RPA2_EUPOC
ID RPA2_EUPOC Reviewed; 1166 AA.
AC P28365;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA2;
DE Short=RNA polymerase I subunit 2;
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:P22138};
GN Name=RPA2;
OS Euplotoides octocarinatus (Freshwater ciliate) (Euplotes octocarinatus).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Hypotrichia; Euplotida; Euplotidae; Euplotes.
OX NCBI_TaxID=2716877;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=(68)-VIII;
RX PubMed=1461731; DOI=10.1093/nar/20.22.5985;
RA Kaufmann J., Florian V., Klein A.;
RT "TGA cysteine codons and intron sequences in conserved and nonconserved
RT positions are found in macronuclear RNA polymerase genes of Euplotes
RT octocarinatus.";
RL Nucleic Acids Res. 20:5985-5989(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-546.
RC STRAIN=(68)-VIII;
RX PubMed=1408746; DOI=10.1093/nar/20.17.4445;
RA Kaufmann J., Klein A.;
RT "Gene dosage as a possible major determinant for equal expression levels of
RT genes encoding RNA polymerase subunits in the hypotrichous ciliate Euplotes
RT octocarinatus.";
RL Nucleic Acids Res. 20:4445-4450(1992).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Second largest core component of RNA polymerase I which synthesizes
CC ribosomal RNA precursors. Proposed to contribute to the polymerase
CC catalytic activity and forms the polymerase active center together with
CC the largest subunit. Pol I is composed of mobile elements and RPA2 is
CC part of the core element with the central large cleft and probably a
CC clamp element that moves to open and close the cleft (By similarity).
CC {ECO:0000250|UniProtKB:P22138}.
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; Evidence={ECO:0000250|UniProtKB:P22138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC Evidence={ECO:0000250|UniProtKB:P22138};
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000250|UniProtKB:P22138}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P22138}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; X66451; CAA47067.1; -; Genomic_DNA.
DR PIR; S70413; S70413.
DR AlphaFoldDB; P28365; -.
DR SMR; P28365; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; 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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR009674; Rpa2_dom_4.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF06883; RNA_pol_Rpa2_4; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Nucleus; Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1166
FT /note="DNA-directed RNA polymerase I subunit RPA2"
FT /id="PRO_0000048076"
FT ZN_FING 1081..1130
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P22138"
SQ SEQUENCE 1166 AA; 132714 MW; 7253965D6173F0C9 CRC64;
MKTNAKFDRK EISKIYKNIA RHHIDSFDFA MSTCLNRACE HMLPFDYIVP EESASCGFKK
LTLWYDSFEL GQPSLGEIDY DSHILYPSEC RQRKMTYTIP LFATIFKKFD DEMVDNFKVK
LGDIPTMGRK KFCNLKGLTK KELAKRGEDM LEFGGYFIVN GNEKVIRMLI VPKRNFPIAF
KRSKFLERGK DFTDYGVQMR CVRDDFTAQT ITLTYLSDGS VSLRLIYQKQ EFLIPIILIL
KALKNCTDRQ IYERIVKGNF NQRQISDRVE AILAVGKDLN IYDSDQSKAL IGSRFRIVLA
GITSETSDID AGDLFLSKHI CIHTDSYEAK FDTLILMIDK LYASVANEVE LDNLDSVAMQ
DVLLGGHLYL QILSEKLFDC LHINLRARLN KELKRHNFDP MKFRDVLTNQ KINCGIGLIG
KRMENFLATG NLISRTNLDL MQTSGFCIIG DKLNNIRFLS HFRSIHRGQY FAEQKTTSVR
KLLPESWGFI CPVHTPDGAP CGLLNHISMS CVPIGSEEKQ IDIDKFRNIL GELGMNSISS
DLCLNYHTGY YPVIFDGIHL GYVEKDIGES FVEGLRYLKC TQSQPDYAIP RTLEIAFIPF
SGYSRNLQWP GIFLASTPAR FTRPVKNLHY NCIEWISPLE QMNLSIACTD EDITPETTHQ
ELDPINILSI VASVGVFAEY NQSPRNMYQC QMAKQTMGTP YHNHQFRTDN KIYRLLFPHR
PIVKTRTQVD FDIEEYPSGT NAVVAVISYT GYDLEDAMII NKSSYERGFG HGVVYKSYTH
DLNESNSQST RGIKSSVRYK FLNNVSQKDK SKIKLENIDP DGLPKIGSQL TKGKPELCIF
DTLKRGAKLS KFKDSEKARI ETVRVCGNDD KNPDNLSIGY TIRYSRIPVI GDKFSSRHGQ
KGVLSVLWPQ VDMPFTENGI TPDLIINPHA FPSRMTMGML IQSMAAKSGS LRGEFKTVET
FQRYDDNDIV GHFGKELLDK GFNYHGNELM YSGIFGTPLK ADIFIGVVYY QRLRHMVSDK
SQARGTGPID ILTHQPVKGR KKGGGIRFGE MERDSLLAHG AAYCLNDRLF RSSDYSEGFV
CQNCGSILSC YVNRAIMKTQ TFIPPSLDES NKDTEDKEIH MNEKVICKVC KKNSNCKKVA
LPFVLRFLAN ELASMGIKLK FTVNDF
