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Reviewed, UniProtKB/Swiss-Prot P36958 (RPB9_DROME)

Last modified June 16, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DNA-directed RNA polymerase II subunit RPB9
      Short name=RNA polymerase II subunit B9
Alternative name(s):
    DNA-directed RNA polymerase II 15.1 kDa polypeptide
Gene names
Name: RpII15
ORF Names: CG3284
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template By similarity.

Subunit structure

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits By similarity.

Subcellular location

Nucleus By similarity.

Developmental stage

Expressed both maternally and zygotically throughout development. Ref.1

Sequence similarities

Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.

Contains 1 TFIIS-type zinc finger.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MED6Q8MSX21EBI-167046,EBI-194467
RpII215P040521EBI-167046,EBI-173525

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 129129DNA-directed RNA polymerase II subunit RPB9
PRO_0000121470

Regions

Zinc finger21 – 4626C4-type By similarity
Zinc finger86 – 12843TFIIS-type

Sites

Metal binding211Zinc 1 By similarity
Metal binding241Zinc 1 By similarity
Metal binding431Zinc 1 By similarity
Metal binding461Zinc 1 By similarity
Metal binding901Zinc 2 By similarity
Metal binding931Zinc 2 By similarity
Metal binding1181Zinc 2 By similarity
Metal binding1231Zinc 2 By similarity

Experimental info

Sequence conflict51 – 533EAD → KTN in AAB21674. Ref.1
Sequence conflict1001F → S in AAB29028. Ref.2
Sequence conflict1021Q → K in AAB21674. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P36958-1 [UniParc].

Last modified November 8, 2005. Version 2.
Checksum: B96CAB2022752DB3

FASTA12915,098
        10         20         30         40         50         60 
MTTAFDAAHT EGPGFVGIRF CQECNNMLYP KEDKENKILL YACRNCDYKQ EADSNCIYVN 

        70         80         90        100        110        120 
KIMHEIDELT HIVPDVISDP TLPRTEDHAC PKCSHREAVF FQAQTRRAEE EMRLYYVCTN 


QNCTHRWTE 

« Hide

References

« Hide 'large scale' references
[1]"The RNA polymerase II 15-kilodalton subunit is essential for viability in Drosophila melanogaster."
Harrison D.A., Mortin M.A., Corces V.G.
Mol. Cell. Biol. 12:928-935(1992) [PubMed: 1545824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
[2]"RPII15 codes for the M(r) 15,000 subunit 9 of Drosophila melanogaster RNA polymerase II."
Liu Z., Kontermann R.E., Schulze R.A., Petersen G., Bautz E.K.
FEBS Lett. 335:73-75(1993) [PubMed: 8243669] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.

Cross-references

Sequence databases

S88139 Genomic DNA. Translation: AAB21674.1.
S66940 Genomic DNA. Translation: AAB29028.2.
AE014297 Genomic DNA. Translation: AAF55045.1.
PIRS39445.
RefSeqNP_731898.1.
UniGeneDm.11852

3D structure databases

HSSPHSSP built from PDB template 1I3Q based on UniProtKB P27999.
ModBaseSearch...

Protein-protein interaction databases

IntActP36958. 3 interactions.

Genome annotation databases

EnsemblFBgn0004855. Drosophila melanogaster. [Contig view]
GeneID41741.
KEGGdme:Dmel_CG3284.
NMPDRfig|7227.3.peg.12746.

Organism-specific databases

FlyBaseFBgn0004855. RpII15.

Phylogenomic databases

HOGENOMP36958.
OMAP36958. REAVFFQ.

Gene expression databases

ArrayExpressP36958.
GermOnlineCG3284. Drosophila melanogaster.

Family and domain databases

InterProIPR019761. DNA-dir_RNA_pol-M_15_CS.
IPR001529. DNA-dir_RNA_pol_M/15kDsu.
IPR001222. Znf_TFIIS.
[Graphical view]
PfamPF02150. RNA_POL_M_15KD. 1 hit.
PF01096. TFIIS_C. 1 hit.
[Graphical view]
SMARTSM00661. RPOL9. 1 hit.
SM00440. ZnF_C2C2. 1 hit.
[Graphical view]
PROSITEPS01030. RNA_POL_M_15KD. 1 hit.
PS00466. ZF_TFIIS_1. 1 hit.
PS51133. ZF_TFIIS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio825340.

Entry information

Entry nameRPB9_DROME
AccessionPrimary (citable) accession number: P36958
Secondary accession number(s): Q9VFK8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 8, 2005
Last modified: June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents