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RNA-directed RNA polymerase (EC 2.7.7.48) (Protein VP1)

 T2CEB0_9REOV            Unreviewed;      1088 AA.
T2CEB0;
13-NOV-2013, integrated into UniProtKB/TrEMBL.
13-NOV-2013, sequence version 1.
05-DEC-2018, entry version 23.
RecName: Full=RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU363117};
EC=2.7.7.48 {ECO:0000256|RuleBase:RU363117};
AltName: Full=Protein VP1 {ECO:0000256|RuleBase:RU363117};
Name=VP1 {ECO:0000313|EMBL:AGV31652.1};
ORFNames=L312_42259gpVP1 {ECO:0000313|EMBL:AGV31652.1},
L312_46549gpVP1a {ECO:0000313|EMBL:AHZ91931.1},
L312_46699gpVP1 {ECO:0000313|EMBL:AHZ33398.1},
L312_49832gpVP1 {ECO:0000313|EMBL:AHZ91313.1},
L312_49833gpVP1 {ECO:0000313|EMBL:AHZ91844.1},
L312_49835gpVP1 {ECO:0000313|EMBL:AHZ91881.1},
L312_49836gpVP1 {ECO:0000313|EMBL:AHZ91468.1},
L312_49837gpVP1 {ECO:0000313|EMBL:AHZ92056.1},
L312_49839gpVP1 {ECO:0000313|EMBL:AHZ91070.1},
L312_49840gpVP1 {ECO:0000313|EMBL:AHZ91944.1},
NC78_46709gpVP1 {ECO:0000313|EMBL:AKA40211.1},
NC78_46724gpVP1 {ECO:0000313|EMBL:AKA40421.1};
Rotavirus A.
Viruses; dsRNA viruses; Reoviridae; Sedoreovirinae; Rotavirus.
NCBI_TaxID=28875 {ECO:0000313|EMBL:AGV31652.1, ECO:0000313|Proteomes:UP000157540};
[1] {ECO:0000313|EMBL:AGV31652.1, ECO:0000313|Proteomes:UP000157540}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RVA/Human-wt/ZAF/MRC-DPRU1262/2004/G1P[8]
{ECO:0000313|EMBL:AGV31652.1};
Wentworth D.E., Halpin R.A., Akopov A., Fedorova N., Tsitrin T.,
McLellan M., Stockwell T., Amedeo P., Appalla L., Bishop B.,
Edworthy P., Gupta N., Hoover J., Katzel D., Schobel S.,
Shrivastava S., Thovarai V., Wang S., Nyaga M.M., Magagula N.B.,
Peenze I., Seheri M.L., Mphahlele J.;
Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Proteomes:UP000157540}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Huebschen J.;
Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|Proteomes:UP000099318, ECO:0000313|Proteomes:UP000120182, ECO:0000313|Proteomes:UP000127505}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RVA/Human-wt/ZAF/MRC-DPRU1224/2004/G1P[8]
{ECO:0000313|EMBL:AHZ91070.1},
RVA/Human-wt/ZAF/MRC-DPRU1233/2004/G1P[8]
{ECO:0000313|EMBL:AHZ91931.1},
RVA/Human-wt/ZAF/MRC-DPRU1275/2004/G1P[8]
{ECO:0000313|EMBL:AHZ91468.1},
RVA/Human-wt/ZAF/MRC-DPRU1277/2004/G1P[8]
{ECO:0000313|EMBL:AHZ91944.1},
RVA/Human-wt/ZAF/MRC-DPRU1280-04/2004/G1P[8]
{ECO:0000313|EMBL:AHZ92056.1},
RVA/Human-wt/ZAF/MRC-DPRU1283/2004/G1P[8]
{ECO:0000313|EMBL:AHZ91881.1},
RVA/Human-wt/ZAF/MRC-DPRU1285/2004/G1P[8]
{ECO:0000313|EMBL:AHZ91313.1},
RVA/Human-wt/ZAF/MRC-DPRU1299/2004/G1P[8]
{ECO:0000313|EMBL:AHZ91844.1}, and
RVA/Human-wt/ZAF/MRC-DPRU426/2004/G1P[8]
{ECO:0000313|EMBL:AHZ33398.1};
Wentworth D.E., Halpin R.A., Stucker K.M., Akopov A., Fedorova N.,
Tsitrin T., Puri V., Stockwell T., Amedeo P., Bishop B., Gupta N.,
Hoover J., Katzel D., Schobel S., Shrivastava S., Nyaga M.M.,
Magagula N.B., Peenze I., Seheri M.L., Mphahlele J., Steele A.D.,
Mwenda M.J.;
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|Proteomes:UP000157540}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Chooi Y.-H.;
Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:AKA40211.1, ECO:0000313|Proteomes:UP000124710, ECO:0000313|Proteomes:UP000157540}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RVA/Human-wt/ZAF/MRC-DPRU1192/2002/G1P[8]
