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P0C8K4 (RPB2_ASFP4) Reviewed, UniProtKB/Swiss-Prot

Last modified March 8, 2011. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA-directed RNA polymerase subunit 2

EC=2.7.7.6
Gene names
Ordered Locus Names:Pret-065
OrganismAfrican swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996) (ASFV) [Complete proteome]
Taxonomic identifier561443 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageAsfarviridaeAsfivirus
Virus hostOrnithodoros (relapsing fever ticks) [TaxID: 6937]
Sus scrofa (Pig) [TaxID: 9823]
Phacochoerus africanus (Warthog) [TaxID: 41426]
Phacochoerus aethiopicus (Warthog) [TaxID: 85517]
Potamochoerus larvatus (Bushpig) [TaxID: 273792]

Protein attributes

Sequence length1242 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the DNA-dependent RNA polymerase that catalyzes the transcription in the cytoplasm of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Subunit 2 is the second largest component of RNA polymerase. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. DNA-dependent RNA polymerase is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template By similarity.

Catalytic activity

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

Subunit structure

Component of the RNA polymerase that consists of at least 6 subunits Probable.

Subcellular location

Host cytoplasm Potential.

Miscellaneous

The binding of ribonucleoside triphosphate to the RNA polymerase transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion coordinated by three conserved aspartate residues of the two largest RNA Pol subunits By similarity.

Sequence similarities

Belongs to the RNA polymerase beta chain family.

Ontologies

Keywords
   Biological processTranscription
   Cellular componentDNA-directed RNA polymerase
Host cytoplasm
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionNucleotidyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12421242DNA-directed RNA polymerase subunit 2
PRO_0000355627

Regions

Zinc finger1180 – 120122C4-type

Sequences

Sequence LengthMass (Da)Tools
P0C8K4 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 10E23F427C1CA48E

FASTA1,242139,864
        10         20         30         40         50         60 
MEPLRPQITY GPIETVDNEE LTEADMLSFI SAAVNSTGLI GYNIKSFDDL MDNGIPQIVK 

        70         80         90        100        110        120 
QMFNVDITYK DQRDHTEIDK LRESVQIQFN FTDVNIERPQ HRNYSQGNKI NLLPNKARLC 

       130        140        150        160        170        180 
GLSYSGPVNL AAEVILTAHY SNGRQEVKRA SIPPFQVSTF PIMRGSNRCH THHLSKTAKK 

       190        200        210        220        230        240 
EIGEDPNEPG GYFIARGGEW VVDLLENIRF NTLHIHYHTM QQGNNEIIRG EFISQPGGAF 

       250        260        270        280        290        300 
ENSSQIIIRY MTTGAITIEI NSTKFSKLRI PWYLIFRMFG MTGDDSIIEQ VVFDLESNSL 

       310        320        330        340        350        360 
VNTFMIEILE KSIHVLDPIF QPVQHELNRE KIIQFLSEKV SKFVSNPSAY KSDENAVQYL 

       370        380        390        400        410        420 
NERQLTILDK ILLPHMGQTA DTRVRKLRFL GLLIHKILLV IMNVFPPTDR DSYRTKRVHG 

       430        440        450        460        470        480 
SGVSLAKAFK AIFNTSVIAP IINGFKELLK QTAFEELTQR NIIEAFSAAL SKNTASDLNR 

       490        500        510        520        530        540 
SMEQSIISGN KTIMVRQRPI VNRVSTQSLE RKNLLNTISA LRTVNTHNTT NASKQTERAD 

       550        560        570        580        590        600 
MMRRVHASYP GYICVAQSAD TGEKVGMSKQ LAITANVCTA GEVLSLKQRL LSDPAIQQLA 

       610        620        630        640        650        660 
DVSNKDIVRK GLARVFINGE WIGCCTNAFE LAQRYRMLRR EGKIVHPHTT IYWDSMVDEV 

       670        680        690        700        710        720 
EFWLDVGRLT RPLLIVDNNI EKYNQACYKA AEARKKGDKD WEKHKIPFVQ NTRFTSQMAK 

       730        740        750        760        770        780 
DILAGTLTLE DLVAQGICEF ITPEEAENCL VAFSIIELRK HKHDVTRRFT HVDVPQAILG 

       790        800        810        820        830        840 
LAALVSPYAN CTQPARVTYE TNQGRQTGGW YCFSWPYRVD MNRFFQFYNE MPLVKTIAHN 

       850        860        870        880        890        900 
YVIPNGLNTI VAYMIYGGYN QEDSVIVSQS FIDRGGFAGT FYREEKVELE SDIESFGKPD 

       910        920        930        940        950        960 
PLITKNLKPG ANYEKLVDGF VPVGTVVKKG DIIIGKVAKI RGEKDELNKY IDRSVMYGFD 

       970        980        990       1000       1010       1020 
EPAVVDAVMR PHGPNDEIFG LMRLRYERNL NIGDKMSSRS GNKGIAALAL PTSDMPFTED 

      1030       1040       1050       1060       1070       1080 
GLQPDLIVNP HSHPSRMTNG QMIETTVGLA NALQGVVTDG TAFLPINVQL LSERLAQEGL 

      1090       1100       1110       1120       1130       1140 
RFNGCQKMFN GQTGEYFDAA IFIGPTYHQR LQKFVLDDRY AVASYGPTDA LTGQPLDGKR 

      1150       1160       1170       1180       1190       1200 
SHGGLRLGEM EHWVLTAQGA MQTIIEKSHD DSDGCISYVC RNCGEPAIYN ASHPIYKCMN 

      1210       1220       1230       1240 
CDVQADIGMV DSRRSSIVFQ HEMRAANVNI TSVLSPRVFQ PA 

« Hide

References

[1]"African swine fever virus genomes."
Kutish G.F., Rock D.L.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY261363 Genomic DNA. No translation available.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR015712. DNA-dir_RNA_pol_su2.
IPR007120. DNA-dir_RNA_pol_su2_6.
IPR007121. RNA_pol_bsu_CS.
IPR007644. RNA_pol_bsu_protrusion.
IPR007642. RNA_pol_Rpb2_2.
IPR007645. RNA_pol_Rpb2_3.
IPR007646. RNA_pol_Rpb2_4.
IPR007647. RNA_pol_Rpb2_5.
IPR007641. RNA_pol_Rpb2_7.
IPR014724. RNA_pol_RPB2_OB-fold.
[Graphical view]
Gene3DG3DSA:2.40.270.10. G3DSA:2.40.270.10. 2 hits.
G3DSA:2.40.50.150. Ribosomal_L2. 1 hit.
PANTHERPTHR20856. RNA_pol_I_sub2. 1 hit.
PfamPF04563. RNA_pol_Rpb2_1. 1 hit.
PF04561. RNA_pol_Rpb2_2. 1 hit.
PF04565. RNA_pol_Rpb2_3. 1 hit.
PF04566. RNA_pol_Rpb2_4. 1 hit.
PF04567. RNA_pol_Rpb2_5. 1 hit.
PF00562. RNA_pol_Rpb2_6. 1 hit.
PF04560. RNA_pol_Rpb2_7. 1 hit.
[Graphical view]
PROSITEPS01166. RNA_POL_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRPB2_ASFP4
AccessionPrimary (citable) accession number: P0C8K4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: March 8, 2011
This is version 12 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