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O37061

- RDRP_ROTSP

UniProt

O37061 - RDRP_ROTSP

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Protein

RNA-directed RNA polymerase

Gene
N/A
Organism
Rotavirus A (strain SA11-Patton G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Patton))
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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.2 PublicationsPROSITE-ProRule annotation

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation

Cofactori

Magnesium.Curated

GO - Molecular functioni

  1. nucleotide binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB-KW
  3. RNA-directed RNA polymerase activity Source: UniProtKB-KW

GO - Biological processi

  1. transcription, DNA-templated Source: InterPro
  2. viral genome replication Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, RNA-directed RNA polymerase, Transferase

Keywords - Biological processi

Viral RNA replication

Keywords - Ligandi

Magnesium, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-directed RNA polymerase (EC:2.7.7.48)
Alternative name(s):
Protein VP1
OrganismiRotavirus A (strain SA11-Patton G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Patton))
Taxonomic identifieri36434 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiMacaca mulatta (Rhesus macaque) [TaxID: 9544]

Subcellular locationi

Virion Curated
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).By similarity

GO - Cellular componenti

  1. virion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10881088RNA-directed RNA polymerasePRO_0000367812Add
BLAST

Interactioni

Subunit structurei

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).By similarityCurated

Structurei

Secondary structure

1
1088
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1512
Beta strandi23 – 286
Helixi32 – 4918
Turni50 – 523
Helixi58 – 614
Helixi63 – 686
Beta strandi69 – 779
Helixi85 – 895
Helixi90 – 923
Helixi108 – 1103
Helixi115 – 1184
Turni122 – 1243
Turni128 – 1303
Beta strandi134 – 1363
Helixi138 – 15114
Turni152 – 1543
Helixi157 – 17822
Helixi193 – 1964
Helixi203 – 21412
Helixi220 – 23213
Turni233 – 2353
Beta strandi237 – 2393
Helixi240 – 2456
Helixi248 – 2514
Turni252 – 2543
Beta strandi257 – 2637
Beta strandi269 – 2768
Helixi282 – 29716
Helixi302 – 3109
Turni311 – 3133
Turni316 – 3194
Helixi320 – 3289
Helixi329 – 3324
Helixi339 – 3446
Helixi361 – 37313
Helixi376 – 3805
Helixi384 – 3874
Helixi389 – 3968
Beta strandi399 – 41012
Beta strandi413 – 4197
Helixi420 – 4289
Turni429 – 4313
Beta strandi442 – 4454
Beta strandi447 – 4526
Beta strandi455 – 4573
Beta strandi460 – 4634
Helixi468 – 48518
Turni491 – 4933
Helixi499 – 50810
Beta strandi514 – 5207
Helixi522 – 5254
Helixi528 – 54619
Helixi552 – 56918
Beta strandi571 – 5766
Beta strandi578 – 5869
Beta strandi593 – 5953
Helixi596 – 61621
Beta strandi622 – 6298
Beta strandi632 – 6387
Helixi645 – 66016
Turni661 – 6633
Beta strandi667 – 6737
Beta strandi675 – 6773
Beta strandi681 – 6833
Beta strandi686 – 6883
Beta strandi695 – 6973
Helixi706 – 72318
Helixi729 – 74012
Beta strandi742 – 75211
Helixi754 – 7585
Beta strandi759 – 7613
Helixi779 – 79012
Helixi797 – 8048
Helixi806 – 81914
Helixi826 – 83712
Helixi838 – 8414
Helixi843 – 86018
Helixi874 – 8818
Helixi882 – 8843
Beta strandi885 – 8906
Helixi905 – 91410
Helixi929 – 9379
Helixi944 – 9518
Helixi955 – 96410
Helixi969 – 9757
Helixi979 – 99618
Turni997 – 10004
Turni1002 – 10065
Helixi1012 – 10165
Helixi1027 – 104822
Beta strandi1049 – 10568
Helixi1060 – 107011
Helixi1079 – 10879

