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Protein

DNA-directed RNA polymerase III subunit rpc1

Gene

rpc1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi66 – 661Zinc 1By similarity
Metal bindingi69 – 691Zinc 1By similarity
Metal bindingi76 – 761Zinc 1By similarity
Metal bindingi79 – 791Zinc 1By similarity
Metal bindingi106 – 1061Zinc 2By similarity
Metal bindingi109 – 1091Zinc 2By similarity
Metal bindingi153 – 1531Zinc 2By similarity
Metal bindingi493 – 4931Magnesium; catalyticBy similarity
Metal bindingi495 – 4951Magnesium; catalyticBy similarity
Metal bindingi497 – 4971Magnesium; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Transcription

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-1834949. Cytosolic sensors of pathogen-associated DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase III subunit rpc1 (EC:2.7.7.6)
Short name:
RNA polymerase III subunit C1
Alternative name(s):
DNA-directed RNA polymerase III largest subunit
RPC158
Gene namesi
Name:rpc1
ORF Names:SPBC651.08c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC651.08c.
PomBaseiSPBC651.08c. rpc1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • DNA-directed RNA polymerase III complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14051405DNA-directed RNA polymerase III subunit rpc1PRO_0000073951Add
BLAST

Proteomic databases

MaxQBiO94666.

Interactioni

Subunit structurei

Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.By similarity

Protein-protein interaction databases

BioGridi277609. 3 interactions.
MINTiMINT-4686028.

Structurei

3D structure databases

ProteinModelPortaliO94666.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni838 – 85013Bridging helixBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1381 – 13855Poly-Glu

Sequence similaritiesi

Belongs to the RNA polymerase beta' chain family.Curated

Phylogenomic databases

HOGENOMiHOG000222974.
InParanoidiO94666.
KOiK03018.
OMAiGEDLCAN.
OrthoDBiEOG780RVQ.
PhylomeDBiO94666.

Family and domain databases

InterProiIPR000722. 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]
PfamiPF04997. 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]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94666-1 [UniParc]FASTAAdd to basket

« Hide

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

LEITA
Length:1,405
Mass (Da):157,562
Last modified:May 1, 1999 - v1
Checksum:i104B1AC4145A3B7B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ156227 mRNA. Translation: ABA54855.1.
CU329671 Genomic DNA. Translation: CAB37604.1.
PIRiT40607.
RefSeqiNP_595506.1. NM_001021416.2.

Genome annotation databases

EnsemblFungiiSPBC651.08c.1; SPBC651.08c.1:pep; SPBC651.08c.
GeneIDi2541094.
KEGGispo:SPBC651.08c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ156227 mRNA. Translation: ABA54855.1.
CU329671 Genomic DNA. Translation: CAB37604.1.
PIRiT40607.
RefSeqiNP_595506.1. NM_001021416.2.

3D structure databases

ProteinModelPortaliO94666.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277609. 3 interactions.
MINTiMINT-4686028.

Proteomic databases

MaxQBiO94666.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC651.08c.1; SPBC651.08c.1:pep; SPBC651.08c.
GeneIDi2541094.
KEGGispo:SPBC651.08c.

Organism-specific databases

EuPathDBiFungiDB:SPBC651.08c.
PomBaseiSPBC651.08c. rpc1.

Phylogenomic databases

HOGENOMiHOG000222974.
InParanoidiO94666.
KOiK03018.
OMAiGEDLCAN.
OrthoDBiEOG780RVQ.
PhylomeDBiO94666.

Enzyme and pathway databases

ReactomeiR-SPO-1834949. Cytosolic sensors of pathogen-associated DNA.

Miscellaneous databases

PROiO94666.

Family and domain databases

InterProiIPR000722. 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]
PfamiPF04997. 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]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 972 / ATCC 24843.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiRPC1_SCHPO
AccessioniPrimary (citable) accession number: O94666
Secondary accession number(s): Q0QYE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.