ID   RPA2_ASHGO              Reviewed;        1196 AA.
AC   Q75DS1;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=DNA-directed RNA polymerase I subunit RPA2;
DE            EC=2.7.7.6 {ECO:0000250|UniProtKB:P22138};
DE   AltName: Full=DNA-directed RNA polymerase I polypeptide 2;
DE            Short=RNA polymerase I subunit 2;
GN   Name=RPA2; OrderedLocusNames=ABR029W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 674-688 AND 700-712.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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 14 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; AE016815; AAS50799.2; -; Genomic_DNA.
DR   RefSeq; NP_982975.2; NM_208328.2.
DR   AlphaFoldDB; Q75DS1; -.
DR   SMR; Q75DS1; -.
DR   STRING; 33169.AAS50799; -.
DR   PRIDE; Q75DS1; -.
DR   EnsemblFungi; AAS50799; AAS50799; AGOS_ABR029W.
DR   GeneID; 4618998; -.
DR   KEGG; ago:AGOS_ABR029W; -.
DR   eggNOG; KOG0216; Eukaryota.
DR   HOGENOM; CLU_000524_5_1_1; -.
DR   InParanoid; Q75DS1; -.
DR   OMA; FFGVVHY; -.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0001054; F:RNA polymerase I activity; IEA:EnsemblFungi.
DR   GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IEA:EnsemblFungi.
DR   GO; GO:0006363; P:termination of RNA polymerase I transcription; IEA:EnsemblFungi.
DR   GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IEA:EnsemblFungi.
DR   GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IEA:EnsemblFungi.
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; Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1196
FT                   /note="DNA-directed RNA polymerase I subunit RPA2"
FT                   /id="PRO_0000048077"
FT   ZN_FING         1097..1124
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P22138"
SQ   SEQUENCE   1196 AA;  134285 MW;  170B79555B3506BF CRC64;
     MSVMEPLSAN RTAQFRTLER EARFVSPPKD KSAYPLLYEA VEPHVGSFNA LTEGPGGGLL
     NLGARDIGAK VVFDGKASDE NPNYLGNKLA LSVTQVSLTK PMSNDGVTAA AERNVFPAEA
     RKRLTTYRGK LLLKLNWSVN DGEETFSEVR DCGPLPVMLQ SNRCHLHKMS PQELVEHKEE
     SDELGGYFIV NGIEKLIRML IVQRRNHPMA IIRPSFANRG TSYSHYGVQI RCVRPDQTSQ
     TNVLHYLNDG QVTFRFSWRK NEYLVPVVLI LKALTDASDR EIFDGIVGAD TSNSFLTDRL
     ELLLRGFKKR FPQLLNRRQV LQYLGDKFRV VLQASPDMSD YLVGQELLRR IVLVHLGDEN
     TDKSNMLMFM IRKLYSLVAG ECCPDNPDAT QHQEVLLGGF LYGMIVKEKI EEYLQNIKLQ
     IQADVNRGMP VDFKDRKYMT RVLTRINENI GSKLQYFLST GNLVSQSGLD LQQVSGYTVV
     AEKINFYRFI SHFRMVHRGS FFAQLKTTTV RKLLPESWGF LCPVHTPDGS PCGLLNHFAH
     KCKISTTQSD VSKIPTLLYS LGVSPAAHVT AAGPSLCCVQ LDGKIVGWCS HEQGRIVADT
     LRYWKVEGKT DGLPLDLEIG YVPASKRGQY PGLYLFGGHS RMMRPVRYLP LDKQDIVGPF
     EQVYMDIAVT PEEIQNNVHT HVEFSPTNIL SILANLTPFS DFNQSPRNMY QCQMGKQTMG
     TPGVALCHRS DNKLYRLQSG QTPIVKANLY DDYGMDNFPN GTNAVVAVIS YTGYDMDDAM
     IINKSADERG FSYGTVYKTE KIDLSLSRGR GDPVTQHFGF GTDEWPKEWL EKLDEDGLPI
     IGSYVEEGDP ICAYFDDTLN KTKIKTYHSS EPAYIEEVTL IGDESNKFQE LQYITIKYRI
     RRVPQIGDKF SSRHGQKGVC SRKWPTVDMP FSETGIQPDV IINPHAFPSR MTIGMFVESL
     AGKAGALHGI AQDATPWTFS EEDTPADYFG DQLLKAGYNY HGNEPMYSGA TGEELRADIY
     IGVVYYQRLR HMVNDKFQVR STGPVNSLTM QPVKGRKRHG GIRVGEMERD ALIGHGTSFL
     LQDRLLNSSD YTQSAVCREC GSILTTQSSV PKIGSMVTIR CRRCAISFDE AKKIITQQDS
     EDSIFIDDSH IWEDGQGNKF VGGGNTTTVA IPFVLKYLDS ELAAMGIRLR YNVDPK