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R7OX-ray3.35A1-1088[»]
2R7QX-ray2.90A1-1088[»]
2R7RX-ray2.60A1-1088[»]
2R7SX-ray3.24A1-1088[»]
2R7TX-ray3.00A1-1088[»]
2R7UX-ray3.10A1-1088[»]
2R7VX-ray2.80A1-1088[»]
2R7WX-ray2.60A1-1088[»]
2R7XX-ray2.80A/B1-1088[»]
4F5XX-ray5.00W1-1088[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO37061.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini501 – 687187RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR001795. RNA-dir_pol_luteovirus.
IPR007097. RNA-dir_pol_reovirus.
IPR022071. Rotavirus_VP1.
[Graphical view]
PfamiPF02123. RdRP_4. 1 hit.
PF12289. Rotavirus_VP1. 1 hit.
[Graphical view]
PROSITEiPS50523. RDRP_DSRNA_REO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O37061-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKYNLILSE YLSFIYNSQS AVQIPIYYSS NSELENRCIE FHSKCLENSK
60 70 80 90 100
NGLSLRKLFV EYNDVIENAT LLSILSYSYD KYNAVERKLV KYAKGKPLEA
110 120 130 140 150
DLTVNELDYE NNKMTSELFP TAEEYTDSLM DPAILTSLSS NLNAVMFWLE
160 170 180 190 200
KHENDVAEKL KVYKRRLDLF TIVASTINKY GVPRHNAKYR YEYDVMKDKP
210 220 230 240 250
YYLVTWANSS IEMLMSVFSH DDYLIAKELI VLSYSNRSTL AKLVSSPMSI
260 270 280 290 300
LVALVDINGT FITNEELELE FSNKYVRAIV PDQTFDELNQ MLDNMRKAGL
310 320 330 340 350
VDIPKMIQDW LVDRSIEKFP LMAKIYSWSF HVGFRKQKML DAALDQLKTE
360 370 380 390 400
YTENVDDEMY REYTMLIRDE VVKMLEEPVK HDDHLLRDSE LAGLLSMSSA
410 420 430 440 450
SNGESRQLKF GRKTIFSTKK NMHVMDDMAN ERYTPGIIPP VNVDKPIPLG
460 470 480 490 500
RRDVPGRRTR IIFILPYEYF IAQHAVVEKM LIYAKHTREY AEFYSQSNQL
510 520 530 540 550
LSYGDVTRFL SNNTMVLYTD VSQWDSSQHN TQPFRKGIIM GLDILANMTN
560 570 580 590 600
DAKVLQTLNL YKQTQINLMD SYVQIPDGNV IKKIQYGAVA SGEKQTKAAN
610 620 630 640 650
SIANLALIKT VLSRISNKHS FATKIIRVDG DDNYAVLQFN TEVTKQMIQD
660 670 680 690 700
VSNDVRETYA RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK
710 720 730 740 750
RGQSTQWDQA AILYSNYIVN RLRGFETDRE FILTKIMQMT SVAITGSLRL
760 770 780 790 800
FPSERVLTTN STFKVFDSED FIIEYGTTVD EVYIQRAFMS LSSQKSGIAD
810 820 830 840 850
EIAASSTFKN YVTRLSEQLL FSKNNIVSRG IALTEKAKLN SYAPISLEKR
860 870 880 890 900
RAQISALLTM LQKPVTFKSS KITINDILRD IKPFFTVSDA HLPIQYQKFM
910 920 930 940 950
PTLPDNVQYI IQCIGSRTYQ IEDDGSKSAI SRLISKYSVY KPSIEELYKV
960 970 980 990 1000
ISLHENEIQL YLISLGIPKI DADTYVGSKI YSRDKYRILE SYVYNLLSIN
1010 1020 1030 1040 1050
YGCYQLFDFN SPDLEKLIRI PFKGKIPAVT FILHLYAKLE VINYAIKNGS
1060 1070 1080
WISLFCNYPK SEMIKLWKKM WNITSLRSPY TNANFFQE
Length:1,088
Mass (Da):125,252
Last modified:March 24, 2009 - v2
Checksum:i7A5AD04A37BA0E8C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF015955 mRNA. Translation: AAC58684.1. Different termination.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF015955 mRNA. Translation: AAC58684.1 . Different termination.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2R7O X-ray 3.35 A 1-1088 [» ]
2R7Q X-ray 2.90 A 1-1088 [» ]
2R7R X-ray 2.60 A 1-1088 [» ]
2R7S X-ray 3.24 A 1-1088 [» ]
2R7T X-ray 3.00 A 1-1088 [» ]
2R7U X-ray 3.10 A 1-1088 [» ]
2R7V X-ray 2.80 A 1-1088 [» ]
2R7W X-ray 2.60 A 1-1088 [» ]
2R7X X-ray 2.80 A/B 1-1088 [» ]
4F5X X-ray 5.00 W 1-1088 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei O37061.

Family and domain databases

InterProi IPR001795. RNA-dir_pol_luteovirus.
IPR007097. RNA-dir_pol_reovirus.
IPR022071. Rotavirus_VP1.
[Graphical view ]
Pfami PF02123. RdRP_4. 1 hit.
PF12289. Rotavirus_VP1. 1 hit.
[Graphical view ]
PROSITEi PS50523. RDRP_DSRNA_REO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Rotavirus RNA polymerase requires the core shell protein to synthesize the double-stranded RNA genome."
    Patton J.T., Jones M.T., Kalbach A.N., He Y.-W., Xiaobo J.
    J. Virol. 71:9618-9626(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "The rotavirus RNA-binding protein NS35 (NSP2) forms 10S multimers and interacts with the viral RNA polymerase."
    Kattoura M.D., Chen X., Patton J.T.
    Virology 202:803-813(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NSP2.
  3. "Mechanism for coordinated RNA packaging and genome replication by rotavirus polymerase VP1."
    Lu X., McDonald S.M., Tortorici M.A., Tao Y.J., Vasquez-Del Carpio R., Nibert M.L., Patton J.T., Harrison S.C.
    Structure 16:1678-1688(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), COFACTOR, FUNCTION.

Entry informationi

Entry nameiRDRP_ROTSP
AccessioniPrimary (citable) accession number: O37061
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: October 29, 2014
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3