Reviewed, UniProtKB/Swiss-Prot P25167 (RPC2_DROME)

Names and origin

Protein names

Recommended name:
    DNA-directed RNA polymerase III subunit RPC2
      Short name=RNA polymerase III subunit C2
    EC=2.7.7.6
Alternative name(s):
    DNA-directed RNA polymerase III 128 kDa polypeptide
      Short name=C128

Gene names

Name:	RpIII128
Synonyms:	RP128
ORF Names:	CG8344

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	1137 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft By similarity.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits By similarity.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the RNA polymerase beta chain family.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct ribonucleoside binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9W4I6	1	EBI-156773,EBI-142324
Sce	Q9VB08	1	EBI-156773,EBI-145507

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1137	1137	DNA-directed RNA polymerase III subunit RPC2		PRO_0000048094
Regions
	Zinc finger	1084 – 1099	16	C4-type
Sites
	Metal binding	1086	1	Zinc By similarity
	Metal binding	1089	1	Zinc By similarity
	Metal binding	1098	1	Zinc By similarity
	Metal binding	1101	1	Zinc By similarity
Experimental info
	Sequence conflict	150	1	Missing in CAA41631. Ref.1
	Sequence conflict	490	1	D → Y in CAA41631. Ref.1
	Sequence conflict	668	1	P → T in CAA41631. Ref.1
	Sequence conflict	708 – 709	2	QK → HN in CAA41631. Ref.1
	Sequence conflict	898 – 899	2	EI → R in CAA41631. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P25167-1 [UniParc]. Last modified October 25, 2005. Version 2. Checksum: 043EC430D998E1FD	FASTA	1,137	128,515
	10 20 30 40 50 60 MVELKMGDHN VEATTWDPGD SKDWSVPIKP LTEKWKLVPA FLQVKGLVKQ HIDSFNHFIN 70 80 90 100 110 120 VDIKKIVKAN ELVTSGADPL FYLKYLDVRV GKPDIDDGFN ITKATTPHEC RLRDTTYSAP 130 140 150 160 170 180 ITVDIEYTRG TQRIKRNNLL IGRMPLMLRC SNCALTGKSE FELSKLNECP LDPGGYFVVR 190 200 210 220 230 240 GQEKVILIQE QLSWNKMLTE DFNGVVQCQV TSSTHEKKSR TLVLSKHGKY YLKHNSMTDD 250 260 270 280 290 300 IPIVVIFKAL GVVSDQEIQS LIGIDSKSQN RFGASLIDAY NLKVFTQQRA LEYMGSKLVV 310 320 330 340 350 360 KRFQSATTKT PSEEARELLL TTILAHVPVD NFNLQMKAIY VSMMVRRVMA AELDKTLFDD 370 380 390 400 410 420 RDYYGNKRLE LAGSLLSMMF EDLFKRMNWE LKTIADKNIP KVKAAQFDVV KHMRAAQITA 430 440 450 460 470 480 GLESAISSGN WTIKRFKMER AGVTQVLSRL SYISALGMMT RVNSQFEKTR KVSGPRSLQP 490 500 510 520 530 540 SQWGMLCPSD TPEGEACGLV KNLALMTHIT TEVEERPVMI VAFNAGVEDI REVSGNPINN 550 560 570 580 590 600 PNVFLVFING NVLGLTLNHK HLVRNLRYMR RKGRMGSYVS VHTSYTQRCI YIHTDGGRLC 610 620 630 640 650 660 RPYVIVENRR PLVKQHHLDE LNRGIRKFDD FLLDGLIEYL DVNEENDSFI AWNEDQIEDR 670 680 690 700 710 720 TTHLEIEPFT LLGVCAGLVP YPHHNQSPRN TYQCAMGKQA MGMIGYNQKN RIDSLMYNLV 730 740 750 760 770 780 YPHAPMVKSK TIELTNFDKL PAGQNATVAV MSYSGYDIED ALILNKASID RGYGRCLVYK 790 800 810 820 830 840 NSKCTVKRYA NQTFDRIMGP MKDALTNKVI FKHDVLDTDG IVAPGEQVQN KQIMINKEMP 850 860 870 880 890 900 AVTSMNPLQG QSAQVPYTAV PISYKGPEPS YIERVMVSAN AEEDFLIKIL LRQTRIPEIG 910 920 930 940 950 960 DKFSSRHGQK GVTGLIVEQE DMPFNDFGIC PDMIMNPHGF PSRMTVGKTL ELLGGKAGLL 970 980 990 1000 1010 1020 EGKFHYGTAF GGSKVEDIQA ELERHGFNYV GKDFFYSGIT GTPLEAYIYS GPVYYQKLKH 1030 1040 1050 1060 1070 1080 MVQDKMHARA RGPKAVLTRQ PTQGRSREGG LRLGEMERDC LISYGASMLI MERLMISSDA 1090 1100 1110 1120 1130 FEVDVCRTCG RMAYCSWCHF CQSSANVSKI SMPYACKLLF QELTSMNVVP KMILENY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of the genes coding for the second-largest subunits of RNA polymerases I and III of Drosophila melanogaster." Seifarth W., Petersen G., Kontermann R., Riva M., Huet J.-C., Bautz E.K.F. Mol. Gen. Genet. 228:424-432(1991) [PubMed: 1910149] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Oregon-R.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X58826 Genomic DNA. Translation: CAA41631.1. AE013599 Genomic DNA. Translation: AAF58590.1. AY121645 mRNA. Translation: AAM51972.1. Different initiation.
PIR	RNFF32. S16894.
RefSeq	NP_523706.1.
UniGene	Dm.2692
3D structure databases
HSSP	HSSP built from PDB template 1I6H based on UniProtKB P08518.
ModBase	Search...
Protein-protein interaction databases
IntAct	P25167. 4 interactions.
Genome annotation databases
Ensembl	FBgn0004463. Drosophila melanogaster. [Contig view]
GeneID	36289.
KEGG	dme:Dmel_CG8344.
NMPDR	fig|7227.3.peg.4743.
Organism-specific databases
FlyBase	FBgn0004463. RpIII128.
Phylogenomic databases
HOGENOM	P25167.
OMA	P25167. FKMERAG.
Enzyme and pathway databases
BRENDA	2.7.7.6. 48.
Gene expression databases
ArrayExpress	P25167.
GermOnline	CG8344. 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	797763.

Entry information

Entry name

RPC2_DROME

Accession

Primary (citable) accession number: P25167
Secondary accession number(s): Q8MRD5, Q9V649

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	October 25, 2005
Last modified:	June 16, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project