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A9Q1K7 (RDRP_ROTB2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 23. 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 (isolate Human/Bangladesh/ADRV-N B219/2002) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-B219)) [Complete proteome]
Taxonomic identifier348136 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusunclassified rotaviruses
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1167 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 dsDNA formation. To do so, the polymerase specifically recognizes conserved 3' sequence(s) in plus-strand RNA templates. 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).

Subunit structure

Interacts with VP3 Potential. Interacts with VP2 Potential. Interacts with NSP5; this interaction is probably necessary for the formation of functional virus factories 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

Keywords
   Biological processViral RNA replication
   Cellular componentVirion
   LigandNucleotide-binding
RNA-binding
   Molecular functionNucleotidyltransferase
RNA-directed RNA polymerase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranscription, DNA-templated

Inferred from electronic annotation. Source: InterPro

viral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular_componentvirion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11671167RNA-directed RNA polymerase
PRO_0000369830

Regions

Domain553 – 735183RdRp catalytic

Sequences

Sequence LengthMass (Da)Tools
A9Q1K7 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: C612426A9D1FE310

FASTA1,167132,901
        10         20         30         40         50         60 
MEPENYLAWL ARDIVRNLSY TSLVYNNPKV AIVELLDNKE AFFTYEKEQK TPEALINYID 

        70         80         90        100        110        120 
SIVKSSISVE DKIEALLKIR YISVYVDDKS DKRDIVLQLL NRTIKKIESK TKISNELNDA 

       130        140        150        160        170        180 
INAITIESRN WKIQNSESFK PYHYNQLVSD FLKYNEFEIL EGTDPLKWKS DTLQGLSPNY 

       190        200        210        220        230        240 
NHRTHTLISS IIYATSVRFD NYNDEQLQVL LYLFSIIKTN YVNGYLEILP NRKWSHSLAD 

       250        260        270        280        290        300 
LRENKSIMMY SAKIIHASCA MISILHAVPI DYFFLAQIIA SFSEIPAHAA KQLSSPMTLY 

       310        320        330        340        350        360 
IGIAQLRSNI VVSTKIAAES VATESPNISR LEESQLREWE QEMNEYPFQS SRMVRMMKKN 

       370        380        390        400        410        420 
IFDVSVDVFY AIFNCFSATF HVGHRIDNPQ DAIEAQVKVE YTSDVDKEMY DQYYFLLKRM 

       430        440        450        460        470        480 
LTDQLAEYAE EMYFKYNSDV TAESLAAMAN SSNGYSRSVT FIDREIKTTK KMLHLDDDLS 

       490        500        510        520        530        540 
KNLNFTNIGE QIKKGIPMGT RNVPARQTRG IFILSWQVAA IQHTIAEFLY KKAKKGGFGA 

       550        560        570        580        590        600 
TFAEAYVSKA ATLTYGILAE ATSKADQLIL YTDVSQWDAS QHNTEPYRSA WINAIKEART 

       610        620        630        640        650        660 
KYKINYNQEP VVLGMNVLDK MIEIQEALLN SNLIVESQGS KRQPLRIKYH GVASGEKTTK 

       670        680        690        700        710        720 
IGNSFANVAL ITTVFNNLTN TMPSIRVNHM RVDGDDNVVT MYTANRIDEV QENIKEKYKR 

       730        740        750        760        770        780 
MNAKVKALAS YTGLEMAKRF IICGKIFERG AISIFTAERP YGTDLSVQST TGSLIYSAAV 

       790        800        810        820        830        840 
NAYRGFGDDY LNFMTDVLVP PSASVKITGR LRSLLSPVTL YSTGPLSFEI TPYGLGGRMR 

       850        860        870        880        890        900 
LFSLSKENME LYKILTSSLA ISIQPDEIKK YSSTPQFKAR VDRMISSVQI AMKSEAKIIT 

       910        920        930        940        950        960 
SILRDKEEQK TLGVPNVATA KNRQQIDKAR KTLSLPKEIL PKVTKYYPEE IFHLILRNST 

       970        980        990       1000       1010       1020 
LTIPKLNTMT KVYMNNSVNI TKLQQQIGVR VSSGIQVHKP INTLLKLVEK HSPIKISPSD 

      1030       1040       1050       1060       1070       1080 
LILYSKKYDL TNLNGKKQFL MDLGISGNEL RFYLNSKLLF HDLLLSKYDK LYEAPGFGAT 

      1090       1100       1110       1120       1130       1140 
QLNALPLDLT AAEKVFSIKL NLPNTYYELL MLVLLYEYVN FVMFTGNTFR AVCIPESQTI 

      1150       1160 
NAKLVKTIMT MIDNIQLDTV MFSDNIF 

« Hide

References

[1]"Whole genomic characterization of a human rotavirus strain B219 belonging to a novel group of the genus Rotavirus."
Nagashima S., Kobayashi N., Ishino M., Alam M.M., Ahmed M.U., Paul S.K., Ganesh B., Chawla-Sarkar M., Krishnan T., Naik T.N., Wang Y.-H.
J. Med. Virol. 80:2023-2033(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF453355 mRNA. Translation: ABR32122.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Entry information

Entry nameRDRP_ROTB2
AccessionPrimary (citable) accession number: A9Q1K7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 23 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