RPB2_CAEEL
ID RPB2_CAEEL Reviewed; 1193 AA.
AC Q10578;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB2;
DE Short=RNA polymerase II subunit 2;
DE Short=RNA polymerase II subunit B2;
DE EC=2.7.7.6;
GN Name=rpb-2; ORFNames=C26E6.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 200-1058.
RX PubMed=7953533; DOI=10.1016/s0960-9822(00)00131-7;
RA Sidow A., Thomas W.K.;
RT "A molecular evolutionary framework for eukaryotic model organisms.";
RL Curr. Biol. 4:596-603(1994).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Second largest component of RNA polymerase II which synthesizes mRNA
CC precursors and many functional non-coding RNAs. Proposed to contribute
CC to the polymerase catalytic activity and forms the polymerase active
CC center together with the largest subunit. Pol II is the central
CC component of the basal RNA polymerase II transcription machinery. It is
CC composed of mobile elements that move relative to each other. RPB2 is
CC part of the core element with the central large cleft, the clamp
CC element that moves to open and close the cleft and the jaws that are
CC thought to grab the incoming DNA template (By similarity).
CC {ECO:0000250}.
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;
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA
CC polymerase II transcribing complex probably involves a two-step
CC mechanism. The initial binding seems to occur at the entry (E) site and
CC involves a magnesium ion coordinated by three conserved aspartate
CC residues of the two largest RNA Pol II subunits (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; FO080680; CCD65728.1; -; Genomic_DNA.
DR EMBL; U10333; AAA50224.1; -; mRNA.
DR PIR; E88445; E88445.
DR PIR; T43701; T43701.
DR RefSeq; NP_498047.1; NM_065646.4.
DR AlphaFoldDB; Q10578; -.
DR SMR; Q10578; -.
DR BioGRID; 40901; 24.
DR STRING; 6239.C26E6.4; -.
DR iPTMnet; Q10578; -.
DR EPD; Q10578; -.
DR PaxDb; Q10578; -.
DR PeptideAtlas; Q10578; -.
DR PRIDE; Q10578; -.
DR EnsemblMetazoa; C26E6.4.1; C26E6.4.1; WBGene00016140.
DR GeneID; 175668; -.
DR KEGG; cel:CELE_C26E6.4; -.
DR CTD; 175668; -.
DR WormBase; C26E6.4; CE52920; WBGene00016140; rpb-2.
DR eggNOG; KOG0214; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_2_1; -.
DR InParanoid; Q10578; -.
DR OMA; RDLHGTH; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; Q10578; -.
DR Reactome; R-CEL-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-CEL-113418; Formation of the Early Elongation Complex.
DR Reactome; R-CEL-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-CEL-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-CEL-6782135; Dual incision in TC-NER.
DR Reactome; R-CEL-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-CEL-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-CEL-6803529; FGFR2 alternative splicing.
DR Reactome; R-CEL-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-CEL-72086; mRNA Capping.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-CEL-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-CEL-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-CEL-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-CEL-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-CEL-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-CEL-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-CEL-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q10578; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00016140; Expressed in embryo and 4 other tissues.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
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: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; 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 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; 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 PROSITE; PS01166; RNA_POL_BETA; 1.
PE 2: Evidence at transcript level;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1193
FT /note="DNA-directed RNA polymerase II subunit RPB2"
FT /id="PRO_0000048083"
FT ZN_FING 1125..1146
FT /note="C4-type"
FT BINDING 798
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with RPB1"
FT /evidence="ECO:0000250"
FT BINDING 1125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1193 AA; 134905 MW; B8A85E74E9CC7EBE CRC64;
MYDDEDEMVN DPMDGDYIDD SDEISAEAWQ EACWVVISAY FDEKGLVRQQ LDSFDEFVQM
NVQRIVEDSP PVELQSENQH LGTDMENPAK FSLKFNQIYL SKPTHWEKDG APMPMMPNEA
RLRNLTYASP LYVDITKVVT RDDSATEKVY DKVFVGKVPV MLRSSYCMLS NMTDRDLTEL
NECPLDPGGY FVINGSEKVL IAQEKMATNT VYVFSMKDGK YAFKTECRSC LENSSRPTST
MWVNMLARGG GGGKKTAMGQ RIIGILPYIK QEIPIMIVFR ALGFVSDRDI LGHIIYDFND
PEMMEMVKPS LDEAFVIQEQ NVALNFIGAR GAKPGVTREQ RIKYAREILQ KELLPHVGVS
EHCETKKAFF IGYMVHRLLL AALGRRELDD RDHIGNKRLD LAGPLLAFLF RSLFRNLLKE
MRMTAQKYIN KNDDFALDVC VKTSTITRGL TYSLATGNWG DQKKAHQSRA GVSQVLNRLT
YTATLSHLRR ANSPIGREGK LAKPRQLHNT QWGMVCPAET PEGQAVGLVK NLALMAYISV
GSLPEPILEF LEEWSMENLE EVSPSAIADA TKIFVNGAWV GIHREPDQLM TTLKKLRRQM
DIIVSEVSMV RDIRDREIRI YTDAGRVCRP LLIVENQKLA LKKRHIDQLK EAADEANKYT
WSDLVGGGVV ELIDSMEEET SMIAMMPEDL RSGGYCDTHT HCEIHPAMIL GVCASIIPFP
DHNQSPRNTY QSAMGKQAMG VYTTNFHVRM DTLAHVLYYP QKPLVTTRSM EYLRFNELPA
GINAIVAILS YSGYNQEDSV IMNNSAIDRG LFRSVFYRSY RDNEANLDNA NEELIEKPTR
EKCSGMRHSL YDKLDEDGII SPGMRVSGDD VIIGKTVALP DIDDDLDASG KKYPKRDAST
FLRSSETGIV DQVMLSLNSD GNKFVKIRMR SVRLPQIGDK FASRHGQKGT MGIMYRQEDM
PFTAEGLTPD IIINPHAVPS RMTIGHLIEC LQGKLSANKG EIGDATPFND TVNVQKISGL
LCEYGYHLRG NEVMYNGHTG KKLTTQIFFG PTYYQRLKHM VDDKIHSRAR GPIQMMNRQP
MEGRARDGGL RFGEMERDCQ ISHGATQFLR ERLFEVSDPY HVYVCNNCGL IVVANLRTNS
FECKACRNKT QVSAVRIPYA CKLLFQELMS MSIAPRLMVK PRQSKRSKHQ SEA
