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Q9QNB3 (RDRP_ROTHK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-directed RNA polymerase

EC=2.7.7.48
Alternative name(s):
Protein VP1
OrganismRotavirus A (strain Human/Japan/KU/1995 G1-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) [Complete proteome]
Taxonomic identifier10952 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1088 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity.

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Cofactor

Magnesium Potential.

Subunit structure

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 By similarity.

Subcellular location

Virion Potential. 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 By similarity.

Sequence similarities

Belongs to the reoviridae RNA-directed RNA polymerase family.

Contains 1 RdRp catalytic domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10881088RNA-directed RNA polymerase
PRO_0000368040

Regions

Domain501 – 687187RdRp catalytic

Sequences

Sequence LengthMass (Da)Tools
Q9QNB3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 214CA10B55825508

FASTA1,088125,017
        10         20         30         40         50         60 
MGKYNLILSE YLSFVYNSQS AVQIPIYYSS NSELETRCIE FHAKCVDNSK KGLSLKPLFE 

        70         80         90        100        110        120 
EYKDVTDNAT LLSILSYSYD KYNAVERKLV SYAKGKPLEA DLTANELDYE NNKITSELFQ 

       130        140        150        160        170        180 
SAEEYTDSLM DPAILTSLSS NLNAVMFWLE RHSNDIADAN KIYKRRLDLF TIVASTINKY 

       190        200        210        220        230        240 
GVPRHNEKYR YEYEVMKDKP YYLVTWANSS IEMLMSVFSH EDYLIAKELI VLSYSNRSTL 

       250        260        270        280        290        300 
AKLVSSPMSI LVALIDINGT FITNEELELE FSDKYVKAIV PDQTFDELQE MINNMKKIGL 

       310        320        330        340        350        360 
VDIPRMIQEW LIDCSLEKFT LMSKIYSWSF HVGFRKQKMI DAALDQLKTE YTKDVDDEMY 

       370        380        390        400        410        420 
NEYTMLIRDE IVKMLEIPVK HDDHLLRDSE LAGLLSMSSA SNGESRQIKF GRKTIFSTKK 

       430        440        450        460        470        480 
NMHVMDDIAH GKYTPGVIPP VNVDKPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKM 

       490        500        510        520        530        540 
LLYAKHTREY AEFYSQSNQL LSYGDVTRFL SSNSMVLYTD VSQWDSSQHN TQPFRKGIIM 

       550        560        570        580        590        600 
GLDMLSNMTN DPKVVQALNL YKQTQINLMD SYVQIPDGNV IKKNQYGAVA SGEKQTKAAN 

       610        620        630        640        650        660 
SIANLALIKT VLSRIANKYS FITKIIRVSG DDNYAVLQFN TDLTKQMIQD VSNDVRYIYF 

       670        680        690        700        710        720 
RMNAKVKALV STVGIEIAKR YLAGGKIFFR AGINLLNNEK RGQSTQWDQA AILYSNYIVN 

       730        740        750        760        770        780 
KLRGFETDRE FILTKIIQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD 

       790        800        810        820        830        840 
EVYIQRAFMS LSSQKSGIAD EIASSQTFKN YVSKLSDQLL VSKNVIVSKG IAVTEKAKLN 

       850        860        870        880        890        900 
SYAPIYLEKR RAQISALLTM LQKPVSFKSN KNTINEILRD IKPFFVTTED NLPIQYRKFM 

       910        920        930        940        950        960 
PTLPDNVQYV IQCIGSRTYQ IEDSGSKSSI SKLISKYSVY KPSIEELYKV ISLREQEIQL 

       970        980        990       1000       1010       1020 
YLVSLGVPLV DASAYVASRI YSQDKYKILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI 

      1030       1040       1050       1060       1070       1080 
PFKGKIPAVT FILHLYAKLE IINYAIKNRA WISVFCNYPK SEMIKLWKKM WSITALRSPY 


TSANFFQD 

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References

[1]Taniguchi K.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB022765 mRNA. Translation: BAA84962.1.

3D structure databases

ProteinModelPortalQ9QNB3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001795. RNA-dir_pol_luteovirus.
IPR007097. RNA-dir_pol_reovirus.
IPR022071. Rotavirus_VP1.
[Graphical view]
PfamPF02123. RdRP_4. 1 hit.
PF12289. Rotavirus_VP1. 1 hit.
[Graphical view]
PROSITEPS50523. RDRP_DSRNA_REO. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRDRP_ROTHK
AccessionPrimary (citable) accession number: Q9QNB3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families