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 16-JUN-2009, entry version 61. DE RecName: Full=DNA-directed RNA polymerase II subunit RPB2; DE Short=RNA polymerase II subunit B2; DE Short=RNA polymerase II subunit 2; 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; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; OC Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Grosse lisse; RX MEDLINE=96178872; PubMed=8616257; DOI=10.1007/BF00020119; RA Warrilow D., Symons R.H.; RT "Sequence analysis of the second largest subunit of tomato RNA RT polymerase II."; RL Plant Mol. Biol. 30:337-342(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. Second largest component of RNA polymerase II which CC synthesizes mRNA precursors and many functional non-coding RNAs. CC Proposed to contribute to the polymerase catalytic activity and CC forms the polymerase active center together with the largest CC subunit. Pol II is the central component of the basal RNA CC polymerase II transcription machinery. It is composed of mobile CC elements that move relative to each other. RPB2 is part of the CC core element with the central large cleft, the clamp element that CC moves to open and close the cleft and the jaws that are thought to CC grab the incoming DNA template (By similarity). CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex CC consisting of 12 subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the CC RNA polymerase II transcribing complex probably involves a two- CC step mechanism. The initial binding seems to occur at the entry CC (E) site and involves a magnesium ion coordinated by three CC conserved aspartate residues of the two largest RNA Pol II CC subunits (By similarity). CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U28403; AAC49273.1; -; mRNA. DR PIR; S65068; S65068. DR UniGene; Les.86; -. DR HSSP; P08518; 1I50. DR BRENDA; 2.7.7.6; 281054. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNA_pol_su2_6. 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 PANTHER; PTHR20856; RNA_pol_I_sub2; 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; Transcription; Transferase; Zinc; KW Zinc-finger. FT CHAIN 1 1191 DNA-directed RNA polymerase II subunit FT RPB2. FT /FTId=PRO_0000048082. FT ZN_FING 1123 1144 C4-type. FT COMPBIAS 14 19 Asp/Glu-rich (acidic). FT METAL 799 799 Magnesium; shared with RPB1 (By FT similarity). FT METAL 1123 1123 Zinc (By similarity). FT METAL 1126 1126 Zinc (By similarity). FT METAL 1141 1141 Zinc (By similarity). FT METAL 1144 1144 Zinc (By similarity). 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 //