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

 A0A024CF44_9REOV        Unreviewed;      1088 AA.
A0A024CF44;
09-JUL-2014, integrated into UniProtKB/TrEMBL.
09-JUL-2014, sequence version 1.
25-OCT-2017, entry version 10.
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:AHZ33021.1};
ORFNames=L312_46698gpVP1 {ECO:0000313|EMBL:AHZ32425.1},
L312_46711gpVP1 {ECO:0000313|EMBL:AHZ32901.1},
L312_46716gpVP1 {ECO:0000313|EMBL:AHZ33021.1},
L312_46717gpVP1 {ECO:0000313|EMBL:AHZ32461.1},
L312_46718gpVP1 {ECO:0000313|EMBL:AHZ33338.1},
L312_46719gpVP1 {ECO:0000313|EMBL:AHZ32581.1};
Rotavirus A.
Viruses; dsRNA viruses; Reoviridae; Sedoreovirinae; Rotavirus.
NCBI_TaxID=28875 {ECO:0000313|EMBL:AHZ33021.1, ECO:0000313|Proteomes:UP000156718};
[1] {ECO:0000313|Proteomes:UP000104860, ECO:0000313|Proteomes:UP000105692, ECO:0000313|Proteomes:UP000117880}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RVA/Human-wt/ZAF/MRC-DPRU358/2000/G9P[6]
{ECO:0000313|EMBL:AHZ33021.1},
RVA/Human-wt/ZAF/MRC-DPRU384/2000/G9P[6]
{ECO:0000313|EMBL:AHZ32461.1},
RVA/Human-wt/ZAF/MRC-DPRU4079-00/2000/G9P[6]
{ECO:0000313|EMBL:AHZ32425.1},
RVA/Human-wt/ZAF/MRC-DPRU421/2002/G9P[6]
{ECO:0000313|EMBL:AHZ33338.1},
RVA/Human-wt/ZAF/MRC-DPRU751/2006/G9P[6]
{ECO:0000313|EMBL:AHZ32901.1}, and
RVA/Human-wt/ZAF/MRC-DPRU797/2000/G9P[6]
{ECO:0000313|EMBL:AHZ32581.1};
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.
-!- 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: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {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; KJ751669; AHZ32425.1; -; Genomic_RNA.
EMBL; KJ751702; AHZ32461.1; -; Genomic_RNA.
EMBL; KJ751812; AHZ32581.1; -; Genomic_RNA.
EMBL; KJ752106; AHZ32901.1; -; Genomic_RNA.
EMBL; KJ752216; AHZ33021.1; -; Genomic_RNA.
EMBL; KJ752508; AHZ33338.1; -; Genomic_RNA.
Proteomes; UP000104860; Genome.
Proteomes; UP000105692; Genome.
Proteomes; UP000117880; Genome.
Proteomes; UP000156718; Genome.
Proteomes; UP000157259; Genome.
Proteomes; UP000175457; 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:UP000104860,
ECO:0000313|Proteomes:UP000105692, ECO:0000313|Proteomes:UP000117880,
ECO:0000313|Proteomes:UP000156718};
Magnesium {ECO:0000256|RuleBase:RU363117};
Nucleotide-binding {ECO:0000256|RuleBase:RU363117};
Nucleotidyltransferase {ECO:0000256|RuleBase:RU363117,
ECO:0000313|EMBL:AHZ33021.1};
RNA-binding {ECO:0000256|RuleBase:RU363117};
RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU363117,
ECO:0000313|EMBL:AHZ33021.1};
Transferase {ECO:0000256|RuleBase:RU363117,
ECO:0000313|EMBL:AHZ33021.1};
Viral RNA replication {ECO:0000256|RuleBase:RU363117};
Virion {ECO:0000256|RuleBase:RU363117}.
DOMAIN 501 687 RdRp catalytic.
{ECO:0000259|PROSITE:PS50523}.
SEQUENCE 1088 AA; 124978 MW; 4849EF6959CD44E4 CRC64;
MGKYNLILSE YLSFIYNSQS AVQIPIYYSS NSELESRCIE FHSKCLENSK NGLSLKKLFN
EYSDVIENAT LLSILSYSYD KYNAVERKLV KYAKGKPLEA DLTVNELDYE NNKITSELFP
TAEEYTDSLM DPAILTSLSS NLNAVMFWLE KHENDTAEKF KIYKRRLDLF TIVASTVNKY
GVPRHNAKYR YEYDVMKDKP YYLVTWANSS IEMLMSVFSH EDYLIARELI VLSYSNRSTL
AKLVSSPMSI LVALVDINGT FITNEELELE FSNKYVRAIV PDQTFDELKQ MLNSMRKAGL
VDIPKMIQDW LVDCSIEKFP LMAKIYSWSF HVGFRKQKML DAALDQLKTE YTEDVDDEMY
REYTMLIRDE VVKMLEESVK HDDHLLQDSE LAGLLSMSSA SNGESRQLKF GRKTVFSTKK
NMHVMDDMAN GRYTPGIIPP VNVDKPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKM
LIYAKHTREY AEFYSQSNQL LSYGDVTRFL SNNAMVLYTD VSQWDSSQHN TQPFRKGIIM
GLDILANMTN DAKVIQTLNL YKQTQINLMD SYVQIPDGNV IKKIQYGAVA SGEKQTKAAN
SIANLALIKT VLSRISNKYS FATKIIRVDG DDNYAVLQFN TEVTKQMVQD VSNAVRETYA
RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK RGQSTQWDQA AVLYSNYIVN
RLRGFETDRE FILTKIMQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD
EVYIQRAFMS LSSQRSGIAD EIAASPTFKN YVSRLSEQLL FSKNNIVSRG IALTEKAKLN
SYAPISLEKR RAQISALLTM LQKPVTFKSN KITINDILKD IKPFFTVSEA HLPIQYQKFM
PTLPENVQYI IQCIGSRTYQ IEDDGSKSAI SRLISKYSVY KPSIEELYKV ISLHENEIQL
YLISLGIPKI DADTYVGSKI YSQDKYRILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI
PFKGKIPAVT FILHLYAKLE VINHAIKNGS WISLFCNYPK SEMIKLWKKM WNITSLRSPY
TNANFFQD


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