RPC1_DEBHA
ID RPC1_DEBHA Reviewed; 1457 AA.
AC Q6BI69;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC1;
DE Short=RNA polymerase III subunit C1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase III largest subunit;
GN Name=RPC1; OrderedLocusNames=DEHA2G12980g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic core component of RNA polymerase III which
CC synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase
CC active center together with the second largest subunit. A single-
CC stranded DNA template strand of the promoter is positioned within the
CC central active site cleft of Pol III. A bridging helix emanates from
CC RPC1 and crosses the cleft near the catalytic site and is thought to
CC promote translocation of Pol III by acting as a ratchet that moves the
CC RNA-DNA hybrid through the active site by switching from straight to
CC bent conformations at each step of nucleotide addition (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6;
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; CR382139; CAG90588.2; -; Genomic_DNA.
DR RefSeq; XP_462102.2; XM_462102.1.
DR AlphaFoldDB; Q6BI69; -.
DR SMR; Q6BI69; -.
DR STRING; 4959.XP_462102.2; -.
DR EnsemblFungi; CAG90588; CAG90588; DEHA2G12980g.
DR GeneID; 2905015; -.
DR KEGG; dha:DEHA2G12980g; -.
DR VEuPathDB; FungiDB:DEHA2G12980g; -.
DR eggNOG; KOG0261; Eukaryota.
DR HOGENOM; CLU_000487_3_0_1; -.
DR InParanoid; Q6BI69; -.
DR OMA; AVCPPYN; -.
DR OrthoDB; 591636at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..1457
FT /note="DNA-directed RNA polymerase III subunit RPC1"
FT /id="PRO_0000073952"
FT REGION 854..866
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1457 AA; 162213 MW; 36612BF648F639D3 CRC64;
MKEVVVDVAP KCIKGIEFGA LSAKDIIAQS EVEVHTRDLY DLEKGRIPKD GGALDTKMGI
SSNANECATC HGNLASCHGH FGHIKLALPV FHVGYFKATI QVLQCICKNC SAVLLDEQTK
RSFLNDLRRP HIDNLRRMKI LKKLLEQCKK QRRCLNCNHV NGVVKKAASG AGPAALKIVH
DTFRWIGKKA TPEKDLWDKE FDEVFSRNPE LEKFVKRIHD DLNPLKVLNL FKQISPSDCE
LLGIDSARGG RPEMYIWRYL PAPPVCIRPS VMMDAQSNED DLTIKLTEIV WTSSLIKAGI
EKGISINNLM EQWDYLQLSV AMYINSDSAN PALLPSSGGG SKSSKPIRGF CQRLKGKQGR
FRGNLSGKRV DFSGRTVISP DPNLKIDEVA VPDRVAKVLT YPEKCTRYNR KKLQKLILSG
PNVHPGANYL LKQNESAKRN LRFGDRVKLA KNLHIGDVVE RHIEDGDIVL FNRQPSLHRL
SILSHYAKIR PWRTFRLNEC VCTPYNADFD GDEMNIHVPQ TEEARAEAIN LMGVKNNLLT
PKSGEPIIAA TQDFITGSYL VSHKDSFFDR ASLVQLLCMM SDADIQFDIP PPAIFKPVML
WTGKQVFSLL IKPNKKSNVV INLDAKNKTY TPPAKGFPNE MSPNDGFVII RGSQILSGVM
DKSTLGDGKK HSVFYTILRD YGPDEAANAM NRMAKLCARY LGNRGFSIGI NDVIPGSDLK
QKKELMVEQA YLKCDELIDL YNRGNLETQP GCNEEQTLEA KIGGLLSKVR EEVGEICINE
LDSANAPLIM ATCGSKGSTL NVSQMVAVVG QQIISGNRVP DGFQDRSLPH FTKNSKTPQS
KGFVRNSFFS GLTPPEFLFH SISGREGLVD TAVKTAETGY MSRRLMKSLD DLSAQYDHTV
RNSSNGIVQF TYGGDGLDPF DMEGDARPVN FVRQWDHAYN ITFDIEDKGL LPYQIIELVD
SILHPLEDRL VRYDNVGKII PLEDSDKIEY IDQNDAEREF YQSIREFTTN KATKLAEIRE
KKMLKPFLTE PAEDFIRLDE SDESLVAINQ LSKVSANSIN KFLEQCIYKY SRAKVEPGTA
VGAIGAQSIG EPGTQMTLKT FHFAGVASMN VTLGVPRIKE IINASKVIST PIINSVLVND
DDEIAARVVK GRVEKTLLED VAYFIEDVYK NNMAYLSIKI DLNTIEKLQL ELNIESIAHS
IANAPKLKIL AGDVSVTGKD RINVLVTLRE PKSINLMKNA SADYKGTDAS IVNSLFFRMQ
HLKRALPRIC IKGLPDISRA VINIRDDGKK ELLVEGYGLK EVMSTDGVVG TKTSTNHILE
VFQVLGIEAA RASIIGEIDY TMSKHGMSVD PRHIQLLGDV MTYKGEVLGI TRFGLSKMRD
SVLQLASFEK TTDHLFDASF YMKNDKIEGV SECIILGQTM NIGTGAFKLV NSFDVDKKAL
EMKPTLFEGM CEVSATA
