ID   RDRP_ROTHK              Reviewed;        1088 AA.
AC   Q9QNB3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   29-SEP-2021, entry version 57.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein VP1;
OS   Rotavirus A (strain RVA/Human/Japan/KU/1995/G1P1A[8]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10952;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Taniguchi K.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-directed RNA polymerase that is involved in both
CC       transcription and genome replication. Together with VP3 capping enzyme,
CC       forms an enzyme complex positioned near the channels situated at each
CC       of the five-fold vertices of the core. Following infection, the
CC       outermost layer of the virus is lost, leaving a double-layered particle
CC       (DLP) made up of the core and VP6 shell. VP1 then catalyzes the
CC       transcription of fully conservative plus-strand genomic RNAs that are
CC       extruded through the DLP's channels into the cytoplasm where they
CC       function as mRNAs for translation of viral proteins. One copy of each
CC       of the viral (+)RNAs is also recruited during core assembly, together
CC       with newly synthesized polymerase complexes and VP2. The polymerase of
CC       these novo-formed particles catalyzes the synthesis of complementary
CC       minus-strands leading to dsRNA formation. To do so, the polymerase
CC       specifically recognizes and binds 4 bases 5'-UGUG-3' in the conserved
CC       3'-sequence of plus-strand RNA templates. VP2 presumably activates the
CC       autoinhibited VP1-RNA complex to coordinate packaging and genome
CC       replication. Once dsRNA synthesis is complete, the polymerase switches
CC       to the transcriptional mode, thus providing secondary transcription (By
CC       similarity). {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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Interacts with VP3 (Potential). Interacts with VP2; this
CC       interaction activates VP1. Interacts with NSP5; this interaction is
CC       probably necessary for the formation of functional virus factories.
CC       Interacts with NSP2; this interaction is weak (By similarity).
CC       {ECO:0000250, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Attached inside the
CC       inner capsid as a minor component. Also found in spherical cytoplasmic
CC       structures, called virus factories, that appear early after infection
CC       and are the site of viral replication and packaging (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; AB022765; BAA84962.1; -; mRNA.
DR   SMR; Q9QNB3; -.
DR   PRIDE; Q9QNB3; -.
DR   Proteomes; UP000001458; Genome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR   Gene3D; 1.10.10.1990; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042032; RNA-dir_pol_4-hel_dom.
DR   InterPro; IPR001795; RNA-dir_pol_luteovirus.
DR   InterPro; IPR007097; RNA-dir_pol_reovirus.
DR   InterPro; IPR022071; Rotavirus_VP1_C.
DR   Pfam; PF02123; RdRP_4; 1.
DR   Pfam; PF12289; Rotavirus_VP1; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE   2: Evidence at transcript level;
KW   Magnesium; Nucleotide-binding; Nucleotidyltransferase; RNA-binding;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..1088
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000368040"
FT   DOMAIN          501..687
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   1088 AA;  125017 MW;  214CA10B55825508 CRC64;
     MGKYNLILSE YLSFVYNSQS AVQIPIYYSS NSELETRCIE FHAKCVDNSK KGLSLKPLFE
     EYKDVTDNAT LLSILSYSYD KYNAVERKLV SYAKGKPLEA DLTANELDYE NNKITSELFQ
     SAEEYTDSLM DPAILTSLSS NLNAVMFWLE RHSNDIADAN KIYKRRLDLF TIVASTINKY
     GVPRHNEKYR YEYEVMKDKP YYLVTWANSS IEMLMSVFSH EDYLIAKELI VLSYSNRSTL
     AKLVSSPMSI LVALIDINGT FITNEELELE FSDKYVKAIV PDQTFDELQE MINNMKKIGL
     VDIPRMIQEW LIDCSLEKFT LMSKIYSWSF HVGFRKQKMI DAALDQLKTE YTKDVDDEMY
     NEYTMLIRDE IVKMLEIPVK HDDHLLRDSE LAGLLSMSSA SNGESRQIKF GRKTIFSTKK
     NMHVMDDIAH GKYTPGVIPP VNVDKPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKM
     LLYAKHTREY AEFYSQSNQL LSYGDVTRFL SSNSMVLYTD VSQWDSSQHN TQPFRKGIIM
     GLDMLSNMTN DPKVVQALNL YKQTQINLMD SYVQIPDGNV IKKNQYGAVA SGEKQTKAAN
     SIANLALIKT VLSRIANKYS FITKIIRVSG DDNYAVLQFN TDLTKQMIQD VSNDVRYIYF
     RMNAKVKALV STVGIEIAKR YLAGGKIFFR AGINLLNNEK RGQSTQWDQA AILYSNYIVN
     KLRGFETDRE FILTKIIQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD
     EVYIQRAFMS LSSQKSGIAD EIASSQTFKN YVSKLSDQLL VSKNVIVSKG IAVTEKAKLN
     SYAPIYLEKR RAQISALLTM LQKPVSFKSN KNTINEILRD IKPFFVTTED NLPIQYRKFM
     PTLPDNVQYV IQCIGSRTYQ IEDSGSKSSI SKLISKYSVY KPSIEELYKV ISLREQEIQL
     YLVSLGVPLV DASAYVASRI YSQDKYKILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI
     PFKGKIPAVT FILHLYAKLE IINYAIKNRA WISVFCNYPK SEMIKLWKKM WSITALRSPY
     TSANFFQD