ID   RPA2_DICDI              Reviewed;        1130 AA.
AC   Q54BM1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=polr1b; Synonyms=rpa2; ORFNames=DDB_G0293560;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- MISCELLANEOUS: Three distinct zinc-containing RNA polymerases are found
CC       in eukaryotic nuclei: polymerase I for the ribosomal RNA precursor,
CC       polymerase II for the mRNA precursor, and polymerase III for 5S and
CC       tRNA genes.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000218; EAL60592.1; -; Genomic_DNA.
DR   RefSeq; XP_629008.1; XM_629006.1.
DR   AlphaFoldDB; Q54BM1; -.
DR   SMR; Q54BM1; -.
DR   STRING; 44689.DDB0216278; -.
DR   PaxDb; Q54BM1; -.
DR   PRIDE; Q54BM1; -.
DR   EnsemblProtists; EAL60592; EAL60592; DDB_G0293560.
DR   GeneID; 8629292; -.
DR   KEGG; ddi:DDB_G0293560; -.
DR   dictyBase; DDB_G0293560; rpa2.
DR   eggNOG; KOG0216; Eukaryota.
DR   HOGENOM; CLU_000524_5_1_1; -.
DR   InParanoid; Q54BM1; -.
DR   OMA; FFGVVHY; -.
DR   PhylomeDB; Q54BM1; -.
DR   Reactome; R-DDI-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-DDI-73772; RNA Polymerase I Promoter Escape.
DR   PRO; PR:Q54BM1; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005730; C:nucleolus; ISS:dictyBase.
DR   GO; GO:0005736; C:RNA polymerase I complex; ISS:dictyBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISS:dictyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; ISS:dictyBase.
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; Phosphoprotein; Reference proteome; Transcription; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1130
FT                   /note="DNA-directed RNA polymerase I subunit rpa2"
FT                   /id="PRO_0000327638"
FT   ZN_FING         1070..1096
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P22138"
SQ   SEQUENCE   1130 AA;  128285 MW;  A5DA000C3AEFBA9B CRC64;
     MSEELKSLIQ PHIDSFDFFT DHGIDLVLKD SEPLYFEHNS TQYKIRFTDL KLSRPTRNIV
     EKEIKLYPNE SRETGTTYNA PFKGAIGLYE VNEMDEMDDG TEVDYNKQEP THTFEVDLGR
     LPIMVKSRYC HLNGMSPEKL IESREEELEQ GGYFIVNGNE KVVRMLVMTK ANHPVALHRK
     AWTNRGPGYT KNGITIRCVR PDRSSITNNL HYINDGQTTL RFLYRRQEFF LPATLLLKAL
     KDTTEKEIYE NIVQGDNENT FLTDRVELSL REQKINNINT QEEVLDYIGS RFRARTQFPP
     SFSNIKIGRW FINQFVFVHL PNYNDKYNLL ILMIQKLYAM VGGKCGTDNI DSPAFQEVLL
     AGHIYGMILK EKLTEYLEST KSFVLKSFED KKKSGDKLPD ALKKVLDKNF KIADRFSYFL
     ATGNLRSSSG IDLQQTSGFC VIADKLNFLR FISHFRSIHR GAFFATMKTT AIRKLMPESW
     GFFCPVHTPD GAPCGLLNHL SSNCLVTVDA AQDPTVQKAQ TLLPSFLAAH GMLPIDMVSV
     YQHQYLTITL DGRVLGKIEP KAGEEMVKML RYLRSMGNEP SIPKTMEISY APPTNVENGQ
     YSGISLFTTG ARFMRPVVNL TSGQNELIGP QEQLYMEIAV VPHEVIKGVT THIETSPTAM
     FSLLANLTPF SDYNQSPRNM YQCQMAKQTM GTPLHSYPFR TDNKLYKVQN VQKPIVHTKN
     QFKFRCNDYP HGCNAVIAVI SNTGYDMEDA MIINKSAYER GFGHGSVYKN EYIDLDQGLS
     RFEQKKTFFG RPNTVVDELD KFIDTDGLPF VGRLIKPGEP YYTYIRPSDG RQVTKDYKGK
     EEAYIEDVRI IFGPNGATRD PSKINNICVK LRFNRNPVIG DKFSSRHGQK GVLSQLWPEI
     NMPFTESGMK PDVIINPNAF PSRMTIGMLV EILAGKAGAI HGKFQDATAF QFDENNTAID
     FFGEQLAKAG FNRFGNEQMY SGTTGKEFEC EIFFGVCYYQ RLRHMVKDKY QVRALGKVNA
     LTRQPIKGRK VGGGIRFGEM ERDSLLAHGA SFCLNDRLMK SSDFAKIKVC KLCGSTLTIY
     SKKDYSNQTV SECKSCKSSD SIATISIPYV FTYLVAELAA VNITMKLQVS