ID A0A2R9B535_PANPA Unreviewed; 1112 AA.
AC A0A2R9B535;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU363031};
GN Name=POLR3B {ECO:0000313|Ensembl:ENSPPAP00000024121.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000024121.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000024121.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000024121.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|RuleBase:RU363031}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC diphosphate; 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:0000256|ARBA:ARBA00047768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC Evidence={ECO:0000256|ARBA:ARBA00047768};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits: a ten-subunit catalytic core composed of
CC POLR3A/RPC1, POLR3B/RPC2, POLR1C/RPAC1, POLR1D/RPAC2, POLR3K/RPC10,
CC POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and
CC POLR2L/RPABC5; a mobile stalk composed of two subunits POLR3H/RPC8 and
CC CRCP/RPC9, protruding from the core and functioning primarily in
CC transcription initiation; and additional subunits homologous to general
CC transcription factors of the RNA polymerase II machinery, POLR3C/RPC3-
CC POLR3F/RPC6-POLR3G/RPC7 heterotrimer required for transcription
CC initiation and POLR3D/RPC4-POLR3E/RPC5 heterodimer involved in both
CC transcription initiation and termination.
CC {ECO:0000256|ARBA:ARBA00064375}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000256|ARBA:ARBA00006835, ECO:0000256|RuleBase:RU000434}.
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DR EMBL; AJFE02117029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02117030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02117031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02117032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02117033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02117034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02117035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9B535; -.
DR Ensembl; ENSPPAT00000046946.1; ENSPPAP00000024121.1; ENSPPAG00000035177.1.
DR GeneTree; ENSGT00950000183132; -.
DR Proteomes; UP000240080; Chromosome 12.
DR Bgee; ENSPPAG00000035177; Expressed in placenta and 6 other cell types or tissues.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR FunFam; 2.40.270.10:FF:000006; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 2.40.270.10:FF:000011; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 2.40.50.150:FF:000003; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000004; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1100.10:FF:000006; DNA-directed RNA polymerase subunit beta; 1.
DR FunFam; 3.90.1800.10:FF:000003; DNA-directed RNA polymerase subunit beta; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1100.10; -; 2.
DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1.
DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 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; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR NCBIfam; NF007175; PRK09606.1; 1.
DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 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; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU363031}; Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU363031}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU363031};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 38..412
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 186..363
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 438..502
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 539..594
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 600..632
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 647..1020
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 1022..1107
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
SQ SEQUENCE 1112 AA; 125396 MW; 70AE875D4AE9B18A CRC64;
MDVLAEEFGN LTPEQLAAPI PTVEEKWRLL PAFLKVKGLV KQHIDSFNYF INVEIKKIMK
ANEKVTSDAD PMWYLKYLNI YVGLPDVEES FNVTRPVSPH ECRLRDMTYS APITVDIEYT
RGSQRIIRNA LPIGRMPIML RSSNCVLTGK TPAEFAKLNE CPLDPGGYFI VKGVEKVILI
QEQLSKNRII VEADRKGAVG ASVTSSTHEK KSRTNMAVKQ GRFYLRHNTL SEDIPIVIIF
KAMGVESDQE IVQMIGTEEH VMAAFGPSLE ECQKAQIFTQ MQALKYIGNK VRRQRMWGGG
PKKTKIEEAR ELLASTILTH VPVKEFNFRA KCIYTAVMVR RVILAQGDNK VDDRDYYGNK
RLELAGQLLS LLFEDLFKKF NSEMKKIADQ VIPKQRAAQF DVVKHMRQDQ ITNGMVNAIS
TGNWSLKRFK MDRQGVTQVL SRLSYISALG MMTRISSQFE KTRKVSGPRS LQPSQWGMLC
PSDTPEGEAC GLVKNLALMT HITTDMEDGP IVKLASNLGV EDVNLLCGEE LSYPNVFLVF
LNGNILGVIR DHKKLVNTFR LMRRAGYINE FVSISTNLTD RCVYISSDGG RLCRYICRNF
EDFLHESLVE YLDVNEENDC NIALYEHTIN KDTTHLEIEP FTLLGVCAGL IPYPHHNQSP
RNTYQCAMGK QAMGTIGYNQ RNRIDTLMYL LAYPQKPMVK TKTIELIEFE KLPAGQNATV
AVMSYSGYDI EDALVLNKAS LDRGFGRCLV YKNAKCTLKR YTNQTFDKVM GPMLDAATRK
PIWRHEILDA DGICSPGEKV ENKQVLVNKS MPTVTQIPLE GSNVPQQPQY KDVPITYKGA
TDSYIEKVMI SSNAEDAFLI KMLLRQTRRP EIGDKFSSRH GQKGVCGLIV PQEDMPFCDS
GICPDIIMNP HGFPSRMTVG KLIELLAGKA GVLDGRFHYG TAFGGSKVKD VCEDLVRHGY
NYLGKDYVTS GITGEPLEAY IYFGPVYYQK LKHMVLDKMH ARARGPRAVL TRQPTEGRSR
DGGLRLGEME RDCLIGYGAS MLLLERLMIS SDAFEVDVCG QCGLLGYSGW CHYCKSSCHV
SSLRIPYACK LLFQELQSMN IIPRLKLSKY NE
//
