RPA2_PONAB
ID RPA2_PONAB Reviewed; 1136 AA.
AC Q5REE8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
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:Q9H9Y6};
DE AltName: Full=RPA135;
GN Name=POLR1B;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9H9Y6}.
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:Q9H9Y6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC Evidence={ECO:0000250|UniProtKB:Q9H9Y6};
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000250|UniProtKB:Q9H9Y6}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR857581; CAH89859.1; -; mRNA.
DR RefSeq; NP_001128800.1; NM_001135328.1.
DR AlphaFoldDB; Q5REE8; -.
DR SMR; Q5REE8; -.
DR STRING; 9601.ENSPPYP00000013566; -.
DR GeneID; 100171727; -.
DR KEGG; pon:100171727; -.
DR CTD; 84172; -.
DR eggNOG; KOG0216; Eukaryota.
DR InParanoid; Q5REE8; -.
DR OrthoDB; 42570at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
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:0014029; P:neural crest formation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Chromosome; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1136
FT /note="DNA-directed RNA polymerase I subunit RPA2"
FT /id="PRO_0000230309"
FT ZN_FING 1071..1102
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P22138"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Y6"
SQ SEQUENCE 1136 AA; 128497 MW; 0ACF3C02941D300F CRC64;
MDPGSRWRNL PSGPSLKHLT DPSYGIPREQ QKAALQELTR AHVESFNYAV HEGLGLAVQA
IPPFEFAFKD ERISFTILDA VISPPTVPKG TICKEVSVYP AECRGRRCTY RGKLTADISW
AVNGISKGII KQFLGYVPIM VKSKLCNLYN LPPQALIEHH EEAEEMGGYF IINGIEKVIR
MLIMPRRNFP IAMVRPKWKT RGPGYTHYGV SMHCVREEHS AVNMNLHYLE NGTVMLNFIY
RKELFFLPLG FALKALVSFS DYQIFQELIK GKEDDSFLRN SVSQMLRIVM EEGCSTQKQV
LNYLGECFRV KLNVPDWYPN EQAAEFLFNQ CICIHLKSNT EKFYMLCLMT RKLFALAKGE
CMEDNPDSLV NQEVLTPGQL FLMFLKEKLE GWLVSIKIAF DKKAQKTNVS MNTDNLMRIF
TMGIDLTKPF EYLFATGNLR SKTGLGLLQD SGLCVVADKL NFIRYLSHFR CVHRGADFAK
MRTTTVRRLL PESWGFLCPV HTPDGEPCGL MNHLTAVCEV VTQFVYTASI PALLCNLGVT
PIDGAPHRSY SECYPVLLDG VMVGWVDKEL APGIADSLRH FKVLREKRIP PWTEVVLIPM
TGKPSLYPGL FLFTTPCRLV RPVQNLELGK EELIGTMEQI FMNVAIFEDE VFAGVTTHQE
LFPHSLLSVI ANFIPFSDHN QSPRNMYQCQ MGKQTMGFPL LTYQDRSDNK LYRLQTPQSP
LVRPSMYDYY DMDNYPIGTN AIVAVISYTG YDMEDAMIVN KASWERGFAH GSVYKSEFID
LSEKIKQGDS SLVFGMKPGD PRILQKLDDD GLPFIGAKLQ YGDPYYSYLN LNTGESFVMY
YKSKENCVVD NIKVCSNDTG SGKFKCVCIT MRVPRNPTIG DKFASRHGQK GILSRLWPAE
DMPFTESGMV PDILFNPHGF PSRMTIGMLI ESMAGKSAAL HGLCHDATPF IFSEENSALE
YFGEMLKAAG YNFYGTERLY SGISGLELEA DIFIGVVYYQ RLRHMVSDKF QVRTTGARDR
VTNQPIGGRN VQGGIRFGEM ERDALLAHGT SFFLLHDRLF NCSDRSVAHV CVKCGSLLSP
LLEKPPPSWS AMRNRKYNCT LCNRSDTIDT VSVPYVFRYF VAELAAMNIK VKLDVV
