ID   RPA2_RAT                Reviewed;        1135 AA.
AC   O54888;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=DNA-directed RNA polymerase I subunit RPA2;
DE            Short=RNA polymerase I subunit 2;
DE            EC=2.7.7.6 {ECO:0000305|PubMed:9422795};
DE   AltName: Full=A127;
DE   AltName: Full=RPA135;
GN   Name=Polr1b; Synonyms=Rpa2, Rpo1-2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE RNA POL I COMPLEX,
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9422795; DOI=10.1074/jbc.273.2.1257;
RA   Hannan R.D., Hempel W.M., Cavanaugh A., Arino T., Dimitrov S.I., Moss T.,
RA   Rothblum L.;
RT   "Affinity purification of mammalian RNA polymerase I. Identification of an
RT   associated kinase.";
RL   J. Biol. Chem. 273:1257-1267(1998).
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.
CC       {ECO:0000305|PubMed:9422795}.
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:0000305|PubMed:9422795};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC         Evidence={ECO:0000305|PubMed:9422795};
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC       of at least 13 subunits. {ECO:0000269|PubMed:9422795}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9H9Y6}. Chromosome
CC       {ECO:0000250|UniProtKB:P70700}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; AF025424; AAB94600.1; -; mRNA.
DR   PIR; T42368; T42368.
DR   RefSeq; NP_113961.1; NM_031773.1.
DR   STRING; 10116.ENSRNOP00000024882; -.
DR   iPTMnet; O54888; -.
DR   PhosphoSitePlus; O54888; -.
DR   jPOST; O54888; -.
DR   PaxDb; O54888; -.
DR   PRIDE; O54888; -.
DR   GeneID; 83582; -.
DR   KEGG; rno:83582; -.
DR   UCSC; RGD:620822; rat.
DR   CTD; 84172; -.
DR   RGD; 620822; Polr1b.
DR   eggNOG; KOG0216; Eukaryota.
DR   InParanoid; O54888; -.
DR   OrthoDB; 42570at2759; -.
DR   PhylomeDB; O54888; -.
DR   Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR   PRO; PR:O54888; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005736; C:RNA polymerase I complex; IDA:RGD.
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:0007566; P:embryo implantation; ISO:RGD.
DR   GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR   GO; GO:0017126; P:nucleologenesis; ISO:RGD.
DR   GO; GO:0009303; P:rRNA transcription; IDA:RGD.
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   PANTHER; PTHR20856; PTHR20856; 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   1: Evidence at protein level;
KW   Chromosome; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1135
FT                   /note="DNA-directed RNA polymerase I subunit RPA2"
FT                   /id="PRO_0000048074"
FT   ZN_FING         1070..1101
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P22138"
FT   MOD_RES         1051
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9Y6"
SQ   SEQUENCE   1135 AA;  127721 MW;  0A46D3FE9079A3E3 CRC64;
     MDVDSRWRNL PSGPSLKHLT DPSYAVPPEQ QKAALQDLTR AHVDSFNYAV LEGLSHAVQA
     IPPFEFAFKD ERISLTIVDA AISPPAVPKG TICKELNIYP AECRGRRSTY RGKLTADISW
     AVNGVPKGII KQFLGXVPIM VKSKLCNLYN LPPQVLIEHH EEAEEMGGYF IINGIEKVIR
     MLIMPRRNFP IAMIRPKWKS RGLGYTQFGV SIHCVREEHS AVNMNLHYVE NGTVMLNFIY
     RKELFFLPLG FALKALVSFS DYQIFQELIK GKEEDSFFKN SVSQMLRIVM EEGCHTQKQV
     LDYLGERFRV KLSLPDWYPN AEAAEFLFNQ CICIHLKSNT DKFYLLCLMT RKLFALARGE
     CMEDNPDSLV NQEVLTPGQL FLMFLKEKME NWLLSIKIAL DKRAQKTNVS INNENLMKIF
     SMGTELTRPF EYLLATGNLR SKTGLGFMQD SGLCVVADKL NFIRYLSHFR CVHRGADFAK
     MRTTTVRKLL PESWGFLCPV HTPDGAPCGL LNHLTAVCEV VTKFVYTASI PALLCGLGVT
     PVDAAPCRPY SDCYPVLLDG VMVGWVDKEL APEVADTLRR FKVLRERRCS SLDGGGPDSH
     DRKAKPVPRA VPLHHSLQAG EACAEPGAGQ RRARWNYGAA LHEHCHLRGR GFWWSFHTPG
     ALPSQPAEVI ANFIPFSDHN QSPRNMYQCQ MGKQTMGFPL LTYQDRSDNK LYRLQTPQSP
     LVRPCMYDHY DMDNYPIGTN AIVAVISYTG YDMEDAMIVN KASWERGFAH GSVYKSEFID
     LSEKFKQGDD SLVFGVKPGD PRVMQKLDND GLPFIGAKLE FGDPYYGYLN LNTGEGFVVY
     YKSKENCVVD NIKVCSNDTG SGKFKCVCVT VRVPRNPTIG DKFASRHGQK GILSRLWPAE
     DMPFTESGMM PDILFNPHGF PSRMTIGMLI ESMAGKSAAL HGLCHDATPF IFSEENSALE
     YFGEMLKAAG YNFYGTERLY SGISGMELEA DIFIGVVYYQ RLRHMVSDKF QVRTTGARDK
     VTNQPIGGRN VQGGIRFGEM ERDALLAHGT SFLLHDRLFN CSDRSVAHVC VKCGSLLSPL
     LEKPPPSWSA MRNRKYNCTV CGRSDSIDTV SVPYVFRYFV AELAAMNIKV KLDVI