ID RPC1_GIAIN Reviewed; 1741 AA. AC P25202; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 04-NOV-2026, entry version 113. 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; DE AltName: Full=RNA polymerase III subunit C160; GN Name=RPOA3; OS Giardia intestinalis (Giardia lamblia). OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia. OX NCBI_TaxID=5741; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=SSP. P1; RX PubMed=1549483; DOI=10.1093/nar/20.5.1145; RA Lanzendoerfer M., Palm P., Grampp B., Peattie D.A., Zillig W.; RT "Nucleotide sequence of the gene encoding the largest subunit of the DNA- RT dependent RNA polymerase III of Giardia lamblia."; RL Nucleic Acids Res. 20:1145-1145(1992). 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=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + CC diphosphate; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X60325; CAA42895.1; -; Genomic_DNA. DR PIR; S22812; S22812. DR RefSeq; XP_001709578.1; XM_001709526.1. DR AlphaFoldDB; P25202; -. DR SMR; P25202; -. DR EnsemblProtists; GL50803_0016223_t1; KAE8303672.1; GL50803_0016223. DR KEGG; gla:GL50803_0016223; -. DR VEuPathDB; GiardiaDB:DHA2_16223; -. DR VEuPathDB; GiardiaDB:GL50581_540; -. DR VEuPathDB; GiardiaDB:GL50803_0016223; -. DR VEuPathDB; GiardiaDB:QR46_4079; -. DR eggNOG; KOG0261; Eukaryota. DR OMA; AAATFMN; -. DR OrthoDB; 270392at2759; -. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-ARBA. 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 RNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR CDD; cd02736; RNAP_III_Rpc1_C; 1. DR FunFam; 2.40.40.20:FF:000019; DNA-directed RNA polymerase II subunit RPB1; 1. DR FunFam; 1.10.150.390:FF:000004; DNA-directed RNA polymerase subunit; 1. DR FunFam; 1.10.274.100:FF:000024; DNA-directed RNA polymerase subunit; 1. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 1.10.150.390; -; 1. DR Gene3D; 2.40.40.20; -; 2. DR Gene3D; 6.10.250.2940; -; 1. DR Gene3D; 6.20.50.80; -; 1. DR Gene3D; 3.30.1490.180; RNA polymerase ii; 2. DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1. DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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; IPR038120; Rpb1_funnel_sf. DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1. DR PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 1. DR Pfam; PF04997; RNA_pol_Rpb1_1; 2. DR Pfam; PF00623; RNA_pol_Rpb1_2; 2. 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. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. PE 3: Inferred from homology; KW DNA-directed RNA polymerase; Magnesium; Metal-binding; KW Nucleotidyltransferase; Nucleus; Transcription; Transferase; Zinc. FT CHAIN 1..1741 FT /note="DNA-directed RNA polymerase III subunit RPC1" FT /id="PRO_0000073948" FT REGION 1099..1111 FT /note="Bridging helix" FT /evidence="ECO:0000250" FT REGION 1719..1741 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 79 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 82 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 89 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 122 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 160 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 722 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 724 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 726 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" SQ SEQUENCE 1741 AA; 193929 MW; DE2EF212CBCF6CD8 CRC64; MEPNRRLRYF RSEIPQPVTE HRFPKRVEKL VFSVLSSNAL MKLSEVQITT PILYEHYPSP ATNGVLDKRL GLSDKVGKCA TCGKDTKMCI GHFGTISLAL PVFHPGLIND ARTMLSIVCP FCSRVKISEA DRLKYKVLNH KFSLAIVKEA QEQAKKQVNC PFCHAPSTIC KKSQGFRVLR EMHYEERATK ILADVIKHQK DIEKIQELDQ RLRNHVVDPI QALHILQKVP ECDYPYLGIP WQSRNVYASQ QTPDSIASND ASQLFSRGSS KLLARTASRF IAQHQGISDR ATRLTSHAFL TRPQDVILTH IPVPPSCLRP SVQSGSGAGT TEDNLTSHLV RILTINDKLK EAMVSGAVAT SKVYAKWDQL NMDVSLLYIG KIPGGVQPVK NKTDSGTKEG TGIIDRLKGK AGRFRSNLSG KRVNFSGRTV ISPNPYLSMQ QVAIPRLIAQ NLTFPEIVTS RNIRFLRELI LNGKTYPGAN EVLLLNDTIR YNPALKRLGI DVKQSRDMEA KAMELVSRCV DTFNLNSLCA DLPELQAAIQ HLVSESSNAI NSELKAEDLP QNQPLFAKEV YDPAQKGESN NIDNNVCEID ELKLEDTADY QVGESAGQAS TVAVEQPPES RTVLKLNSIA SLQLTNASSQ HLSTFKLNTV SLLQKDRRGR QAIANSLRPN DIVYRHLLPN DTLLFNRQPS LHRMSIMQFN AVIHENRTFS FNPVVCSPFN ADFDGDEMNI FYMQGQEARA EAGILMGSHE NIISPRHGEC MIGLTQDFLT GIYLLSGKGI FMTRQEYCQH VSYGCDGFGD ATYGVSLYNY GREFIKSIHD RRGTEEDTVG FVKVPCLSQP CIVYPRQLYS GKQVLSVLMK GNDFDSVNIN LEHGDKTYKK DSDRRALSVN DDYIIIQNSE HLVGRLTKTF LASSKNCIFY FLVQNYGPVS AARIMLRFAK VAARFLMNYG FTIGIDDVMP SQRVLGKKEV IVQEGYEKAQ EKIRDYESGK LEAIPGSTVQ ETLEATLNQI LSNVRESCAQ IALKELHFTN KPLIMSLCGS KGSPINIAQM IIILGQQSFG GSRAPDDFYT RSTPYFYHYS KEPNAKGFIL NSFYTGLLPF EFLAHARAGR DGVIDSACKT ADTGYLQRRL VKCLEDLSVS YDFTVRNSKK SVVQFRFGHD GFDPIKLEVG TGQCFDLDTL LRHIILLNRS QDLAEGAFPV LLDRYKAEAE LDVLLNKDFY GQEACLIERS NVTSYFQQSI LPKLTTNTHI ATTVAPALAA SFLQTTLTKK DIDDFLRQVR RKYIRLNLEP GSPCGAVAAQ SVGEPSTQMT LKSFHHAGLA SMNITQGVPR LKEIVDGVVK ISTPITTVEL HVDVDKEELA ATVTEKYLEK ARMMKNIIEC TYLGQISASI IECYSQSVCH IEVNLDMKII ADMGLAGIIT VETVVASILH NDKAKKLVGQ DQSSGSVSIH SATRFSVRPL TQSRDDLLFD IQSLKLLLPM IPVSGISTCS RAVINEYKEF CQGATSSAPL TKYNLLVEGI GLQNILNVSG IDFTRTLSNN IVEVANTLGI EAAVATISNE IKACMDSHGM AVDMRHIRLL ADIMCFRGRV LGFTRFGLTK MKADSVIMLA SFEKTGEHLF NAALGNKVDE ANGVTESIIL GKPMSMGTGS FSLLQAPYFD EKTGKTIEYQ PKQTTRFLGE VLNKQYDEEV DAIVNAFWYD EKLYLTGAEA KAKLLRGRRH ANKRSWSRGK ERHASLKPKN R //