Reviewed, UniProtKB/Swiss-Prot P08266 (RPB2_DROME)

Names and origin

Protein names

Recommended name:
    DNA-directed RNA polymerase II subunit RPB2
      Short name=RNA polymerase II subunit B2
      Short name=RNA polymerase II subunit 2
    EC=2.7.7.6
Alternative name(s):
    DNA-directed RNA polymerase II 140 kDa polypeptide

Gene names

Name:	RpII140
ORF Names:	CG3180

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1176 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. 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. 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 II (Pol II) complex consisting of 12 subunits By similarity.
Subcellular location	Nucleus By similarity.
Miscellaneous	The binding of ribonucleoside triphosphate to the RNA polymerase II 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 II subunits By similarity.
Sequence similarities	Belongs to the RNA polymerase beta chain family.
Sequence caution	The sequence CAA29180.2 differs from that shown. Reason: Frameshift at position 43. The frameshift leads to an erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Domain	Zinc-finger
Ligand	Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	transcription from RNA polymerase II promoter Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	DNA-directed RNA polymerase II, core complex Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Ref.1 Non-traceable author statement. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1176	1176	DNA-directed RNA polymerase II subunit RPB2		PRO_0000048084
Regions
	Zinc finger	1121 – 1142	22	C4-type
Sites
	Metal binding	794	1	Magnesium; shared with RPB1 By similarity
	Metal binding	1121	1	Zinc By similarity
	Metal binding	1124	1	Zinc By similarity
	Metal binding	1139	1	Zinc By similarity
	Metal binding	1142	1	Zinc By similarity
Experimental info
	Sequence conflict	72	1	A → R in CAA29180. Ref.1
	Sequence conflict	666 – 667	2	ID → MY in CAA29180. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P08266-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 224821B335BED7F0	FASTA	1,176	134,043
	10 20 30 40 50 60 MMYDNEEELY EEENAEEISH ELWQEACWIV INAYFDEKGL VRQQLDSFDE FIQMSVQRIV 70 80 90 100 110 120 EDSPAIELQA EAQHTSGEVE TPPRFSLKFE QIYLSKPTHW EKDGSPSPMM PNEARLRNLT 130 140 150 160 170 180 YSAPLYVDIT KTKNVEGLDP VETQHQKTFI GKIPIMLRST YCLLSQLTDR DLTELNECPL 190 200 210 220 230 240 DPGGYFIING SEKVLIAQEK MATNTVYVFS MKDGKYAFKT EIRSCLEHSS RPTSTLWVNM 250 260 270 280 290 300 MARGSQNIKK SAIGQRIIAI LPYIKQEIPI MIVFRALGFV ADRDILEHII YDFDDPEMME 310 320 330 340 350 360 MVKPSLDEAF VVQEQNVALN FIGARGARPG VTKDKRIKYA KEILQKEMLP HVGVSDFCET 370 380 390 400 410 420 KKAYFLGYMV HRLLLASLGR RELDDRDHYG NKRLDLAGPL LAFLFRGLFK NLMKEVRMYT 430 440 450 460 470 480 QKFIDRGKDF NLELAIKTNI ITDGLRYSLA TGNWGDQKKA HQARAGVSQV LNRLTFASTL 490 500 510 520 530 540 SHLRRVNSPI GRDGKLAKPR QLHNTLWGML CPAETPEGAA VGLVKNLALM AYISVGSQPS 550 560 570 580 590 600 PILEFLEEWS MENLEEIAPS AIADATKIFV NGCWVGIHRD PEQLMATLRK LRRQMDIIVS 610 620 630 640 650 660 EVSMIRDIRD REIRIYTDAG RICRPLLIVE NGSLLLKKTH VEMLKERDYN NYSWQVLVAS 670 680 690 700 710 720 GVVEYIDTLE EETVMIAMSP YDLKQDKDYA YCTTYTHCEI HPAMILGVCA SIIPFPDHNQ 730 740 750 760 770 780 SPRNTYQSAM GKQAMGVYIT NFHVRMDTLA HVLYYPMKPL VTTRSMEYLR FRELPAGINS 790 800 810 820 830 840 IVAILCYTGY NQEDSVILNA SAVERGFFRS VFYRSYKDSE NKRVGDQEEN FEKPHRGTCQ 850 860 870 880 890 900 GMRNAHYDKL DDDGIIAPGI RVSGDDVVIG KTITLPENDD ELDSNTKRFS KRDASTFLRN 910 920 930 940 950 960 SETGIVDQVM LTLNSEGYKF CKIRVRSVRI PQIGDKFASR HGQKGTCGIQ YRQEDMAFTC 970 980 990 1000 1010 1020 EGLAPDIIIN PHAIPSRMTI GHLIECLQGK LGSNKGEIGD ATPFNDAVNV QKISTFLQEY 1030 1040 1050 1060 1070 1080 GYHLRGNEVM YNGHTGRKIN AQVFLGPTYY QRLKHMVDDK IHSRARGPVQ ILVRQPMEGR 1090 1100 1110 1120 1130 1140 ARDGGLRFGE MERDCQISHG AAQFLRERLF EVSDPYRVHI CNFCGLIAIA NLRNNTFECK 1150 1160 1170 GCKNKTQISQ VRLPYAAKLL FQELMSMNIA PRLMVT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"RNA polymerase II of Drosophila. Relation of its 140,000 Mr subunit to the beta subunit of Escherichia coli RNA polymerase." Falkenburg D., Dworniczak B., Faust D.M., Bautz E.K.F. J. Mol. Biol. 195:929-937(1987) [PubMed: 3116266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Embryo.
[2]	"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. , 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.
[3]	"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. , 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.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Analysis of the promoter region of the housekeeping gene DmRP140 by sequence comparison of Drosophila melanogaster and Drosophila virilis." Sitzler S., Oldenburg I., Petersen G., Bautz E.K.F. Gene 100:155-162(1991) [PubMed: 1905256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X05709 Genomic DNA. Translation: CAA29180.2. Frameshift. AE014297 Genomic DNA. Translation: AAF55024.1. BT003265 mRNA. Translation: AAO25022.1. M62972 Genomic DNA. Translation: AAA28476.1.
PIR	A27826.
RefSeq	NP_476706.1.
UniGene	Dm.6926
3D structure databases
HSSP	HSSP built from PDB template 1I50 based on UniProtKB P08518.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:17498N.
IntAct	P08266. 3 interactions.
Genome annotation databases
Ensembl	FBgn0003276. Drosophila melanogaster. [Contig view]
GeneID	41721.
KEGG	dme:Dmel_CG3180.
NMPDR	fig|7227.3.peg.12716.
Organism-specific databases
FlyBase	FBgn0003276. RpII140.
Phylogenomic databases
HOGENOM	P08266.
OMA	P08266. FGPTYYQ.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-011546-MON.
BRENDA	2.7.7.6. 48.
Gene expression databases
ArrayExpress	P08266.
GermOnline	CG3180. Drosophila melanogaster.
Family and domain databases
InterPro	IPR015712. 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. [Graphical view]
PANTHER	PTHR20856. RNA_pol_I_sub2. 1 hit.
Pfam	PF04563. 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]
PROSITE	PS01166. RNA_POL_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	825231.

Entry information

Entry name

RPB2_DROME

Accession

Primary (citable) accession number: P08266
Secondary accession number(s): Q04155, Q95027, Q9VFM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project