ID   L_BDVV                  Reviewed;        1711 AA.
AC   P52639; Q912Z6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=RNA-directed RNA polymerase L;
DE            Short=Protein L;
DE            EC=2.7.7.48;
DE   AltName: Full=Large structural protein;
DE   AltName: Full=Replicase;
DE   AltName: Full=Transcriptase;
GN   Name=L;
OS   Borna disease virus (strain V) (BDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Bornaviridae; Borna disease virus.
OX   NCBI_TaxID=928296;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9352; Bradypodidae (three-fingered sloths).
OH   NCBI_TaxID=9925; Capra hircus (Goat).
OH   NCBI_TaxID=9850; Cervidae (Deer).
OH   NCBI_TaxID=109474; Crocidura leucodon (Bicoloured white-toothed shrew) (Celebes shrew).
OH   NCBI_TaxID=9788; Equidae (horses).
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=56798; Hexaprotodon liberiensis (Pygmy hippopotamus) (Choeropsis liberiensis).
OH   NCBI_TaxID=9844; Lama glama (Llama).
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
OH   NCBI_TaxID=8801; Struthio camelus (Common ostrich).
OH   NCBI_TaxID=9455; Varecia variegata (Black-and-white ruffed lemur) (Lemur variegatus).
OH   NCBI_TaxID=30538; Vicugna pacos (Alpaca) (Lama pacos).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8183914; DOI=10.1073/pnas.91.10.4362;
RA   Briese T., Schneemann A., Lewis A.J., Park Y.-S., Kim S., Ludwig H.,
RA   Lipkin W.I.;
RT   "Genomic organization of Borna disease virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:4362-4366(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=V/FR;
RX   PubMed=11602780; DOI=10.1099/0022-1317-82-11-2681;
RA   Pleschka S., Staeheli P., Kolodziejek J., Richt J.A., Nowotny N.,
RA   Schwemmle M.;
RT   "Conservation of coding potential and terminal sequences in four different
RT   isolates of Borna disease virus.";
RL   J. Gen. Virol. 82:2681-2690(2001).
RN   [3]
RP   INTERACTION WITH P PROTEIN.
RX   PubMed=10756058; DOI=10.1128/jvi.74.9.4425-4428.2000;
RA   Walker M.P., Jordan I., Briese T., Fischer N., Lipkin W.I.;
RT   "Expression and characterization of the Borna disease virus polymerase.";
RL   J. Virol. 74:4425-4428(2000).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12134049; DOI=10.1128/jvi.76.16.8460-8467.2002;
RA   Walker M.P., Lipkin W.I.;
RT   "Characterization of the nuclear localization signal of the borna disease
RT   virus polymerase.";
RL   J. Virol. 76:8460-8467(2002).
RN   [5]
RP   REVIEW.
RX   PubMed=11815287; DOI=10.2741/a789;
RA   Ikuta K., Ibrahim M.S., Kobayashi T., Tomonaga K.;
RT   "Borna disease virus and infection in humans.";
RL   Front. Biosci. 7:470-495(2002).
RN   [6]
RP   FUNCTION.
RX   PubMed=14557662; DOI=10.1128/jvi.77.21.11781-11789.2003;
RA   Schneider U., Naegele M., Staeheli P., Schwemmle M.;
RT   "Active borna disease virus polymerase complex requires a distinct
RT   nucleoprotein-to-phosphoprotein ratio but no viral X protein.";
RL   J. Virol. 77:11781-11789(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=18653450; DOI=10.1128/jvi.00639-08;
RA   Poenisch M., Wille S., Staeheli P., Schneider U.;
RT   "Polymerase read-through at the first transcription termination site
RT   contributes to regulation of borna disease virus gene expression.";
RL   J. Virol. 82:9537-9545(2008).
RN   [8]
RP   REVIEW.
RX   PubMed=22138959; DOI=10.1038/nrmicro2675;
RA   Decroly E., Ferron F., Lescar J., Canard B.;
RT   "Conventional and unconventional mechanisms for capping viral mRNA.";
RL   Nat. Rev. Microbiol. 10:51-65(2011).
CC   -!- FUNCTION: Displays RNA-directed RNA polymerase activity. The mRNA
CC       guanylyl transferase and mRNA (guanine-N(7)-)-methyltransferase
CC       activities are supposedly provided by cellular enzymes
CC       (PubMed:22138959). 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 three subgenomic RNAs, assuring their capping and
CC       polyadenylation by a stuttering mechanism. In replicase mode, the
CC       polymerase replicates the whole viral genome without recognizing the
CC       transcriptional signals. {ECO:0000303|PubMed:22138959,
CC       ECO:0000305|PubMed:14557662, ECO:0000305|PubMed:18653450}.
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:0000255|PROSITE-ProRule:PRU00539};
CC   -!- SUBUNIT: Interacts with the P protein. {ECO:0000269|PubMed:10756058}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host nucleus
CC       {ECO:0000269|PubMed:12134049}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Large structural protein;
CC         IsoId=P52639-1; Sequence=Displayed;
CC       Name=Matrix protein;
CC         IsoId=P0C795-1; Sequence=External;
CC       Name=Envelope glycoprotein p57 precursor;
CC         IsoId=P52638-1; Sequence=External;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA20228.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U04608; AAA20228.1; ALT_INIT; Genomic_RNA.