{ECO:0000313|EMBL:AKA40211.1}, and
RVA/Human-wt/ZAF/MRC-DPRU1262/2004/G1P[8]
{ECO:0000313|EMBL:AKA40421.1};
Das S.R., Halpin R.A., Stucker K.M., Akopov A., Fedorova N., Puri V.,
Stockwell T., Amedeo P., Katzel D., Schobel S., Shrivastava S.,
Nyaga M.M., Magagula N.B., Peenze I., Seheri M.L., Wentworth D.E.,
Mphahlele J.;
Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: RNA-directed RNA polymerase that is involved in both
transcription and genome replication. Together with VP3 capping
enzyme, forms an enzyme complex positioned near the channels
situated at each of the five-fold vertices of the core. Following
infection, the outermost layer of the virus is lost, leaving a
double-layered particle (DLP) made up of the core and VP6 shell.
VP1 then catalyzes the transcription of fully conservative plus-
strand genomic RNAs that are extruded through the DLP's channels
into the cytoplasm where they function as mRNAs for translation of
viral proteins. One copy of each of the viral (+)RNAs is also
recruited during core assembly, together with newly synthesized
polymerase complexes and VP2. The polymerase of these novo-formed
particles catalyzes the synthesis of complementary minus-strands
leading to dsRNA formation. To do so, the polymerase specifically
recognizes and binds 4 bases 5'-UGUG-3' in the conserved 3'-
sequence of plus-strand RNA templates. VP2 presumably activates
the autoinhibited VP1-RNA complex to coordinate packaging and
genome replication. Once dsRNA synthesis is complete, the
polymerase switches to the transcriptional mode, thus providing
secondary transcription. {ECO:0000256|RuleBase:RU363117}.
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
ChEBI:CHEBI:83400; EC=2.7.7.48;
Evidence={ECO:0000256|RuleBase:RU363117};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|RuleBase:RU363117};
-!- SUBUNIT: Interacts with VP3 (Potential). Interacts with VP2; this
interaction activates VP1. Interacts with NSP5; this interaction
is probably necessary for the formation of functional virus
factories. Interacts with NSP2; this interaction is weak.
{ECO:0000256|RuleBase:RU363117}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000256|RuleBase:RU363117}.
Note=Attached inside the inner capsid as a minor component. Also
found in spherical cytoplasmic structures, called virus factories,
that appear early after infection and are the site of viral
replication and packaging. {ECO:0000256|RuleBase:RU363117}.
-!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase
family. {ECO:0000256|RuleBase:RU363117}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; KF636223; AGV31652.1; -; Genomic_RNA.
EMBL; KJ752563; AHZ33398.1; -; Genomic_RNA.
EMBL; KJ752869; AHZ91070.1; -; Genomic_RNA.
EMBL; KJ753093; AHZ91313.1; -; Genomic_RNA.
EMBL; KJ753237; AHZ91468.1; -; Genomic_RNA.
EMBL; KJ753582; AHZ91844.1; -; Genomic_RNA.
EMBL; KJ753616; AHZ91881.1; -; Genomic_RNA.
EMBL; KJ753662; AHZ91931.1; -; Genomic_RNA.
EMBL; KJ753674; AHZ91944.1; -; Genomic_RNA.
EMBL; KJ753776; AHZ92056.1; -; Genomic_RNA.
EMBL; KP752549; AKA40211.1; -; Genomic_RNA.
EMBL; KP752742; AKA40421.1; -; Genomic_RNA.
Proteomes; UP000099318; Genome.
Proteomes; UP000120182; Genome.
