ID   RDRP_CTFVL              Reviewed;        1435 AA.
AC   Q9DSQ0;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=RNA-directed RNA polymerase VP1;
DE            EC=2.7.7.48;
OS   Colorado tick fever virus (strain USA/Florio N-7180) (CTFV).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Coltivirus;
OC   Colorado tick fever coltivirus.
OX   NCBI_TaxID=648168;
OH   NCBI_TaxID=76772; Callospermophilus lateralis (Golden-mantled ground squirrel) (Spermophilus lateralis).
OH   NCBI_TaxID=34620; Dermacentor andersoni (Rocky mountain wood tick).
OH   NCBI_TaxID=34844; Erethizon dorsatum (North American porcupine).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=105147; Neotoma cinerea (Bushy-tailed woodrat).
OH   NCBI_TaxID=10042; Peromyscus maniculatus (North American deer mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Attoui H., Billoir F., De Micco P., De Lamballerie X.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-directed RNA polymerase involved in transcription and
CC       genome replication. Following infection, catalyzes the synthesis of
CC       fully conservative plus strands. After core assembly, which consists in
CC       recruitment of one capped plus-strand for each genomic segments and
CC       polymerase complexes, the polymerase switches mode and catalyzes the
CC       synthesis of complementary minus-strands (By similarity).
CC       {ECO:0000255|PROSITE-ProRule:PRU00539}.
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 VP4. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; AF133428; AAG34362.1; -; Genomic_RNA.
DR   RefSeq; NP_690891.1; NC_004181.1.
DR   PRIDE; Q9DSQ0; -.
DR   GeneID; 993309; -.
DR   KEGG; vg:993309; -.
DR   Proteomes; UP000001675; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0019079; P:viral genome replication; IEA:InterPro.
DR   InterPro; IPR007097; RNA-dir_pol_reovirus.
DR   PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT   CHAIN           1..1435
FT                   /note="RNA-directed RNA polymerase VP1"
FT                   /id="PRO_0000403189"
FT   DOMAIN          604..880
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   1435 AA;  163036 MW;  BA589A75A1B6D995 CRC64;
     MARRPSKEWR ERFNALSLKC KQLIHSSITN DFTTTDKAQQ STFYSSSGLM DVRKRLSISE
     SLEVFGSLID NWDLVQLVGT RAEPFVLNNP ASYLLVNQLL ALAGQAHSAA SMVFLNSLMY
     DDALDHVNLW PYEVERPIPQ ITREVLSPPP FSVNSYYLQR DIDVIKAKTK AAVYIENYRA
     GDVFAKKRSI SKGATFEERV YHGAVTMLQR MVKLRGSTIQ ECFVIAISSY RCSDCVRRMM
     ASESGTGAIH EMDHICIMRS NALRWLQAAF SDFPEFPFLM TRDGVKFASN CGAVSTQVPL
     LFFQTLEMMV LTMDGTLSST WEGWVCCEWY DRARVGLFSE MFDRRGVVAH LREAILRQSR
     LLRYQSRGLH LASVSNFPKR SVSADGLDDR IIEGLQKFNS KVCSFIQSWI FQIDLVDEPA
     RWLAVMIKTF ASALLYVMGA TSLSLEQSAQ GTLGIGDPIS FPRQEILLEG EWIAVDWYYP
     DPDLADMREM GMALVDNASP EYTDWEYGFF NVQTTNSAGN VKEVIEERRK QLVAEFGDQG
     KLLAKVENTR ILDAVQKITS TFQNPQDFCD SADNVRKAGE RHQVGRRPRV IQMVGTEGQL
     SAFVLHNVLR PAYKATRFTT SGKNSGDIRD MNIVLEISGE LGYKSSLDVK GMDSSTKPFQ
     TNLSLSCVFH RLRGEVLGYP AFFLGSTSSS KDNYVVTRTR YRDEHGGILV EEEYKLTYPQ
     YVLLLGAIHW TSPTRFTDGY FQEFVMTSRT VFRSGLLNTA DQHTFLGVIM YALLEKRLRQ
     RWYGKHGKEM REKIGQRREA LEEYEEHVKL LGSVLGDDQV AGAFCQGIVD EEVILRITRD
     LCDETKFLME RLGYECEPEI SEYSAEFLKQ KGVLGAPELF PERLLLFSSE RGDMAGSLPL
     DRVKIMLSMT DEKIGRARCP LPYASLMLFT SWVSGTASFS IGEEGRLLYR TGRNWKKVFA
     SKRAASVAWK DQFTSDGVFD VRWNGFGMFY KEWASANTKT ILLGCGLLWA CSDALGVPFP
     PLVQKDEILC PGTSVYTIPS NAMTHYLLWA TRRDRADAER MWRAVRDDLL RGDNDPLESY
     IEYVDKMFAE VGVIDIPFSA LHIYGVGMGF VAGVMPVPME VWYDFGLFGK VGGFGTWIAE
     LVFKDIRIDR EKYDLPRLSM WKNAANHSLP SEVRRASLYA RDTLHEKYGM VVPSAVLVAE
     RPGCKIDQAL FEVRRVGMED VRELEKVLDE LTRLNHLERK FTKRLAMGLF IVEKLTERRT
     GYGPAIASNG WGHIAAPYSF QARLLECLAF PMYNGFNYEA VRERVFVDGK LPGDPKLYLK
     IGRQALSYSE EAYNLVSASM GLSSRQAADM RDMILEGING LEEARFALNP RKTFLFDVSR
     RKGAGFFQTP HRRKTNQAYC EMMGMALLLM EPWKFSSGDW RMSFSHRLRA ILGRR