Reviewed, UniProtKB/Swiss-Prot O94666 (RPC1_SCHPO)

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
    RPC158

Gene names

Name:	rpc1
ORF Names:	SPBC651.08c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	1405 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. 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
Domain	Zinc-finger
Ligand	Magnesium 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	cytoplasm Inferred from direct assay. Source: GeneDB_SPombe 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 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 – 1405	1405	DNA-directed RNA polymerase III subunit rpc1		PRO_0000073951
Regions
	Zinc finger	66 – 79	14	C3H1-type Potential
	Region	838 – 850	13	Bridging helix By similarity
	Compositional bias	1381 – 1385	5	Poly-Glu
Sites
	Metal binding	66	1	Zinc 1 By similarity
	Metal binding	69	1	Zinc 1 By similarity
	Metal binding	76	1	Zinc 1 By similarity
	Metal binding	79	1	Zinc 1 By similarity
	Metal binding	106	1	Zinc 2 By similarity
	Metal binding	109	1	Zinc 2 By similarity
	Metal binding	153	1	Zinc 2 By similarity
	Metal binding	493	1	Magnesium; catalytic By similarity
	Metal binding	495	1	Magnesium; catalytic By similarity
	Metal binding	497	1	Magnesium; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	O94666-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 104B1AC4145A3B7B	FASTA	1,405	157,562
	10 20 30 40 50 60 MKDPIDDQIP KRIKHLQFGI NGPEEFVKDG TVEVSRRDLY TMTDRSPAEH GALDLHMGTS 70 80 90 100 110 120 NKQINCATCG ESMADCMGHF GYVKLALPVF HIGYFKATLT ILQNICKDCS SVLLSDQEKR 130 140 150 160 170 180 QFLKDLRRPG IDNLRRSQIC KRINDHCKKM RRCSKCDAMQ GVVKKAGPLK IIHERFRYVR 190 200 210 220 230 240 KSQDDEENFR HSFDEALKTI PELKMHLSKA HDDLNPLKVL NLFKQITPVD CELLGMDPEH 250 260 270 280 290 300 GRPENLLWRY VPAPPVCIRP SVAQEGATTE DDLTVKITEI IWTSSLIRAA LSKGTPISNL 310 320 330 340 350 360 MEQWEFMQLS IAMYINSEMP GLRPSDMPSK PIRGFCQRLK GKQGRFRGNL SGKRVDFSGR 370 380 390 400 410 420 TVISPDPNLR IDQVAVPYRI AKILTFPERV TTQNKKHLQD CIRNGPDVHP GANYVIDRES 430 440 450 460 470 480 GFKRFLRFGN RNRIADDLKI GDIVERHLHD NDVVLFNRQP SLHKLSIMAH LVKVRPWRTL 490 500 510 520 530 540 RFNECVCGPY NADFDGDEMN LHVPQTEEAK TEALELMGIK NNLVSPRNGE PIIAATQDFI 550 560 570 580 590 600 TAAYLLSLKD TFLDRKSISN ICCYMMDAST HIDLPPPAII KPRCLWTGKQ VFTVLMKPNR 610 620 630 640 650 660 FSKVLVNLDA KTRSFSRIKS KTPEMCPKDG YLMIRNSEII AGVVDKSVVG DGKKDSLFYV 670 680 690 700 710 720 ILRDYGALEA AEAITRLSKM CARFLGNRGF SIGIEDVQPG KSLSSQKEIL VNKAYATSDD 730 740 750 760 770 780 FIMQYAKGIL ECQPGMDQEA TLEAKISSTL SKVRDDVGEI CMDELGPANS PLIMATCGSK 790 800 810 820 830 840 GSKINVSQMV ACVGQQIISG KRVPDGFQDR SLPHFHKNSK HPLAKGFVSN SFYSGLTPTE 850 860 870 880 890 900 FLFHAISGRE GLVDTAVKTA ETGYMSRRLM KSLEDLSSAY DGTVRSSNSD VVQFVYGDDG 910 920 930 940 950 960 LDPTYMEGDG QAVEFKRTWI HSVNLNYDRH DSAMLPYEII DYVNRALDDP KFLTNCNRDF 970 980 990 1000 1010 1020 IETIRTFVIE NIAKYLASVR ERRDLAPMLE EPDMDDLDDM EGDEFAPVAK RKSVENIIRV 1030 1040 1050 1060 1070 1080 TEKQLRSFVD RCWEKYMRAK VEPGTAVGAI GAQSIGEPGT QMTLKTFHFA GVAAQTTLGV 1090 1100 1110 1120 1130 1140 PRIKEIINAA KTISTPIITG QLINDRDERS ARVVKGRIEK TYLKDVTSYI EEVYGPVTTY 1150 1160 1170 1180 1190 1200 LSIQVNFDTI SKLQLDITLA DIAAAIWNTP KLKIPSQQVT VNNTLQQIHV HTSSDGKSSE 1210 1220 1230 1240 1250 1260 TEVYYRLQTY KRVLPDVVVA GIPTINRSVI NQESGKIELF MEGTGLQAVM NTEGIVGTKT 1270 1280 1290 1300 1310 1320 STNHVMEMKD VLGIEAARYS IISEIGYTMA KHGLTVDPRH IMLLGDVMTC KGEVLGITRF 1330 1340 1350 1360 1370 1380 GVAKMKDSVL ALASFEKTTD HLFNAAARFA KDSIEGISEC IVLGKLAPIG TNVFQLIRRT 1390 1400 EEEEEQKPKE LLFDTPSLHQ LEITA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ancient origin, functional conservation and fast evolution of DNA-dependent RNA polymerase III." Proshkina G.M., Shematorova E.K., Proshkin S.A., Zaros C., Thuriaux P., Shpakovski G.V. Nucleic Acids Res. 34:3615-3624(2006) [PubMed: 16877568] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 38366 / 972.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ156227 mRNA. Translation: ABA54855.1. CU329671 Genomic DNA. Translation: CAB37604.1.
PIR	T40607.
RefSeq	NP_595506.1.
3D structure databases
HSSP	HSSP built from PDB template 1I6H based on UniProtKB P04050.
ModBase	Search...
Protein-protein interaction databases
STRING	O94666.
Genome annotation databases
GeneID	2541094.
GenomeReviews	Gene locus rpc1 in contig CU329671_GR.
KEGG	spo:SPBC651.08c.
NMPDR	fig|4896.1.peg.1372.
Organism-specific databases
GeneDB_Spombe	SPBC651.08c.
Phylogenomic databases
OMA	CCQDSFL.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003567-MON.
BRENDA	2.7.7.6. 653.
Gene expression databases
ArrayExpress	O94666.
Family and domain databases
InterPro	IPR015700. DNA-dir_RNA_pol3_lsu. IPR000722. RNA_pol_asu. 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]
Gene3D	G3DSA:2.40.40.30. RNA_pol_A. 1 hit. G3DSA:3.90.1120.10. RNA_pol_Rpb1_1. 1 hit.
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_SCHPO

Accession

Primary (citable) accession number: O94666
Secondary accession number(s): Q0QYE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)