RPB2_SOLLC
ID RPB2_SOLLC Reviewed; 1191 AA.
AC Q42877;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
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;
DE AltName: Full=DNA-directed RNA polymerase II 135 kDa polypeptide;
GN Name=RPB2;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Grosse lisse;
RX PubMed=8616257; DOI=10.1007/bf00020119;
RA Warrilow D., Symons R.H.;
RT "Sequence analysis of the second largest subunit of tomato RNA polymerase
RT II.";
RL Plant Mol. Biol. 30:337-342(1996).
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; U28403; AAC49273.1; -; mRNA.
DR PIR; S65068; S65068.
DR RefSeq; NP_001233889.1; NM_001246960.2.
DR AlphaFoldDB; Q42877; -.
DR SMR; Q42877; -.
DR STRING; 4081.Solyc02g078260.2.1; -.
DR PaxDb; Q42877; -.
DR PRIDE; Q42877; -.
DR EnsemblPlants; Solyc02g078260.3.1; Solyc02g078260.3.1; Solyc02g078260.3.
DR GeneID; 544278; -.
DR Gramene; Solyc02g078260.3.1; Solyc02g078260.3.1; Solyc02g078260.3.
DR KEGG; sly:544278; -.
DR eggNOG; KOG0214; Eukaryota.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; Q42877; -.
DR OMA; RDLHGTH; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; Q42877; -.
DR Proteomes; UP000004994; Chromosome 2.
DR ExpressionAtlas; Q42877; baseline and differential.
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..1191
FT /note="DNA-directed RNA polymerase II subunit RPB2"
FT /id="PRO_0000048082"
FT ZN_FING 1123..1144
FT /note="C4-type"
FT REGION 842..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 799
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with RPB1"
FT /evidence="ECO:0000250"
FT BINDING 1123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1191 AA; 135064 MW; 8F177640C072BCD2 CRC64;
MDMEDEYEPQ YNVDDDEEEI TQEDAWAVIS AYFEEKGLVR QQLDSFDEFI QNTMQEIVDE
SADIEIRPES QHNPGHQSDF AETIYKINFG QIYLSKPMMT ESDGETATLF PKAARLRNLT
YSAPLYVDVT KRVIKKGHDG EEVTETQDFT KVFIGKVPIM LRSSYCTLYQ NSEKDLTELG
ECPLDQGGYF IINGSEKVLI AQEKMSTNHV YVFKKRQPNK YAFVAEVRSM ADTQNRPPST
MFVRMLSRTS AKGGSSGQYI RATLPYIRTE IPIIIVFRAL GFVADKDILE HICYDFNDTQ
MMELLRPSLE EAFVIQNQQV ALDYIGKRGA TVGVTREKRI KYAKEILQKE MLPHVGVGEY
CETKKAYYFG YIIHRLLLCA LGRRAEDDRD HYGNKRLDLA GPLLGGLFRM LFRKLTRDVR
GYVQKCVDNG KDVNLQFAIK AKTITSGLKY SLATGNWGQA NAAGTRAGVS QVLNRLTYAS
TLSHLRRLNS PIGREGKLAK PRQLHNSQWG MMCPAETPEG QACGLVKNLA LMVYITVGSA
AYPILEFLEE WGTENFEEIS PAVIPQATKI FVNGTWVGIH RDPDMLVRTL RRLRRRVDVN
TEVGVVRDIR LKELRIYTDY GRCSRPLFIV EKQRLMIKKK DIQTLQQRES PDEGGWHDLV
AKGYIEYIDT EEEETTMISM TINDLVQARL NPGDAYSDTY THCEIHPSLI LGVCASIIPF
PDHNQSPRNT YQSAMGKQAM GIYVTNYQFR MDTLAYVLYY PQKPLVTTRA MEHLHFRQLP
AGINAIVAIS CYSGYNQEDS VIMNQSSIDR GFFRSLFFRS YRDEEKKMGT LVKEDFGRPD
RASTMGMRHG SYDKLDDDGL APPGTRVSGE DVIIGKTTPI SQDDAQGQAS RYTRKDHSTS
LRHSETGMVD QVLLTTNADG LRFVKVRVRS VRIPQIGDKF SSRHGQKGTV GMTYTQEDMP
WTVEGITPDI IVNPHAIPSR MTIGQLIECI MGKVAAHMGK EGDATPFTDV TVDNISKALH
KCGYQMRGFE TMYNGHTGRR LSAMIFLGPT YYQRLKHMVD DKIHSRGRGP VQILTRQPAE
GRSRDGGLRF GEMERDCMIA HGAAHFLKER LFDQSDAYRV HVCERCGLIA IANLKKNSFE
CRGCKNKTDI VQVHIPYACK LLFQELMAMA IAPRMLTKDV KLAKDQKKKG A