Proteomes; UP000124710; Genome.
Proteomes; UP000127505; Genome.
Proteomes; UP000134932; Genome.
Proteomes; UP000152843; Genome.
Proteomes; UP000157540; Genome.
Proteomes; UP000161236; Genome.
Proteomes; UP000165810; Genome.
Proteomes; UP000170589; Genome.
Proteomes; UP000170907; Genome.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019079; P:viral genome replication; IEA:InterPro.
InterPro; IPR001795; RNA-dir_pol_luteovirus.
InterPro; IPR007097; RNA-dir_pol_reovirus.
InterPro; IPR022071; Rotavirus_VP1_C.
Pfam; PF02123; RdRP_4; 1.
Pfam; PF12289; Rotavirus_VP1; 1.
PROSITE; PS50523; RDRP_DSRNA_REO; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000099318,
ECO:0000313|Proteomes:UP000120182, ECO:0000313|Proteomes:UP000124710,
ECO:0000313|Proteomes:UP000127505};
Magnesium {ECO:0000256|RuleBase:RU363117};
Nucleotide-binding {ECO:0000256|RuleBase:RU363117};
Nucleotidyltransferase {ECO:0000256|RuleBase:RU363117,
ECO:0000313|EMBL:AGV31652.1};
RNA-binding {ECO:0000256|RuleBase:RU363117};
RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU363117,
ECO:0000313|EMBL:AGV31652.1};
Transferase {ECO:0000256|RuleBase:RU363117,
ECO:0000313|EMBL:AGV31652.1};
Viral RNA replication {ECO:0000256|RuleBase:RU363117};
Virion {ECO:0000256|RuleBase:RU363117}.
DOMAIN 501 687 RdRp catalytic.
{ECO:0000259|PROSITE:PS50523}.
SEQUENCE 1088 AA; 124962 MW; A021E11B33270E88 CRC64;
MGKYNLILSE YLSFVYNSQS AVQIPIYYSS NSELEKRCIE FHTKCVDSSK KGLSLKPLFE
EYKDVIDNAT LLSILSYSYD KYNAVERKLV NYAKGKPLEA DLTANEIDYE NNKITSELFQ
SAEEYTDSLM DPAILTSLSS NLNAVMFWLE RHSNDVADAN KIYKRRLDLF TIVASTINKY
GVPRHNEKYR YEYEVMKDKP YYLVTWANSS IEMLMSVFSH EDYLIAKELI ILSYSNRSTL
AKLVSSPMSI LVALIDINGT FITNEELELE FSDKYVKAIV PDQIFDELQE MIDNMRKAGL
VDIPRMIQEW LVDCSLEKFT LMSKIYSWSF HVGFRKQKMI DAALDQLKTE YTEDVDNEMY
NEYTMLIRDE IVKMLEVPVK HDDHLLRDSE LAGLLSMSSA SNGESRQLKF GRKTIFSTKK
NMHVMDDIAH GRYTPGVIPP VNVDRPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKM
LLYAKHTREY AEFYSQSNQL LSYGDVTRFL SSNSMVLYTD VSQWDSSQHN TQPFRKGIIM
GLDMLSNMTN DPKVVQTLNL YKQTQINLMD SYVQIPDGNV IKKIQYGAVA SGEKQTKAAN
SIANLALIKT VLSRIANKYS FITKIIRVDG DDNYAVLQFT TDVTKQMVQD VSNDVRYIYS
RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK RGQSTQWDQA AILYSNYIVN
KLRGFETDRE FILTKIIQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD
EVYIQRAFMS LSSQKSGIAD EIASSQTFKN YVNKLSDQLL ISKNVIVSKG IAITEKAKLN
SYAPVYLEKR RAQISALLTM LQKPVSFKSN KITINDILRD IKPFFVTSEA NLPIQYRKFM
PTLPNNVQYV IQCIGSRTYQ IEDSGSKSSI SKLISKYSVY KPSIEELYKV ISLREQEIQL
YLISLGVPPV DAGTYVGSRI YSQDKYKILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI
PFKGKIPAVT FILHLYAKLE IINYAIKNGA WISLFCNYPK SEMIKLWKKM WNITALRSPY
TSANFFQD


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