RPC1_TRYBB
ID RPC1_TRYBB Reviewed; 1530 AA.
AC P08968;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 111.
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;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=427 / Isolate MITat 1.2A;
RX PubMed=3174432; DOI=10.1093/nar/16.18.8753;
RA Cornelissen A.W.C.A., Evers R., Koeck J.;
RT "Structure and sequence of the gene for the largest subunit of trypanosomal
RT RNA polymerase III.";
RL Nucleic Acids Res. 16:8753-8772(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2808366; DOI=10.1016/s0021-9258(19)84682-3;
RA Smith J.L., Levin J.R., Agabian N.;
RT "Molecular characterization of the Trypanosoma brucei RNA polymerase I and
RT III largest subunit genes.";
RL J. Biol. Chem. 264:18091-18099(1989).
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; X12494; CAA31014.1; -; Genomic_DNA.
DR EMBL; M27163; AAA30233.1; -; Genomic_DNA.
DR PIR; S01393; S01393.
DR AlphaFoldDB; P08968; -.
DR SMR; P08968; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:GeneDB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISA:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; ISA:GeneDB.
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; Transcription; Transferase; Zinc.
FT CHAIN 1..1530
FT /note="DNA-directed RNA polymerase III subunit RPC1"
FT /id="PRO_0000073950"
FT REGION 846..858
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT REGION 992..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
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 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 1325
FT /note="D -> E (in Ref. 2; AAA30233)"
FT /evidence="ECO:0000305"
FT CONFLICT 1493
FT /note="I -> V (in Ref. 2; AAA30233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1530 AA; 170272 MW; FC03D700CEF9D742 CRC64;
MLKGSSSTSF LLPQQFVEPL PHAPVEISAL HYGLLSRNDV HRLSVLPCRR VVGDVKEYGV
NDARLGVCDR LSICETCGLN SIECVGHPGH IDLEAPVFHL GFFTTVLRIC RTICKRCSHV
LLDDTEIDYY KRRLSSSSLE PLQRTMLIKT IQTDAYKTRV CLKCGGLNGV VRRVRPMRLV
HEKYHVEPRR GEGPRENPGG FFDAELRTAC AYNKVVGECR EFVHDFLDPV RVRQLFLAVP
PGEVILLGLA PGVSPTDLLM TTLLVPPVPV RPRGCAGTTT VRDDDLTAQY NDILVSTDTM
QDGSLDATRY TETWEMLQMR AARLLDSSLP GFPPNVRTSD LKSYAQRLKS KHGRFRCNLS
GKRVDYSGRS VISPDPNLDV DELAVPLHVA RVLTYPQRVF KANHELMRRL VRNGPHVHPG
ATTVYLAQEG SKKSLKNERD RHRLAARLAV GDIVERHVMN GDLVLFNRQP SLHRVSMMAH
RARVLPFRTF RFNECCCAPY NADFDGDEMN VHFVQTEKAR AEALQLMSTA RNIISAKNGE
PIIACTQDFL AAAYLVTSRD VFFDRGEFSQ MVSHWLGPVT QFRLPIPAIL KPVELWTGKQ
LFELIVRPSP EVDVLLSFEA PTKFYTRKGK HDCAEEGYVA FLDSCFISGR LDKKLLGGGA
KDGLFARLHT IAGGGYTARV MSRIAQFTSR YLTNYGFSLG LGDVAPTPEL NKQKAAVLAR
SVEVCDGLIK SAKTGRMIPL PGLTVKQSLE ARLNTELSKV RDECGTAAVQ TLSIHNNTPL
IMVQSGSKGS ALNIAQMMAC VGQQTVSGKR ILDAFQDRSL PHFHRFEEAP AARGFVANSF
YSGLSPTEFF FHTMAGREGL VDTAVKTAET GYIYRRLMKA MENLSVRYDG TVRNTKGDVI
QLRFGEDGLD PQLMEGNSGT PLNLEQEWLS VRAAYARWVV GLLAGSKTAS DGNAIRDNEN
YFNEFISMLP TEGPSFVEAC LNGDQEALKV CEEQESREDA LHNSNGKTND RESRPRTGRL
RRAVLISHLV KVCSRKFKDD IQDFFVKKVR EQQRIRNLLN LPNTSRERTE GGGDNSGPIA
NKRTKKRAPS LKVKDSKEGG RVSELRDLEM LQTELLPLTR GMVTRFIAQC ASKYLRKACE
PGTPCGAIAA QSVGEPSTQM TLRTFHFAGV ASMSITQGVP RLVEVINANR NIATPVVTAP
VLLMEGEENH CEIFRKRARF VKAQIERVLL REVVSEIVEV CSDTEFYLRV HLNMSVITKL
HLPINAITVR QRILAAAGHT MSPLRMLNED CIEVFSLDTL AVYPHFQDAR WVHFSLRRIL
GLLPDVVVGG IGGINRAMIS SNGTEVLAEG AELRAVMNLW GVDSTRVVCN HVAVVERVLG
IEAARRVIVD EIQNILKAYS LSIDVRHVYL LADLMTQRGV VLGITRYGIQ KMNFNVLTMA
SFERTTDHLY NAAATQRVDR DLSVSDSIIV GKPVPLGTTS FDLLLDGSIS NDILPPQRCV
KRGMGPNFHT AKRHHLVPLA AEGVFRLDLF
