Q6BI69 (RPC1_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-directed RNA polymerase III subunit RPC1
Short name=RNA polymerase III subunit C1
EC=2.7.7.6

Alternative name(s):
DNA-directed RNA polymerase III largest subunit

Gene names

Name:	RPC1
Ordered Locus Names:	DEHA2G12980g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces

Protein attributes

Sequence length	1457 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition 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
Ligand	Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
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 ribonucleoside binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1457	1457	DNA-directed RNA polymerase III subunit RPC1		PRO_0000073952
Regions
	Region	854 – 866	13	Bridging helix By similarity
Sites
	Metal binding	67	1	Zinc 1 By similarity
	Metal binding	70	1	Zinc 1 By similarity
	Metal binding	77	1	Zinc 1 By similarity
	Metal binding	80	1	Zinc 1 By similarity
	Metal binding	107	1	Zinc 2 By similarity
	Metal binding	110	1	Zinc 2 By similarity
	Metal binding	154	1	Zinc 2 By similarity
	Metal binding	508	1	Magnesium; catalytic By similarity
	Metal binding	510	1	Magnesium; catalytic By similarity
	Metal binding	512	1	Magnesium; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BI69 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 36612BF648F639D3	FASTA	1,457	162,213
	10 20 30 40 50 60 MKEVVVDVAP KCIKGIEFGA LSAKDIIAQS EVEVHTRDLY DLEKGRIPKD GGALDTKMGI 70 80 90 100 110 120 SSNANECATC HGNLASCHGH FGHIKLALPV FHVGYFKATI QVLQCICKNC SAVLLDEQTK 130 140 150 160 170 180 RSFLNDLRRP HIDNLRRMKI LKKLLEQCKK QRRCLNCNHV NGVVKKAASG AGPAALKIVH 190 200 210 220 230 240 DTFRWIGKKA TPEKDLWDKE FDEVFSRNPE LEKFVKRIHD DLNPLKVLNL FKQISPSDCE 250 260 270 280 290 300 LLGIDSARGG RPEMYIWRYL PAPPVCIRPS VMMDAQSNED DLTIKLTEIV WTSSLIKAGI 310 320 330 340 350 360 EKGISINNLM EQWDYLQLSV AMYINSDSAN PALLPSSGGG SKSSKPIRGF CQRLKGKQGR 370 380 390 400 410 420 FRGNLSGKRV DFSGRTVISP DPNLKIDEVA VPDRVAKVLT YPEKCTRYNR KKLQKLILSG 430 440 450 460 470 480 PNVHPGANYL LKQNESAKRN LRFGDRVKLA KNLHIGDVVE RHIEDGDIVL FNRQPSLHRL 490 500 510 520 530 540 SILSHYAKIR PWRTFRLNEC VCTPYNADFD GDEMNIHVPQ TEEARAEAIN LMGVKNNLLT 550 560 570 580 590 600 PKSGEPIIAA TQDFITGSYL VSHKDSFFDR ASLVQLLCMM SDADIQFDIP PPAIFKPVML 610 620 630 640 650 660 WTGKQVFSLL IKPNKKSNVV INLDAKNKTY TPPAKGFPNE MSPNDGFVII RGSQILSGVM 670 680 690 700 710 720 DKSTLGDGKK HSVFYTILRD YGPDEAANAM NRMAKLCARY LGNRGFSIGI NDVIPGSDLK 730 740 750 760 770 780 QKKELMVEQA YLKCDELIDL YNRGNLETQP GCNEEQTLEA KIGGLLSKVR EEVGEICINE 790 800 810 820 830 840 LDSANAPLIM ATCGSKGSTL NVSQMVAVVG QQIISGNRVP DGFQDRSLPH FTKNSKTPQS 850 860 870 880 890 900 KGFVRNSFFS GLTPPEFLFH SISGREGLVD TAVKTAETGY MSRRLMKSLD DLSAQYDHTV 910 920 930 940 950 960 RNSSNGIVQF TYGGDGLDPF DMEGDARPVN FVRQWDHAYN ITFDIEDKGL LPYQIIELVD 970 980 990 1000 1010 1020 SILHPLEDRL VRYDNVGKII PLEDSDKIEY IDQNDAEREF YQSIREFTTN KATKLAEIRE 1030 1040 1050 1060 1070 1080 KKMLKPFLTE PAEDFIRLDE SDESLVAINQ LSKVSANSIN KFLEQCIYKY SRAKVEPGTA 1090 1100 1110 1120 1130 1140 VGAIGAQSIG EPGTQMTLKT FHFAGVASMN VTLGVPRIKE IINASKVIST PIINSVLVND 1150 1160 1170 1180 1190 1200 DDEIAARVVK GRVEKTLLED VAYFIEDVYK NNMAYLSIKI DLNTIEKLQL ELNIESIAHS 1210 1220 1230 1240 1250 1260 IANAPKLKIL AGDVSVTGKD RINVLVTLRE PKSINLMKNA SADYKGTDAS IVNSLFFRMQ 1270 1280 1290 1300 1310 1320 HLKRALPRIC IKGLPDISRA VINIRDDGKK ELLVEGYGLK EVMSTDGVVG TKTSTNHILE 1330 1340 1350 1360 1370 1380 VFQVLGIEAA RASIIGEIDY TMSKHGMSVD PRHIQLLGDV MTYKGEVLGI TRFGLSKMRD 1390 1400 1410 1420 1430 1440 SVLQLASFEK TTDHLFDASF YMKNDKIEGV SECIILGQTM NIGTGAFKLV NSFDVDKKAL 1450 EMKPTLFEGM CEVSATA

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382139 Genomic DNA. Translation: CAG90588.2.
RefSeq	XP_462102.2. XM_462102.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6BI69.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2905015.
GenomeReviews	Gene locus DEHA2G12980g in contig CR382139_GR.
KEGG	dha:DEHA2G12980g.
Phylogenomic databases
eggNOG	fuNOG05474.
HOGENOM	HBG499785.
OMA	PRRPLIF.
OrthoDB	EOG4X3M8C.
Family and domain databases
InterPro	IPR000722. RNA_pol_asu. IPR015700. RNA_pol_III_lsu. IPR006592. RNA_pol_N. IPR007080. RNA_pol_Rpb1_1. IPR007066. RNA_pol_Rpb1_3. IPR007083. RNA_pol_Rpb1_4. IPR007081. RNA_pol_Rpb1_5. [Graphical view]
KO	K03018.
PANTHER	PTHR19376:SF15. RNA_pol3. 1 hit.
Pfam	PF04997. RNA_pol_Rpb1_1. 1 hit. PF00623. RNA_pol_Rpb1_2. 1 hit. PF04983. RNA_pol_Rpb1_3. 1 hit. PF05000. RNA_pol_Rpb1_4. 1 hit. PF04998. RNA_pol_Rpb1_5. 1 hit. [Graphical view]
SMART	SM00663. RPOLA_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RPC1_DEBHA

Accession

Primary (citable) accession number: Q6BI69

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	December 16, 2008
Last modified:	November 16, 2011
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program