RPC1_PLAFA
ID RPC1_PLAFA Reviewed; 2339 AA.
AC P27625;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1656254; DOI=10.1016/0166-6851(91)90047-a;
RA Li W.B., Bzik D.J., Tanaka M., Gu H., Fox B.A., Inselburg J.;
RT "Characterization of the gene encoding the largest subunit of Plasmodium
RT falciparum RNA polymerase III.";
RL Mol. Biochem. Parasitol. 46:229-240(1991).
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; M73770; AAA29729.1; -; Genomic_DNA.
DR PIR; A45597; A45597.
DR AlphaFoldDB; P27625; -.
DR SMR; P27625; -.
DR PRIDE; P27625; -.
DR VEuPathDB; PlasmoDB:PF3D7_1329000; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000432100; -.
DR VEuPathDB; PlasmoDB:Pf7G8_130033500; -.
DR VEuPathDB; PlasmoDB:PfCD01_030023700; -.
DR VEuPathDB; PlasmoDB:PfDd2_130034900; -.
DR VEuPathDB; PlasmoDB:PfGA01_130035200; -.
DR VEuPathDB; PlasmoDB:PfGB4_130035000; -.
DR VEuPathDB; PlasmoDB:PfGN01_130035800; -.
DR VEuPathDB; PlasmoDB:PfHB3_130035400; -.
DR VEuPathDB; PlasmoDB:PfIT_130034300; -.
DR VEuPathDB; PlasmoDB:PfKE01_130034700; -.
DR VEuPathDB; PlasmoDB:PfKH01_130033300; -.
DR VEuPathDB; PlasmoDB:PfKH02_130032000; -.
DR VEuPathDB; PlasmoDB:PfML01_130032900; -.
DR VEuPathDB; PlasmoDB:PfNF135_130033900; -.
DR VEuPathDB; PlasmoDB:PfNF166_130034600; -.
DR VEuPathDB; PlasmoDB:PfNF54_030023200; -.
DR VEuPathDB; PlasmoDB:PfSD01_130035800; -.
DR VEuPathDB; PlasmoDB:PfSN01_130032100; -.
DR VEuPathDB; PlasmoDB:PfTG01_130034800; -.
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; 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; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 2.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
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..2339
FT /note="DNA-directed RNA polymerase III subunit RPC1"
FT /id="PRO_0000073949"
FT REGION 955..967
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT REGION 1503..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2038..2079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2058..2079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 611
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 613
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 615
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2339 AA; 272832 MW; EDD899363086FD48 CRC64;
MMKKKNIDIE ELKRLIEESS MKKRFVKDIK RNCEIKSIRF GIMSKEDIIK YSEVKIMNRE
MYKNNSGIPY PYGVLDLKLG AHKSNSVCET CNKKLINCSG HFGYIELNYP VFHIGYYKYI
