ID   L_HENDV                 Reviewed;        2244 AA.
AC   O89344;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   25-NOV-2008, entry version 38.
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   Hendra virus.
OC   Viruses; ssRNA negative-strand viruses; Mononegavirales;
OC   Paramyxoviridae; Paramyxovirinae; Henipavirus.
OX   NCBI_TaxID=63330;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH   NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH   NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=20481636; PubMed=11024125;
RX   DOI=10.1128/JVI.74.21.9972-9979.2000;
RA   Wang L.-F., Yu M., Hansson E., Pritchard L.I., Shiell B.,
RA   Michalski W.P., Eaton B.T.;
RT   "The exceptionally large genome of Hendra virus: support for creation
RT   of a new genus within the family Paramyxoviridae.";
RL   J. Virol. 74:9972-9979(2000).
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; AF017149; AAC83194.2; -; Genomic_RNA.
DR   PIR; T08212; T08212.
DR   RefSeq; NP_047113.2; -.
DR   GeneID; 1446468; -.
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   2244       Large structural protein.
FT                                /FTId=PRO_0000236010.
FT   DOMAIN      715    899       RdRp catalytic.
FT   NP_BIND    1840   1849       ATP (Potential).
SQ   SEQUENCE   2244 AA;  257284 MW;  F4C29F354CEA2E2E CRC64;
     MAHELSISDI IYPECHLDSP IVSGKLISAI EYAQLRHNQP NGDKRLTENI KINLQGKRRS
     VYISRQSRLG NYIRDNIKNL KEFLHVSYPE CNKSLFSLKS PGMTSKLSNI MKKSFKAYNI
     VSRKIIEMLQ NITRNLITQD QKDEVLGIYE QDRLSNIGKY MSQSQWYECF LFWFTIKTEM
     RAVIKNSQKP KFRSDSCIIH MKDNNMEIVM NPNLVCIYKN DKDGKRCYYL TPEIVLMCCD
     VLEGRMMIET SIKSDIKYQS LITRSNALWT FIDSLFPIMG NRIYNIVSMI EPLVLALLQL
     KDEARILRGA FLHHCIKEIH QELIGCGFTD QKTRSIFIDD LLSVMNIDNI HLLAEFFSFF
     RTFGHPILEA KTAADKVREH MLADKVLEYG PIMKAHAVFC GTIINGYRDR HRGAWPPLYL
     PSHASKHIIR LKNSGESLTV DDCVKNWESF CGIQFDCFME LKLDSDLSMY MKDKALSPIK
     EEWDSVYPRE VLNYTPPRST EPRRLVDVFV NDENFDPYNM LEYVLTGDYL TDEQFNVSYS
     LKEKETKQAG RLFAKMTYKM RACQVIAEAL IASGVGKYFK ENGMVKDEHE LLKTLFQLSI
     SSVPRGNSQG RDSEFSNNTE KSLISLKRTT GRLLNNEVPC RMNIMSALID KNQSDQKKHN
     ILPNTRNRHK CDNTSQTFLD YHMEFSPYKS DRMDRTETSD FSKYDDGTGT KFDTVSAFLT
     TDLKKFCLNW RYESMAIFAE RLDEIYGLPG FFNWMHKRLE KSVIYVADPN CPPDIGKHIN
     LDDTPEDDIF IHSPKGGIEG YSQKTWTIAT IPFLFLSAYE TNTRIAAIVQ GDNESIAITQ
     KVHPNLPYKV KKEICARQAQ LYFDRLRMNL RALGLNLKAT ETIISTHLFV YSKKIHYDGA
     VLSQALKSMS RCCFWSETLV DETRSACSNI STTIAKAIEN GLSRNVGYCI NVLKVIQQLL
     ISTEFSINET LTADVTSPIS NNLDWLVTAS RIPAPIGGFN YLNLSRIFVR NIGDPVTASL
     ADLKRMIEHD LMTDKVLQKV MNQEPGDASF LDWASDPYSG NLPDSQSITK TIKNITARTI
     LRTSPNPMLK GLFHDKSFEE DLELATFLMD RRIILPRAAH EILDNSLTGA REEIAGLLDT
     TKGLIRSGLK KSGIQPKLVS RLSNHDYNQF LILNRLLSNK KRNDLISPKT CSVDLAKALR
     CHMWRDLALG RSIYGLEVPD ALEAMTGRYI TGSMECQLCD QGNTMYGWFF VPRDSQLDQV
     NKEHSSIRVP YVGSSTDERS DIKLGNVKRP TRALRSAIEL QLFIPGHTEI LKKVGMRLGT
     WLPRGVNIDI DVLKAITPVS TSNNLSHRLR DRSTQFKLPG SVLNRVSRYV NISNDNLDFR
     VEGEKVDTNL IYQQTMLLGL SVLEGKFRLR TETDDYNGIY HLHVRDNCCV KEVADIGGVN
     AELPVPEYTE VENNRLIYDP DPVSEIDCDR LSKQESKARE LDFPLWSTEE LHDVLAKTVA
     QTVLEIITKA DKDVLKQHLA IDSDDSINSL ITEFLMVDPE LFALYLGQSI SVKWAFEIHH
     RRPHGRHTMV DLLSDLISNT SKHTYKVLSN ALSHPRVFKR FVNCGLLLPT QGPYLHQQDF
     EKLSQNLLIT SYMNYLMNWC DFKKFPFLIA EQDEAVVELR EDIITSKHLC MIIDLYANHH
     KPPWIIDLNP QEKICVLRDF ISKCRHTDVS SRSWNITDLD FMVFYASLTY LRRGIIKQLR
     IRQVTEVIDT TTMLRDNILV ENPPIKTGVL DIRGCIIYNL EEILSMNTKS TSRKVFNLGS
     KLSVENHKYR RIGLNSSSCY KALNLSPLIQ RYLPAGSQRL FVGEGSGSMM LLYQQTLGCS
     ISFYNSGIDG DYIPGQRELR LFPSEYSIAE DDPSQSDKLK GLVVPLFNGR PETTWIGNLD
     SYEYIINRTA GRNIGLVHSD MESGIDKQVE EIMIEHSHLI SIAINVMIED GVLVSKIAFA
     PGFPISRLLN MYRSYFGLVL VCFPVYSNPE STEVYLICLQ KTIKTIIPPQ KVLDHSYLSD
     EINDQGITSV IFKIKNIQSK QFHEDLVKHY QVEQPFFVPS HITCDEKLLM QAGLKMNGPE
     ILKNEVGYDI GSDINTLRST IIILLNEAMN YFDDERSPSH HLEPFPVLEK TRVKTIMGRV
     TRKVTVYSLI KLKETKSPEL YNIKNYIRRK VLILDFRSHT MIKLLPKGMK ERREKSGFKE
     IWIFDLSNRE VKIWWKIIGY LSLV
//