ID   RDRP_THOGV              Reviewed;         710 AA.
AC   O41353;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   29-SEP-2021, entry version 76.
DE   RecName: Full=RNA-directed RNA polymerase catalytic subunit;
DE            EC=2.7.7.48;
DE   AltName: Full=RNA-directed RNA polymerase subunit P2;
GN   OrderedLocusNames=Segment 2;
OS   Thogoto virus (isolate SiAr 126) (Tho).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Thogotovirus.
OX   NCBI_TaxID=126796;
OH   NCBI_TaxID=34610; Amblyomma variegatum (Tropical bont tick).
OH   NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH   NCBI_TaxID=210652; Mungos mungo (Banded mongoose).
OH   NCBI_TaxID=34631; Rhipicephalus appendiculatus (Brown ear tick).
OH   NCBI_TaxID=6941; Rhipicephalus microplus (Cattle tick) (Boophilus microplus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9282786; DOI=10.1016/s0168-1702(97)00072-5;
RA   Leahy M.B., Dessens J.T., Weber F., Kochs G., Nuttall P.A.;
RT   "The fourth genus in the Orthomyxoviridae: sequence analyses of two Thogoto
RT   virus polymerase proteins and comparison with influenza viruses.";
RL   Virus Res. 50:215-224(1997).
CC   -!- FUNCTION: RNA-dependent RNA polymerase which is responsible for
CC       replication and transcription of virus RNA segments. The transcription
CC       of viral mRNAs occurs by a unique mechanism called cap-snatching. 5'
CC       methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides
CC       by PA. In turn, these short capped RNAs are used as primers by PB1 for
CC       transcription of viral mRNAs. During virus replication, PB1 initiates
CC       RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn
CC       serves as a template for the production of more vRNAs.
CC       {ECO:0000250|UniProtKB:P03431}.
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: RNA polymerase is composed of three subunits: PA, PB1 and PB2.
CC       {ECO:0000250|UniProtKB:P03431}.
CC   -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF004985; AAC25959.1; -; mRNA.
DR   RefSeq; YP_145794.1; NC_006495.1.
DR   SMR; O41353; -.
DR   GeneID; 5075733; -.
DR   KEGG; vg:5075733; -.
DR   Proteomes; UP000008973; Genome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR007099; RNA-dir_pol_NSvirus.
DR   InterPro; IPR001407; RNA_pol_PB1_influenza.
DR   Pfam; PF00602; Flu_PB1; 1.
DR   PIRSF; PIRSF000827; RdRPol_OMV; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1.
PE   2: Evidence at transcript level;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT   CHAIN           1..710
FT                   /note="RNA-directed RNA polymerase catalytic subunit"
FT                   /id="PRO_0000078778"
FT   DOMAIN          285..460
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   710 AA;  81285 MW;  F00BA397272E2F17 CRC64;
     MNLFTPRSEI NPTTTQELLY AYTGPAPVAY GTRTRAVLEN IIRPYQYFYK EPNVQRALDI
     KTGCKEPEDI NVEGPSSGFH TASVLKLADN FFRKYRPAME KLKYWILVKL PKLKYAELSK
     GRQTYSFIHK RNLPAPIALE ETVEFLEQNL RRKIGPTLLS YCQAIADVME LDETTYEGAR
     DPRPWDIQLE EIDSDEEDPL FRQVGREETY TIKFSREELW DQMRTLNTMC KHLERGRLNR
     RTIATPSMLI RGFVKIVEDA AKEILENVPT SGVPVGGEEK LAKLASKQTF HTAVTGELSG
     DQEKFNECLD PDAMRLMWTV FLRKLGCPDW IMELFNIPFM VFKSKLADMG EGLVYTKGKL
     TDRKPLGEMP SEFDDLVRNV VGNSISCRLG MFMGMYNLTS TLLALISIER EELTGSHVES
     SDDFIHFFNC KTHEEMFKQA ETLRLTLKLV GINMSPSKCI LISPAGIGEF NSKFHHRDFV
     GNVATELPAL VPNGTNPMTD LAMGLNVIKH SVNTGQMNLC TGALAMRIFN HAYKYAYMAL
     GVTRRTRFME ENAITPLLTN QGASPVHSFS TMHLDEVALR RHLGLLDEET LRRILNPNNP
     VTQKGDPSMF FRIENKMPQI MEDYSVPSCF KYTLSRNRTI QDKPHKALLN KEERYQRVTS
     IINKLFPEVL IQEASAPGTV RESLKRRLEL VVERSDLDEE RKKRILSRIF