IHILYCICKY CSSLLLSKEK IDFYCNLKKK STDDSFYKKH LFKRILNNCK KVNKCYICGN
PQGVIKKIIK PSLDQFMKLK HILKVKENGK MIIKEEDLNS LYVLKLFKNI NPYHVKLLNI
ENPEKLIITA LLVPPNTIRP SVIIDEHGTA EDDLTCILSE ITQLNNTIYN QCTNGYQTNQ
FLGNVEFLQL QITRFINSDS PAVSQLLATQ NISKPGRGIC QRLKGKEGRF RCNLSGKRVD
FSSRTVISPD PNISIDEVVI PKIIAMRLTY PETVNKYNID KLKMLIKNGC NKWPGANYII
KKSKKGTDPY SDISTSYNNN SNNISSIGCS NIFNVVNNYI NNNCKNVRYN IKDVNNNVLL
KDMCDINNMN NDINNNINNI YKNTSETNLC NVNNHNNNNN IYCNNQTQDN EEERKNSQFN
KISLKYANKN HVIQNLNIGD VVERHICDGD IVLFNRQPSL HRMSIMCHKA KIMDFKTFRF
NECVCSPYNA DFDGDEMNLD VPQTEEARAE ALYLMNVKHN LITPKNGEVI IALTQDFLSA
SYIITNKDTF LDRDTFCLLC SYFSDASLYI ELPIPAILKP KELWTGKQLI SVLIKPNKKE
NTIINFEIQE REYSNKFGDL KHLCLNDSYV CFYKSELICG SLGKKVLGSS KYGLFYYLIH
HNSSHIALKI MNRLSKLTSR YFSNKGMTIG IDDVRPSQTL TEKKKDLLLK GYEKVNNEII
LYNEKKMQIQ PGCTLEETLE IKVKSILDDL RNDAGKTCNQ YLHYLNKPLI MFNSGAKGAL
INIAQMIACV GQQNVAGQRI QNGFINRTLP HFHFHCKDSE SRGFVQNSFY TGLSPTEFFF
HTMSGREGLV DTAVKTAETG YMQRRLMKAL EDLSIHYDYS VRSCDKQIVQ FIYGDDALNP
SYIDNNNTYL DQFDKVFDHI VSISSSHLLL SYKNKIPYLP HVQHQNKTSN MNNIYNNMNN
INNNDSNRSI IYNNDSNMNN INNNDSNMNS IHNNNSNMNN IHNNDSNRSI IHNNDSNMNS
IHNNDSNMNS IHNNNSNMNN IHNNDSNRSI IHNNDSNMNS IHNNDSNNNN NYKDCTHNPY
ICNESLIIRN IMNRLIYQNI AQEDLFIPLE HDEFLVNKIM ESYTDQECNY EDIIRSLDLN
KNVSYIHNDQ GKHLSLQMCA EEHITINNTN NDNTYVEQIE MKELSKNKTK EKQSFKGTIR
DMHEDSEEQM NKFITKKAKF FIEKKKGKMH ECNDDIEYNN TQYDNIQYNN ISCNYIKSQN
LENTHHQVNN DLSFIKNNVI LPPKEYHSIF HFVNDYRNVV EIKNLMDKKK IFLNNSEKNV
VQSKYNRMSK NLKKKIEIIN NIYRNEKKKL NRWKTKMDND DNYWSSDDDS IIAKKIIKIK
NKEKRKYHPK EEKENFDRNN YKMITDNNNN DNNNNNNDNN NNDNNNNNNN SNNNNYYYNL
HDDVNNLGVT NYNTNIYPND CNGIYEKETN NNELTTNSNM CDKNNDFSDE FFNNINENDL
LYDNKYYRQI FKNVIGFVSV FEYVESYKQH YILFPYEIIK WTSFLLEYLT EIIPTNIFLH
TKLSKKEKPT HQKNTGKMKI YIEEIKKWLF IKAINIYKYF SFKKSIELIK KKDYFNYIIK
NYDISHRYII HDYSFINLKQ LYLFIFFNIY KYFKYISTPG DAVGSISAQS IGEPGTQMTL
KTFHFAGVAS MNVTLGVPRI KEIINASNSI QTPILNIPLE VNDNYNFALM MKSKLEKTTI
RDICMYIKED YTSRGVFLSV KFNEELIQKL FLNINAYNIK DIILKQSHIN KIKINKIHIN
VINKYKLHIS LKNDEFIFFQ MESLKKGLLD LLIYGDKDIK RCIIKKEDIE VTDNEDEICD
DMDEYYNVSQ GTELYERKCN SKEENKNAIR VKKEEIDDNL EKEENIIYVS EKDSVNQLKS
EKKKDINDDN NNNDDNNNNN DDDNKINDTI FNDDIDSDRN NLKENGSKLE NVGEHIIERL
SYKMKEKNVK KEHIKKEPNL INLDTINLDT LNFDEINVHN INNEKIEFYD EHLNICQGNK
KHIQKKKKKK TVYSILVEGN SLNYVLGLEG VDFKHIISNH VINVFQVLGI EAARITIINE
IKKCVEAYSI DIDIRHIMLL ADIMAFTGDI LGINRFGIQK ARQSTLMLAS FEETNEHLFV
SSFFKNVDEI NNISESIIVG KNIPIGTGAF QLLYDYKLEK ETKNLTLLEK AERETAMNY
