RPC1_GIAIN
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 03-AUG-2022, entry version 100.
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=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; X60325; CAA42895.1; -; Genomic_DNA.
DR PIR; S22812; S22812.
DR RefSeq; XP_001709578.1; XM_001709526.1.
DR AlphaFoldDB; P25202; -.
DR SMR; P25202; -.
DR GeneID; 5702502; -.
DR KEGG; gla:GL50803_0016223; -.
DR VEuPathDB; GiardiaDB:DHA2_16223; -.
DR VEuPathDB; GiardiaDB:GL50581_540; -.
DR VEuPathDB; GiardiaDB:GL50803_0016223; -.
DR eggNOG; KOG0261; Eukaryota.
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 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; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 2.
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.
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