DR   EMBL; AJ311521; CAC70639.1; -; Genomic_RNA.
DR   RefSeq; NP_042024.3; NC_001607.1.
DR   SMR; P52639; -.
DR   GeneID; 26799167; -.
DR   KEGG; vg:26799167; -.
DR   Proteomes; UP000007804; Segment.
DR   Proteomes; UP000124375; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR026890; Mononeg_mRNAcap.
DR   InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR   Pfam; PF14318; Mononeg_mRNAcap; 1.
DR   Pfam; PF00946; Mononeg_RNA_pol; 1.
DR   PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Host nucleus; mRNA capping;
KW   mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..1711
FT                   /note="RNA-directed RNA polymerase L"
FT                   /id="PRO_0000079207"
FT   DOMAIN          543..715
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   MOTIF           844..852
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:12134049"
FT   VARIANT         1526
FT                   /note="A -> G"
SQ   SEQUENCE   1711 AA;  191734 MW;  554DF018E0E17877 CRC64;
     MSFHASLLRE EETPRPVAGI NRTDQSLKNP LLGTEVSFCL KSSSLPHHVR ALGQIKARNL
     ASCDYYLLFR QVVLPPEVYP IGVLIRAAEA ILTVIVSAWK LDHMTKTLYS SVRYALTNPR
     VRAQLELHIA YQRIVGQVSY SREADIGPKR LGNMSLQFIQ SLVIATIDTT SCLMTYNHFL
     AAADTAKSRC HLLIASVVQG ALWEQGSFLD HIINMIDIID SINLPHDDYF TIIKSIFPYS
     QGLVMGRHNV SVSSDFASVF AIPELCPQLD SLLKKLLQLD PVLLLMVSSV QKSWYFPEIR
     MVDGSREQLH KMRVELETPQ ALLSYGHTLL SIFRAEFIKG YVSKNAKWPP VHLLPGCDKS
     IKNARELGRW SPAFDRRWQL FEKVVILRIA DLDMDPDFND IVSDKAIISS RRDWVFEYNA
     AAFWKKYGER LERPPARSGP SRLVNALIDG RLDNIPALLE PFYRGAVEFE DRLTVLVPKE
     KELKVKGRFF SKQTLAIRIY QVVAEAALKN EVMPYLKTHS MTMSSTALTH LLNRLSHTIT
     KGDSFVINLD YSSWCNGFRP ELQAPICRQL DQMFNCGYFF RTGCTLPCFT TFIIQDRFNP
     PYSLSGEPVE DGVTCAVGTK TMGEGMRQKL WTILTSCWEI IALREINVTF NILGQGDNQT
     IIIHKSASQN NQLLAERALG ALYKHARLAG HNLKVEECWV SDCLYEYGKK LFFRGVPVPG
     CLKQLSRVTD STGELFPNLY SKLACLTSSC LSAAMADTSP WVALATGVCL YLIELYVELP
     PAIIQDESLL TTLCLVGPSI GGLPTPATLP SVFFRGMSDP LPFQLALLQT LIKTTGVTCS
     LVNRVVKLRI APYPDWLSLV TDPTSLNIAQ VYRPERQIRR WIEEAIATSS HSSRIATFFQ
     QPLTEMAQLL ARDLSTMMPL RPRDMSALFA LSNVAYGLSI IDLFQKSSTV VSASQAVHIE
     DVALESVRYK ESIIQGLLDT TEGYNMQPYL EGCTYLAAKQ LRRLTWGRDL VGVTMPFVAE
     QFHPHSSVGA KAELYLDAII YCPQETLRSH HLTTRGDQPL YLGSNTAVKV QRGEITGLAK
     SRAANLVKDT LVLHQWYKVR KVTDPHLNTL MARFLLEKGY TSDARPSIQG GTLTHRLPSR
     GDSRQGLTGY VNILSTWLRF SSDYLHSFSK SSDDYTIHFQ HVFTYGCLYA DSVIRSGGVI
     STPYLLSASC KTCFEKIDSE EFVLACEPQY RGAEWLISKP VTVPEQITDA EVEFDPCVSA
     SYCLGILIGK SFLVDIRASG HDIMEQRTWA NLERFSVSDM QKLPWSIVIR SLWRFLIGAR
     LLQFEKAGLI RMLYAATGPT FSFLMKVFQD SALLMDCAPL DRLSPRINFH SRGDLVAKLV
     LLPFINPGIV EIEVSGINSK YHAVSEANMD LYIAAAKSVG VKPTQFVEET NDFTARGHHH
     GCYSLSWSKS RNQSQVLKMV VRKLKLCVLY IYPTVDPAVA LDLCHLPALT IILVLGGDPA
     YYERLLEMDL CGAVSSRVDI PHSLAARTHR GFAVGPDAGP GVIRLDRLES VCYAHPCLEE
     LEFNAYLDSE LVDISDMCCL PLATPCKALF RPIYRSLQSF RLALMDNYSF VMDLIMIRGL
     DIRPHLEEFD ELLVVGQHIL GQPVLVEVVY YVGVVRKRPV LARHPWSADL KRITVGGRAP
     CPSAARLRDE DCQGSLLVGL PAGLTQLLII D
//