTLITIH
     LKEIIEVQSS HTEDYTSLLF TPYNIGAAGK VRTIIKLILE RSLMYTVRNW LVLPSSIRDS
     VRQDLELGSF RLMSILSEQT FLKKTPTKKY LLDQLTRTYI STFFNSHSVL PLHRPYQKQI
     WKALGSVIYC SETVDIPLIK DIQIEDINDF EDIERGIDGE EL
//