Reviewed, UniProtKB/Swiss-Prot Q42877 (RPB2_SOLLC)

Names and origin

Protein names

Recommended name:
    DNA-directed RNA polymerase II subunit RPB2
      Short name=RNA polymerase II subunit B2
      Short name=RNA polymerase II subunit 2
    EC=2.7.7.6
Alternative name(s):
    DNA-directed RNA polymerase II 135 kDa polypeptide

Gene names

Name:

RPB2

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	1191 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template By similarity.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits By similarity.
Subcellular location	Nucleus By similarity.
Miscellaneous	The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits By similarity.
Sequence similarities	Belongs to the RNA polymerase beta chain family.

Ontologies

Keywords
Biological process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Domain	Zinc-finger
Ligand	Magnesium Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Gene Ontology (GO)
Biological process	transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1191	1191	DNA-directed RNA polymerase II subunit RPB2		PRO_0000048082
Regions
	Zinc finger	1123 – 1144	22	C4-type
	Compositional bias	14 – 19	6	Asp/Glu-rich (acidic)
Sites
	Metal binding	799	1	Magnesium; shared with RPB1 By similarity
	Metal binding	1123	1	Zinc By similarity
	Metal binding	1126	1	Zinc By similarity
	Metal binding	1141	1	Zinc By similarity
	Metal binding	1144	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q42877-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8F177640C072BCD2	FASTA	1,191	135,064
	10 20 30 40 50 60 MDMEDEYEPQ YNVDDDEEEI TQEDAWAVIS AYFEEKGLVR QQLDSFDEFI QNTMQEIVDE 70 80 90 100 110 120 SADIEIRPES QHNPGHQSDF AETIYKINFG QIYLSKPMMT ESDGETATLF PKAARLRNLT 130 140 150 160 170 180 YSAPLYVDVT KRVIKKGHDG EEVTETQDFT KVFIGKVPIM LRSSYCTLYQ NSEKDLTELG 190 200 210 220 230 240 ECPLDQGGYF IINGSEKVLI AQEKMSTNHV YVFKKRQPNK YAFVAEVRSM ADTQNRPPST 250 260 270 280 290 300 MFVRMLSRTS AKGGSSGQYI RATLPYIRTE IPIIIVFRAL GFVADKDILE HICYDFNDTQ 310 320 330 340 350 360 MMELLRPSLE EAFVIQNQQV ALDYIGKRGA TVGVTREKRI KYAKEILQKE MLPHVGVGEY 370 380 390 400 410 420 CETKKAYYFG YIIHRLLLCA LGRRAEDDRD HYGNKRLDLA GPLLGGLFRM LFRKLTRDVR 430 440 450 460 470 480 GYVQKCVDNG KDVNLQFAIK AKTITSGLKY SLATGNWGQA NAAGTRAGVS QVLNRLTYAS 490 500 510 520 530 540 TLSHLRRLNS PIGREGKLAK PRQLHNSQWG MMCPAETPEG QACGLVKNLA LMVYITVGSA 550 560 570 580 590 600 AYPILEFLEE WGTENFEEIS PAVIPQATKI FVNGTWVGIH RDPDMLVRTL RRLRRRVDVN 610 620 630 640 650 660 TEVGVVRDIR LKELRIYTDY GRCSRPLFIV EKQRLMIKKK DIQTLQQRES PDEGGWHDLV 670 680 690 700 710 720 AKGYIEYIDT EEEETTMISM TINDLVQARL NPGDAYSDTY THCEIHPSLI LGVCASIIPF 730 740 750 760 770 780 PDHNQSPRNT YQSAMGKQAM GIYVTNYQFR MDTLAYVLYY PQKPLVTTRA MEHLHFRQLP 790 800 810 820 830 840 AGINAIVAIS CYSGYNQEDS VIMNQSSIDR GFFRSLFFRS YRDEEKKMGT LVKEDFGRPD 850 860 870 880 890 900 RASTMGMRHG SYDKLDDDGL APPGTRVSGE DVIIGKTTPI SQDDAQGQAS RYTRKDHSTS 910 920 930 940 950 960 LRHSETGMVD QVLLTTNADG LRFVKVRVRS VRIPQIGDKF SSRHGQKGTV GMTYTQEDMP 970 980 990 1000 1010 1020 WTVEGITPDI IVNPHAIPSR MTIGQLIECI MGKVAAHMGK EGDATPFTDV TVDNISKALH 1030 1040 1050 1060 1070 1080 KCGYQMRGFE TMYNGHTGRR LSAMIFLGPT YYQRLKHMVD DKIHSRGRGP VQILTRQPAE 1090 1100 1110 1120 1130 1140 GRSRDGGLRF GEMERDCMIA HGAAHFLKER LFDQSDAYRV HVCERCGLIA IANLKKNSFE 1150 1160 1170 1180 1190 CRGCKNKTDI VQVHIPYACK LLFQELMAMA IAPRMLTKDV KLAKDQKKKG A

References

[1]	"Sequence analysis of the second largest subunit of tomato RNA polymerase II." Warrilow D., Symons R.H. Plant Mol. Biol. 30:337-342(1996) [PubMed: 8616257] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Grosse lisse.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U28403 mRNA. Translation: AAC49273.1.
PIR	S65068.
UniGene	Les.86
3D structure databases
HSSP	HSSP built from PDB template 1I50 based on UniProtKB P08518.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.7.6. 281054.
Family and domain databases
InterPro	IPR015712. DNA-dir_RNA_pol_su2. IPR007120. DNA-dir_RNA_pol_su2_6. IPR007121. RNA_pol_bsu_CS. IPR007644. RNA_pol_bsu_protrusion. IPR007642. RNA_pol_Rpb2_2. IPR007645. RNA_pol_Rpb2_3. IPR007646. RNA_pol_Rpb2_4. IPR007647. RNA_pol_Rpb2_5. IPR007641. RNA_pol_Rpb2_7. [Graphical view]
PANTHER	PTHR20856. RNA_pol_I_sub2. 1 hit.
Pfam	PF04563. RNA_pol_Rpb2_1. 1 hit. PF04561. RNA_pol_Rpb2_2. 1 hit. PF04565. RNA_pol_Rpb2_3. 1 hit. PF04566. RNA_pol_Rpb2_4. 1 hit. PF04567. RNA_pol_Rpb2_5. 1 hit. PF00562. RNA_pol_Rpb2_6. 1 hit. PF04560. RNA_pol_Rpb2_7. 1 hit. [Graphical view]
PROSITE	PS01166. RNA_POL_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RPB2_SOLLC

Accession

Primary (citable) accession number: Q42877

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)